UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
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|---|---|---|
P0C9F0 | MVRLFYNPIKYLFYRRSCKKRLRKALKKLNFYHPPKECCQIYRLLENAPGGTYFITENMTNELIMIAKDPVDKKIKSVKLYLTGNYIKINQHYYINIYMYLMRYNQIYKYPLICFSKYSKIL | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 100 family. |
P0C9F1 | MVRLFHNPIKCLFYRGSRKTREKKLRKSLKKLNFYHPPGDCCQIYRLLENVPGGTYFITENMTNELIMIVKDSVDKKIKSVKLNFYGSYIKIHQHYYINIYMYLMRYTQIYKYPLICFNKYSYCNS | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 100 family. |
P0C9F2 | MVRLFRNPIKCIFYRRSRKIQEKKLRKSLKKLNFYHPPEDCCQIYRLLENVPGGTYFITENMTNDLIMVVKDSVDKKIKSIKLYLHGSYIKIHQHYYINIYMYLMRYTQIYKYPLICFNKYYNI | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 100 family. |
P0C9E9 | MVRLFRNPIKCIFYRRSRKIQEKKLRKSLKKLNFYHPPEDCCQIYRLLENVPGGTYFITENMTNDLIMVVKDSVDKKIKSIKLYLHGSYIKIHQHYYINIYMYLMRYTQIYKYPLICFNKYYNI | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 100 family. |
Q65209 | MGNKESKYLEMCSEEAWLNIPNIFKCIFIRKLFYNKWLKYQEKKLKKSLKLLSFYHPKKDFVGIRDMLHMAPGGSYFITDNITEEFLMLVVKHPEDGSAEFTKLCLKGSCIVIDGYYYDTLHIFLSETPDIYKYPLIRYDR | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. |
P0C9F4 | MGNKESKYLEMCSEEAWLNIPNIFKCIFIRKLFYNKWLKYQEKNLEKRLKLLSFYHPKKDFMGIRDMLDMAPGGSYFITDNVTEEFLMLVVKHPEDGSAEFTKLCLKGGCIVIDGFYYDDLHIFITENPNLYKYPLIHYDR | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. |
P0C9F5 | MGNKESKYLEMCSDEAWLNIPNVFKCIFIRKLFYNKWLKYQEKKLEKRLRLLSFYHAKKDFIGIRDMLQTAPGGSYFITDNITEEFLMLVLKHPEDGSAEFTKLCLKGSCIMIDGYYYDNLDIFLAESPDLYKYPLIRYDR | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. |
P0C9F6 | MGNKESRYLEMCSEEAWLNIPNIFKCIFIRKLFYNKWLKFQEKKLKKSLKLLSFYHPKKDFVGIRDMLQMAPGGSYFITDNITEEFLMLVVKHPEDGSAEFTKLCLKGSCIVIDGYYYDNLHIFISETPDIYKYPLIRYDR | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. |
P0C9F3 | MGNKESRYLEMCSEEAWLNIPNIFKCIFIRKLFYNKWLKYQEKKLKKSLKLLSFYHPKKDFVGIRDMLQMAPGGSYFITDNMTEEFLMLVVKHPEDGSAEFTKLCLKGSCIVIDGYYYDNLHIFISETPDIYKYPLIRYDR | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. |
Q65210 | MGNRLIRSYLPNTVMSIEDKQNKYNETIEDSKICNKVYIKQSGKIDKQELTRIKKLGFFYSQKSDHEIERMLFSMPNGTFLLTDDATNENIFIVQKDLENGSLNIAKLEFKGKALYINGKDYYSLENYLKTFEDFYKYPLIYNKNK | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. |
P0C9F8 | MGNHLDGSYLPNTVMSIEDKQNTYNEAKEDSKICNKIYIKQSGKIDKKELKRIKKLDFFYSQKNDDEIERMFMNKPNGTFLLTDDATDENLFLVQKDLENGSLNIAKLDFNGKALYINGKNYFSLENYLKTVEDFYKYPLIYDENK | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. |
P0C9F9 | MGNHLDGSYQPNMVMSIEDKQNKYNEAKERSKVCNKVYINQSGKIDKKELKRIKKLDFFYSQKNDDEIERMFFNMPNGTFLLTDDVTHENIYIAQKDLENGSLNIAKLEFKGEALYINGKNYFFLENYLKTFEDIYKYPLTNFNENK | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. |
P0C9G0 | MGNRLNGSYLSNTDMSIEDEQNKYNEAIEDCKICNKVYIKQSGKIDKKELNRIKKLDFFYSQKTDYEIERMFFNVPNGTFLLTDDATNENLFIAQKDLENGSLNIAKLEFKGKALYIDGKDYFSLENYLKTFEDFYKYPLIYNKNE | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. |
P0C9F7 | MGNRLNGSYLSNTDMSIEDKQNKYNEAIEDCKICNKVYIKQSGKIDKKELTRIKKLDFFYSQKSDHEIERMFFNVPNGTFLLTDDATNENLFIAQKDLENGSLNIAKLEFKGKALYIDGKDYFSLENYLKTFEDFYKYPLIYNKNE | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. |
Q4U9M9 | MKFLVLLFNILCLFPILGADELVMSPIPTTDVQPKVTFDINSEVSSGPLYLNPVEMAGVKYLQLQRQPGVQVHKVVEGDIVIWENEEMPLYTCAIVTQNEVPYMAYVELLEDPDLIFFLKEGDQWAPIPEDQYLARLQQLRQQIHTESFFSLNLSFQHENYKYEMVSSFQHSIKMVVFTPKNGHICKMVYDKNIRIFKALYNEYVTSVIGFFRGLKLLLLNIFVIDDRGMIGNKYFQLLDDKYAPISVQGYVATIPKLKDFAEPYHPIILDISDIDYVNFYLGDATYHDPGFKIVPKTPQCITKVVDGNEVIYESSNPSVECVYKVTYYDKKNESMLRLDLNHSPPSYTSYYAKREGVWVTSTYIDLEEKIEELQDHRSTELDVMFMSDKDLNVVPLTNGNLEYFMVTPKPHRDIIIVFDGSEVLWYYEGLENHLVCTWIYVTEGAPRLVHLRVKDRIPQNTDIYMVKFGEYWVRISKTQYTQEIKKLIKKSKKKLPSIEEEDSDKHGGPPKGPEPPTGPGHSSSESKEHEDSKESKEPKEHGSPKETKEGEVTKKPGPAKEHKPSKIPVYTKRPEFPKKSKSPKRPESPKSPKRPVSPQRPVSPKSPKRPESLDIPKSPKRPESPKSPKRPVSPQRPVSPRRPESPKSPKSPKSPKSPKVPFDPKFKEKLYDSYLDKAAKTKETVTLPPVLPTDESFTHTPIGEPTAEQPDDIEPIEESVFIKETGILTEEVKTEDIHSETGEPEEPKRPDSPTKHSPKPTGTHPSMPKKRRRSDGLALSTTDLESEAGRILRDPTGKIVTMKRSKSFDDLTTVREKEHMGAEIRKIVVDDDGTEADDEDTHPSKEKHLSTVRRRRPRPKKSSKSSKPRKPDSAFVPSIIFIFLVSLIVGIL | In microneme/rhoptry complexes. |
Q4N2B5 | MKFLILLFNILCLFPVLAADNHGVGPQGASGVDPITFDINSNQTGPAFLTAVEMAGVKYLQVQHGSNVNIHRLVEGNVVIWENASTPLYTGAIVTNNDGPYMAYVEVLGDPNLQFFIKSGDAWVTLSEHEYLAKLQEIRQAVHIESVFSLNMAFQLENNKYEVETHAKNGANMVTFIPRNGHICKMVYHKNVRIYKATGNDTVTSVVGFFRGLRLLLINVFSIDDNGMMSNRYFQHVDDKYVPISQKNYETGIVKLKDYKHAYHPVDLDIKDIDYTMFHLADATYHEPCFKIIPNTGFCITKLFDGDQVLYESFNPLIHCINEVHIYDRNNGSIICLHLNYSPPSYKAYLVLKDTGWEATTHPLLEEKIEELQDQRACELDVNFISDKDLYVAALTNADLNYTMVTPRPHRDVIRVSDGSEVLWYYEGLDNFLVCAWIYVSDGVASLVHLRIKDRIPANNDIYVLKGDLYWTRITKIQFTQEIKRLVKKSKKKLAPITEEDSDKHDEPPEGPGASGLPPKAPGDKEGSEGHKGPSKGSDSSKEGKKPGSGKKPGPAREHKPSKIPTLSKKPSGPKDPKHPRDPKEPRKSKSPRTASPTRRPSPKLPQLSKLPKSTSPRSPPPPTRPSSPERPEGTKIIKTSKPPSPKPPFDPSFKEKFYDDYSKAASRSKETKTTVVLDESFESILKETLPETPGTPFTTPRPVPPKRPRTPESPFEPPKDPDSPSTSPSEFFTPPESKRTRFHETPADTPLPDVTAELFKEPDVTAETKSPDEAMKRPRSPSEYEDTSPGDYPSLPMKRHRLERLRLTTTEMETDPGRMAKDASGKPVKLKRSKSFDDLTTVELAPEPKASRIVVDDEGTEADDEETHPPEERQKTEVRRRRPPKKPSKSPRPSKPKKPKKPDSAYIPSILAILVVSLIVGIL | In microneme/rhoptry complexes. Sporozoite antigen. |
P0C9H3 | MLVIFLGILGLLANQVLGLPTQAGGHLRSTDNPPQEELGYWCTYMESCKFCWECAHGICKNKVNTSMPLIIENSYLTSCEVSRWYNQCTYSEGNGHYHVMDCSDPVPHNRPHQLLRKIYEKEDL | Causes the redistribution of lumenal ER protein to an enlarged ERGIC compartment. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. |
A9JLI5 | MLVIFLGILGLLANQVLGLPTQAEGHLRSTDNPPQEELGYWCTYMESCKFCWECEHGICKNKVNRSMPWIIENSYLTSCEVSRWYNQCTYDEGNGHYHVMDCSNPVPHNRPHRLGRKIYEKEDL | Causes the redistribution of lumenal ER protein to an enlarged ERGIC compartment. Belongs to the asfivirus MGF 110 family. |
P0C9H0 | MLVVFFLGILGLLANQILGLPTQAGGHLRSTDNPPQEELGYWCTYMESCKFCWECAHGICKNKVNKSMPLIIENSYLTSCEVSRWYNQCTYSEGNGHYHVMDCSDPVPHNRPHQLLKKIYEKEDL | Causes the redistribution of lumenal ER protein to an enlarged ERGIC compartment. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. |
P18557 | MLVIFLGILGLLANQVSSQLVGQLHPTENPSENELEYWCTYMECCQFCWDCQNGLCVNKLGNTTILENEYVHPCIVSRWLNK | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. |
P26705 | MLVIFLGILGLLANQVSSQLVGQLHSTENPSENELEYWCTYMECCQFCWDCQNGLCVHKLGNTTILENEYVHPCIVSRWLNKCMYDLGQGIDHVMVCSQPKHWNPYKILKKEWKENNSQNI | Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. |
P0C9H5 | MLVIFLGILGLLANQVSSQLVGQLHPTENPSENELEYWCTYMECCQFCWDCQDGLCVNKLGNTTILENEYVHPCIVSRWLNKCMYDLGQGIDHVMVCSQPKYWNPYKILKKEWKENNSQN | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. |
P0C9H6 | MLVIFLGILGLLANQVSSQLVGQLHPTENPSENELEYWCTYMECCQFCWDCQNGLCVNKLGNTTILENEYVHPCIVSRWLNKCMYDLGQGIDHVMVCSQPKYWNPYKILKKEWKENNSQNK | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. |
A9JLI7 | MLVIILGVIGLLANQVLGLPTQAGGHLRSTDNPPQEELGYWCTYMESCKFCWECAHGICKNKVNESMPLIIENSYLTSCEVSRWYNQCTYSEGNGHYHVMDCSDPVPHNRPHRLLMKIYEKEDL | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 110 family. |
P0C9H4 | MLVIFLGILGLLANQVSSQLVGQLHPTENPSENELEYWCTYMECCQFCWDCQNGLCVNKLGNTTILENEYVHPCIVSRWLNKCMYDLGQGIDHVMVCSQPKYWNPYKILKKEWKENNSQNK | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. |
P18556 | MLVIFLGILGLLASQVSSQLVGQLRPTEDPPEEELEYWCAYMESCQFCWDCQDGTCINKIDGSAIYKNEYVKACLVSRWLDKCMYDLDKGIYHTMNCSQPWSWNPYKYFRKEWKKDEL | Expressed in the early phase of the viral replicative cycle. N-glycosylated. Belongs to the asfivirus MGF 110 family. |
P0C9H8 | MLVIFLGILGLMASQVLGLPSNQPTGQLRPTEDPPEEELEYWCAYMESCQFCWDCQDGNCINKIDGSVIYKNEFVRPCSVSRWMDKCMYDLNKGIYHTMNCSQPQSWNPYKYFRKEWKKDEL | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. N-glycosylated. Belongs to the asfivirus MGF 110 family. |
P0C9H9 | MLVTFLGILGLLASQVSSQLVGQLRPTEDPPEEELEYWCAYMESCQFCWDCQDGNCINKIDGSVIYKNEYVRPCSVSRSMDKCMYDLNKGIYHSMSCSDPKAWNPYKYFRKEWKKDEL | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. N-glycosylated. Belongs to the asfivirus MGF 110 family. |
P0C9I0 | MLVIFLGILGLLASQVSSQLVGQLRPTEDPPEEELEYWCAYMESCQFCWDCQDGTCINKIDGSVIYKNEYVKSCLVSRWLDKCMYDLDKGIYHTMNCSQPWSWNPYKYFRKEWKKDEL | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. N-glycosylated. Belongs to the asfivirus MGF 110 family. |
P0C9H7 | MLVIFLGILGLLASQVSSQLVGQLRPTEDPPEEELEYWCAYMESCQFCWDCQDGTCINKIDGSVIYKNEYVKSCLVSRWLDKCMYDLDKGIYHTMNCSQPWSWNPYKYFRKEWKKDEL | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. N-glycosylated. Belongs to the asfivirus MGF 110 family. |
P0C9I2 | MLVIILGVIGLLASSNLVSSSTSTRVGGHLPLTFDPPENELGYWCTYVESCRFCWDCEDGVCTSRIWGNNSTSIVENSYIKYCEVSRWGDQCRYDVEEHIYYTMNCSDPKPWNPYKIARKEWKKNEHFRKDLKKDEF | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 110 family. |
P26709 | MLVIILGVIGLLASSNLVSSSTSTRVGGHLPLTFDPPENELGYWCTYVESCRFCWDCEDGICTSRVWGNNSTSIIENDYVKYCEVSRWGDLCRYDVEEHIYHSMNCSDPKPWNPYKIARKEWKKDKHFRKELKKDEF | Belongs to the asfaviruses V110 family. |
P0C9I3 | MLVIILGVIGLLASSNLVSSSTSTRVGGHLPLTFDPPENELGYWYTYVESCRFCWDCEDGVCTSRVWGNNSTSIVENDYVKYCEVSRWGDQCRYDVEEHIYYTMNCSDPKPWNPYKIAKEGVEKG | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 110 family. |
P0C9I4 | MLVIILGIIGLLASSNLVSSSTSTRVGGHLPLTFDPPENELGYWCTYVESCRFCWDCEDGICTSRVWGNNSTSIVENDYVKYCEVSRWGNLCRYDVEEHIYYSMNCSDPKPWNPYKIARKEWKKNEYLRKDLKKDEF | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 110 family. |
P0C9I1 | MLVIILGIIGLLASSNLVSSSTSTRVGGHLPLTFDPPENELGYWCTYVESCRFCWDCEDGICTSRVWGNNSTSIVENDYVKYCEVSRWGNLCRYDVEEHIYHSMNCSDPKPWNPYKIARKEWKKNEHPRKDLKKDEF | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 110 family. |
O96436 | MIEDIKTLREEHVYRAKLAEQAERYDEMAEAMKNLVENCLDQNNSPPGAKGDELTVEERNLLSVAYKNAVGARRASWRIISSVEQKEANRNHMANKALAASYRQKVENELNKICQEILTLLTDKLLPRTTDSESRVFYFKMKGDYYRYISEFSNEEGKKASAEQAEESYKRATDTAEAELPSTHPIRLGLALNYSVFYYEILNQPQKACEMAKLAFDDAITEFDSVSEDSYKDSTLIMQLLRDNLTLWTSDLQTQEQQQQPVGEGAEAPKVEATEQQ | Belongs to the 14-3-3 family. |
Q8SW28 | MASKQYEEALQKANLSDMAERYDDMAKEMRLAVTLAHEDKHILNVMARNLFSVAYKNLVSSRRSSWRMLCSERQKLEGKDPSVVHVINEKIKVVEEELLRFCDEVLDIITTYILSLEEAQKNIEYNIFFLKMKGDYYRYKAEVVTGPEHSEVSKHAAESYKEATEKAKTLPPTNPIKLGLALNYSVFHYEILNDSEKACSIAKGAFDEAIKELDTLSEEHYRDSTLIMQLLRDNLTLWTSREEGNVMGDEGKGDPDEN | Expressed in late sporogonial stages. Belongs to the 14-3-3 family. |
Q39757 | MASRDDLVYMAKLAEQAERFDEMVDHMKAVAQQPKELSVEERNLLSVAYKNVIGSRRASWRVISSIEGKDTVSDQLPLIRDYKSKIETELTDICADILKIIEAELIPNSTSEEGKVFYYKMKGDYHRYLAEFQSADERKTSASDALDAYQLASDHANQDLPPTHPIRLGLALNFSVFYYEILNSPDRACGLAKAAFDDAIAELDTLSEESYKDSTLIIMQLLRDNLTLWTSDQGEAEEAPGNADGTVVEDL | Belongs to the 14-3-3 family. |
E2RU97 | MAEAFTREDYVFMAQLNENAERYDEMVETMRKISGMEGELSDKERNLLSVAYKNVIGPRRAAWRIVSSIEAKEKGRQKPNAKRIEQIRVYRQKIEKELSDICNDILKLLQEQFVPRSTNADAKVFYYKMQGDYYRYLAEYSSGEDKEKIAGSALNAYNSAFEISQQLPPTHPIRLGLALNFSVFYYEILASPDRACELARKAFDAAITDLDKLTEESYKDSTLIMQLLRDNLNLWVTDSAGDDNAEEK | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Binds with varying affinity to various synthetic phosphopeptides having a consensus binding motif RSX(pS/pT)XP, called mode-1, where X is any residue and pS/pT is a phosphorylated serine/threonine, and to synthetic phosphopeptides having a consensus binding motif Xp(S/T)X1-2-COOH, called mode-3, in which the phosphorylated residue occupies the penultimate C-terminal position in the target protein, but does not bind to their unphosphorylated counterparts (PubMed:19733174). Binds to synthetic human RAF1 phosphopeptides, but not to their unphosphorylated forms. Binds to difopein, a polypeptide containing a phosphorylation-independent binding motif (PubMed:16368691, PubMed:19733174). Involved in encystation (PubMed:19733174). Involved in cell proliferation. Required for actin and tubulin cytoskeletal organization. Regulates actin filament formation and nuclear size (PubMed:28932813). Homodimer (PubMed:16368691, PubMed:24658679, PubMed:28932813, PubMed:26551337, PubMed:22452640). Homodimerizes via N-terminal domains (PubMed:24658679, PubMed:26551337). Oligomerizes forming homotrimers, homotetramers and protein filaments. Oligomerization is hindered by polyglycylation in vivo (PubMed:24658679). Interacts with a large number of both cytosolic and membrane proteins in trophozoites and encysting parasites (PubMed:16368691, PubMed:22452640). Interacts with a serine/threonine protein kinase GL50803_112076 (gCDC7). Component of a multiprotein complex containing gCDC7 and GL50803_94117 (gDBF4), a regulatory subunit of gCDC7, during both the trophozoite and encysting stages of the parasite. Interacts with fructose-bisphosphate aldolase GL50803_11043 (gFBA), pyruvate kinase GL50803_17143 (gPyk), acetyl-CoA synthetase GL50803_13608 (gACS), protein kinase GL50803_22165 (gSTE), DEAD box RNA helicase GL50803_34684 (gVASA) and Golgi/cell cycle associated protein GL50803_17472 (gGCCA) (PubMed:22452640). Interacts with actin (PubMed:24728194, PubMed:28932813). Interacts with both monomeric phosphorylated and unphosphorylated actin. The interaction is enhanced by phosphorylation of actin and inhibited by Rho GTPase Rac (PubMed:28932813). In trophozoites and cysts, localizes intensely in the cytoplasm. Not detected in the central area of the cell corresponding to the median body nor in flagella. Detected in the nuclei of the encysting cells. Nuclear localization increases during the transition of cells from the early to the late encysting stage. Does not localize to the encystation-specific vesicles of the encysting cells (PubMed:16368691, PubMed:19733174). In interphase cells, detected throughout the cell with somewhat enriched at the cortex and perinuclear region. Associates with the intracytoplasmic axonemes of all flagella, but it is most apparent in the anterior flagella of interphase cells. Localizes also to the nuclear envelope/endoplasmic reticulum and to the microtubule bare area of the ventral disc during interphase. In mitotic cells, disassociates from the intracytoplasmic axonemes and localizes around the spindle. During cytokinesis, localizes with the ingressing furrow, which does not utilize a contractile ring (PubMed:28932813). Does no colocalize with F-actin (PubMed:24728194, PubMed:28932813). Expressed during excystation, the differentiation from cyst to trophozoite (at protein level) (PubMed:19861170). Expressed in trophozoites (at protein level) (PubMed:24658679, PubMed:19733174, PubMed:24147113, PubMed:24728194, PubMed:28932813, PubMed:22452640, PubMed:23058231, PubMed:21135098). Highly expressed during encystation stage, the differentiation from trophozoite to cyst (at protein level) (PubMed:24658679, PubMed:19733174, PubMed:24147113, PubMed:22452640). Expressed in feces extracted cysts (at protein level) (PubMed:19861170, PubMed:23058231). Expression in them is significantly lower than in trophozoites (at protein level) (PubMed:23058231). Constitutively expressed throughout the life cycle (PubMed:16368691). By encystation. Phosphorylated constitutively throughout the life cycle. Phosphorylation is very high in trophozoites and encysting cells of 12 hours (PubMed:16368691). Phosphorylated during excystation (PubMed:19861170). Phosphorylation promotes its binding to various target proteins and is critical for encystation process. Phosphorylation modification is not influenced by polyglycylation modification (PubMed:19733174). Polyglycylated on a glutamate residue, resulting in polyglycine chain on the gamma-carboxyl group (PubMed:16368691, PubMed:24658679, PubMed:19733174, PubMed:24147113, PubMed:21135098). Polyglycylated by the tubulin--tyrosine ligase-like protein GL50803_8456 (gTTLL3). The polyglycine chain is shortened by metallopeptidases of the M20 family, namely dipeptidases GL50803_15832 (gDIP1) and GL50803_8407 (gDIP2) (PubMed:21135098). The length of the polyglycine chain is developmental stage-dependent. In trophozoites, glycine residues range from 10 to 31, with the greatest occurrence of 21 residues. In 12 hour encystation stage, glycine residues range from 6 to 22, with the greatest occurrence of 10 residues. The differential rate of polyglycylation/deglycylation during the encystation process regulates the intracellular localization of this protein. Relocalizes partially from the cytoplasm inside the nuclei following the shortening of the polyglycine chain in encysting cells (PubMed:16368691, PubMed:19733174). Polyglycylation modification is not influenced by phosphorylation modification (PubMed:19733174). Polyglycylation prevents oligomerization in vivo (PubMed:24658679). Knockdown with morpholino results in dramatically reduced parasite growth, accumulation of multinucleate cells, abnormal flagellar positioning, and polarity and cytokinesis defects. Overall cytoplasmic actin organization is disrupted with ectopic short actin filaments, however, nuclei are enlarged with actin filaments covering the width of the nuclei. This protein may be used to design small molecules that inhibit its interactions with the target proteins. The inhibitors could be used as drugs to treat giardiasis, a disease caused by this parasite. Despite sequential and structural similarity, is not a functional ortholog of Drosophila 14-3-3 protein epsilon. Belongs to the 14-3-3 family. |
O65352 | MAAASSPREENVYLAKLAEQAERYEEMVEFMEKVVAAADGGEELTIEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEGHVSTIRDYRSKIESELSSICDGILKVLDSKLIGSASGGDSKVFYLKMKGDYYRYLAEFKTGDERKLAAENTLSAYKAAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEDSYKDSTLIMQLLRDNLTLWTSDMQDDTAEEVKEAPKPDDQ | Belongs to the 14-3-3 family. |
Q9SP07 | MSPAEPSREENVYMAKLAEQAERYEEMVEFMEKVARTVDTEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVALIKDYRGKIEAELSKICDGILKLLDSHLVPSSTAPESKVFYLKMKGDYHRYLAEFKSGAERKEAAESTLLAYKSAQDIALAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAISELDTLGEESYKDSTLIMQLLRDNLTLWTSDINEEAGDEIKEASKAVEGQ | Belongs to the 14-3-3 family. |
P93259 | MSSESSREENVYMAKLAEQAERYEEMVEFMEKVAKMTDTEELSVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVSTIKEYRGKIETELSKICDGILNLLESHLIPSASTAESKVFYLKMKGDYHRYLAEFKTGAERKEAAENTLLAYKSAQDIALAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAISELDTLGEESYKDSTLIMQLLRDNLTLWTSDNAEEGGDEIKEAAAKRESGEEKPQQ | Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes. Belongs to the 14-3-3 family. |
Q25538 | MAEEIKNLRDEYVYKAKLAEQAERYDEMAEAMKNLVENCLDEQQPKDELSVEERNLLSVAYKNAVGARRASWRIISSVEQKELSKQHMQNKALAAEYRQKVEEELNKICHDILQLLTDKLIPKTSDSESKVFYYKMKGDYYRYISEFSGEEGKKQAADQAQESYQKATETAEGHSPATHPIRLGLALNYSVFFYEILNLPQQACEMAKRAFDDAITEFDNVSEDSYKDSTLIMQLLRDNLTLWTSDLQADQQQQEGGEKPAEQADQ | Belongs to the 14-3-3 family. |
P29307 | MATAPSPREENVYLAKLAEQAERYEEMVEFMEKVCAAADSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNDDHVSTIRDYRSKIETELSNICGGILKLLDSRLIPSAASGDSKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLSAYKAAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLANEAFDEAIAELDTLEEESYKDSTLIMQLLRDNLTLWTSDMQDDGGDEIKEAAPKPDEQY | Belongs to the 14-3-3 family. |
P46266 | MAAAHTPREENVYMAKLAEQAERYEEMVEFMEKVSANADSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVAVIRDYRSKIESELSNICDGILKLLDTRLIPSASSGDSKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLTGYKSAQDIANAELPPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQDDGADEIKEAAPKADEQQ | Belongs to the 14-3-3 family. |
P84972 | LAEQAERYEEMVEFMEK | Is associated with a DNA binding complex to bind to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes. Belongs to the 14-3-3 family. |
P29308 | RNLLSVAYKNVVGARRASWRIISSIEQKEESRGNEDHVSVIRDYRSRIEKELSDNCDGILKLLDTKLVPAASSGDSKVFYLKMKGDYHRYLAEFKTGAQRKEAAESTLTAYKAAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFVEAIAELDTLGEDSYKDSTLIMQLLRDNLTLWTSDMQDEAADEITEEAAKQQKAVNNNKIAY | Belongs to the 14-3-3 family. |
Q41246 | MDKEREKQVYLARLAEQAERYDEMVEAMKTVAKMDVELTVEERNLVSVGYKNVIGARRASWRILSSIEQKEESKGHDQNVKRIKTYQQRVEDELTKYALTLSVIDEHVVPSSTSGESTVFYYKMKGDYYRYLAEFKSGDDRKEAADQSLKAYEAATATASADLAPTHPIRLGLALNFSVFYYEILNSPERACHLAKQAFDEAIAELDSLSEESYKDSTLIMQLLRDNFTLWTSDLEEGGEHSKGDERQGEN | Most abundant in roots and flowers. Belongs to the 14-3-3 family. |
Q99002 | MGHEDAVYLAKLAEQAERYEEMVENMKIVASEDRDLTVEERNLLSVAYKNVIGARRASWRIVTSIEQKEESKGNSSQVTLIKEYRQKIENELAKICDDILEVLDQHLIPSAKSGESKVFYHKIKGDYHRYLAEFAIGDRRKDSADKSLEAYKAATEVAQTELPPTHPIRLGLALNFSVFYYEILNAPDQACHLAKQAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSSEAETPARLMPLLRRRPLLRLPSRRRRAQG | Highest expression during the active growth period 10-12 hours after germination. Belongs to the 14-3-3 family. |
P29309 | AKLSEQAERYDDMAASMKAVTELGAELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNDKRQQMAREYREKVETELQDICKDVLDLLDRFLVPNATPPESKVFYLKMKGDYYRYLSEVASGDSKQETVASSQQAYQEAFEISKSEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKSAFDEAIRELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGEEADNVEGDN | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Belongs to the 14-3-3 family. |
Q6UFZ9 | MDKNDLVQKAKLAEQAERYDDMAAAMKAVTEQGGELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQQMAREYREKIEAELQDICKDVLALLDNYLIANATQAESKVFYLKMKGDYYRYLSEVASGDSKKTTVENSQQAYQEAFDISKKDMQPTHPIRLGLALNFSVFYYEILNSPEQACSLAKAAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Homodimer, and heterodimer with other family members. Expressed in brain, gill, heart, intestine, kidney, liver, ovary, skin, spleen and testis. Expressed throughout development. Expressed in the neural crest, eyes, yolk syncytium, tail bud and caudal somites of somitic embryos. Expressed in the neural crest, gill covers and gill arches, and the pectoral fins of post-somitic embryos. Repressed under stress conditions such as netting. Belongs to the 14-3-3 family. |
Q6UFZ8 | MDKNDLVQKAKLAEQAERYDDMAGAMKSVTEQGGELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQAMAKEYREKIETELQDICNDVLGLLDKYLIANATAAESKVFYLKMKGDYYRYLSEVAAGDAKKTTVDNSQQAYQDAFDISKKEMQPTHPIRLGLALNFSVFFYEILNNPEKACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLKGHLTLWTSENQGDEGETGEGEN | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Homodimer, and heterodimer with other family members. Expressed in brain, gill, heart, intestine, kidney, liver, ovary, skeletal muscle, spleen and testis. Expressed throughout development. Repressed under stress conditions such as netting. Belongs to the 14-3-3 family. |
A3KNI9 | MDKSDLVQKAKLAEQAERYDDMAASMKAVTEGGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQQMAREYREKIEAELQEICNDVLGLLEKYLIPNASQAESKVFYLKMKGDYYRYLSEVASGDSKRTTVENSQKAYQDAFEISKKEMQPTHPIRLGLALNFSVFYYEILNTPEQACSLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Homodimer, and heterodimer with other family members. Belongs to the 14-3-3 family. Extended N-terminus. |
Q5XHK2 | MDKSELVQKAKLSEQAERYDDMAASMKAVTELGAELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNDKRQQMAREYREKVETELQDICKDVLDLLDRFLVPNATPPESKVFYLKMKGDYYRYLSEVASGDSKQETVASSQQAYQEAFEISKSEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKSAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGEEADNVEGDN | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Homodimer, and heterodimer with other family members. Belongs to the 14-3-3 family. |
Q7T356 | MDKSDLVQKAKLAEQAERYDDMAAAMKAVTEGGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQQMAREYREKIETELQDICSDVLGLLEKYLIANASQAESKVFYLKMKGDYYRYLSEVASGDSKATTVENSQKAYQDAFDISKKDMQPTHPIRLGLALNFSVFYYEILNSPENACQLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSENQGEEAGENEN | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Homodimer, and heterodimer with other family members. Belongs to the 14-3-3 family. |
Q00740 | MNLQRFPRYPLTFGPTPIQPLARLSKHLGGKVHLYAKREDCNSGLAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVPDGFDIGFRRSWEDALESVRAAGGKPYAIPAGCSDHPLGGLGFVGFAEEVRAQEAELGFKFDYVVVCSVTGSTQAGMVVGFAADGRADRVIGVDASAKPAQTREQITRIARQTAEKVGLERDIMRADVVLDERFAGPEYGLPNEGTLEAIRLCARTEGMLTDPVYEGKSMHGMIEMVRNGEFPEGSRVLYAHLGGVPALNGYSFIFRDG | Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
G8ZFP4 | MHPKVDALLSRFPRITLIPWETPIQYLPRISRELGVDVYVKRDDLTGLGIGGNKIRKLEFLLGDALSRGCDTVITIGAVHSNHAFVTALAAKKLGLGAVLILRGEEVLKGNYLLDKLMGIETRIYEADNSWELMKVAEEVAEELKGEGKKPYIIPPGGASPVGTLGYIRGVGELYTQVKKLGLRIDTVVDAVGSGGTYAGLLLGSAIVNAEWSVVGIDVSSATEKAKERVKNLVEKTKELLGINVKVQEPRIYDYGFGAYGKIVKEVAKLIKSVGTMEGLLLDPVYTGKAFYGLMDLAKKGDLGESVLFIHTGGLPGIFHYGEEMLELLV | 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
Q8U4R3 | MHPKVQSLLSKFPRVELIPWETPIQYLPNISKLVGADIYVKRDDLTGLGIGGNKIRKLEYLLGDAIIRKADVIITVGAVHSNHAFVTGLAAKKLGFDVVLVLRGKEELRGNYLLDKIMGIETRVYEAKDSFELMKYAEEVAKELEEKGRKPYIIPVGGASPVGTLGYVRASGEIAEQGNRIGVNFDSIVVATGSGGTLAGLSVGLAILRKETRAIGMAVGKFGETMVNKVEELAKATGEFIGVKNLKLKIELYDYSFGEYGKITREVAETIRLVGTKEGVILDPVYTGKAFYGLLDLAKKGELGEKILFIHTGGISGTFHYGDKILSFL | 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
O57809 | MHPKIFALLAKFPRVELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAFVTGLAAKKLGLDAILVLRGKEELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGASPIGTLGYVRAVGEIATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAELLGVKVEVRPELYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGELGEKILFIHTGGISGTFHYGDKLLSLL | 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
B2UGM5 | MNLQRFPRYPLTFGPTPIQPLKRLSAHLGGKVELFAKREDCNSGLAFGGNKTRKLEYLIPEALEGGYDTLVSIGGIQSNQTRQVAAVAAHLGLKCVLVQENWVNYSDAVYDRVGNIEMSRIMGADVRLDSAGFDIGIRPSWEQAMDDVRKRGGKPFPIPAGCSEHPLGGLGFVGFAEEVRQQEAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRADKVIGIDASAKPEQTRAQILRIAQHTAELVDLGRNITERDVVLDTRYGGPEYGLPNEGTLEAIRLCARQEAMLTDPVYEGKSMHGMIDMVRNGEFPAGSRVLYAHLGGVPALNAYSFIFRNG | Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
Q8XS35 | MNLNKHPRHPLTFGPTPIQPLKRLSAHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLVPEVLAGGYDTLVSIGGIQSNQTRQVAAVAAHLGLKCVLVQENWVNYADAVYDRVGNIELSRILGADVRLDAAGFDIGIRPSWEQAMEDVRRAGGKPFPIPAGCSEHPLGGLGFVGFAEEVRQQEAEFGFRFDYIVVCSVTGSTQAGMVVGFAADGRADRVIGIDASAKPEQTREQILRIARDTAKLVELGRDITEDDVVLDTRYGGPEYGLPNEGTLEAIRLCARQEGMLTDPVYEGKSMHGMIDRVRGGEFPEGSRVLYAHLGGVPALNAYSFLFRNG | Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
Q98AM7 | MLEKFERYPLTFGLTPIEKLDRLGKHLGGKVEIYAKREDCNSGLAFGGNKLRKLEYVIPDAIASDADTLVTVGGVQSNHTRMVAAVAAKIGMKCLLVHESWVPHEDVVYDRVGNILLSRILGAEVRLVDDGFDIGIRRSWEKALYEVKARGGRPYAIPAGASVHPNGGLGYVGFAEEVRAQEEQLGFAFDYMVVCTVTGSTHAGMLVGFAKDGRQRNVIGIDASATPAKTKAQVLSIARHTATLVELGSELAEDDVVLLEDYAHPRYGIPSEETKEAIRLCARLEGMITDPVYEGKSMQGMIDLVQKGFFPAGSRILYAHLGGAPAINGYGYTFRNG | Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
Q93AG0 | MSLLEKFERYPLTFGPTPIEHLPRLTAALGGKVDIYAKRDDCNSGLAMGGNKLRKLEYIVPDAIASGADTLVSIGGVQSNHTRMVAATAAKIGMKCVVIQEKWVPHYDAVYDRVGNILMTKLMGADSRLVEDGFDIGIRKSWEDAIQSVEDAGGKPYAIPAGASVHKFGGLGYVGFAEEVAAQEKDLGFIFDYIIVCVVTGSTQGGMIVGFAALDRADRVIGIDASGTLQQTRDQVRKIVDATSELVNLGRSVREDEIVINPDYAYPAYGVPSEETNEAIRLAARTEAMITDPVYEGKSMQGMIDLARKGFFPEGSKVLYAHLGGAPALNGYSYYYKDG | Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
Q9AHF0 | MLEKFERYPLTFGATAIEYLPRLTEALGGDVEIWAKREDCNSGLAMGGNKLRKLEYIVPDAIASNADTLVSIGGVQSNHTRMVAAVAAKLGMKCRLVQESWVPHEDAVYDRVGNILMTRLMGADSRIVDDGFDIGIRQSWEDAIQSVIDEGGKPYAIPAGASVHKYGGLGYVAFAEEVARQEADLGFKFDYIIVCVVTGSTQAGMIVGFAAQDRADRVIGIDASGTPEQTRSQVRQIVDNTAELVELGRPVREDEIVILNDYAYPAYGVPSNETNEAIRLAARTEAMITDPVYEGKSMQGMIDLTRKGFFPKGSKVLYAHLGGAPALNGYSYTYRNG | Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
Q9URX3 | MGLEQFKKYPLTFGPTPITSMKRLSKTLGGKVEIFAKREDCNSGLAFGGNKIRKLEYLIPEAIDGGYDTLVSIGGIQSNQTRQVAAVAAHLGLDCVLIQEDWVDYKDTMYDRVGNIELSRIVNADVRLDSSKFDIGIRPSFKNALEELTKKGKKPFPIPAGCSEHPYGGLGFVGCVEEIYEQEKQLGFKFDKIVVCTVTGSSFAGIIVGMALTGRQKDVIGIDASATPEKTKAQVLRIAQNTAKLIGLEKELTESDVNIDTRFAHPAYGIPNEGTIEAIKLCGATEGVLTDPVYEGKSMQGLIHLVRNNEIAEGSKVLYIHLGGAPALSAYSAYFKNT | Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
Q9WY68 | MRIDLSLKPTPVQFLKRLSEKYGFNIYVKRDDLTELVGSGNKIRKLEYLLWEALKKGATTVFTCGGLQSNHARATAYVSRRYGLKPVLFLRKGEKVLNGNLLLDILLGAEIVEVSPEEYERIDEIFDVHKKMREKKGEKVYVIPEGGSNSLGAFGYFNAVLEMKDQLNLESFDAIVCAVGSGGTIAGLSAGISFLEYHVPVVGVNVTTKNSDYFVGKVKRIISGMEEYGLRVNETVFEVVDDYRGPGYAIPSSEDVEILKEVASIEGIILDPVYTAKAFRGMIEMFRNSEKNVLFIHTGGIFGLFAQSRRLV | 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
Q6J256 | MNLKKFPRHVLTFGPTPIQPLKRLSAHLGGKVDLYAKREDCNSGLAFGGNKTRKLEYLIPEALEGGYDTLVSIGGIQSNQTRQVAAVAAHLGLKCVLVQENWVNYSDAVYDRVGNIEMSRIMGADVRLDAAGFDIGIRQSWEQAMADVRAAGGKPFPIPAGCSEHPRGGLGSVGFAEEVRQQEAELGFKFDYLVVCSVTGSTQAGMVVGFAADGRADRVIGIDASAKPQQTFEQILRIAKNTAELVELGRDITEKDVVLDRRFGGPEYGLPNEGTLEAIRLSARFEGMLTDPVYEGKSMHGMIEKVRLGEFPAGSKVLYAHLGGVPALNAYSFLFRNG | Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
C5CQC9 | MNLKKFPRHALTFGPTPIHPLKRLSAHLGGEVELYAKREDCNSGLAFGGNKTRKLEYLIPEALEGGYDTLVSIGGIQSNQTRQVAAVAAHLGLKCVLVQENWVNYSDAVYDRVGNIEMSRIMGADVRLDSAGFDIGIRKSWEEAMADVRKAGGKPFPIPAGCSEHPRGGLGFVGFAEEVRQQEAELGFKFDYIVTCSVTGSTQAGMVVGFAADGRADRVIGIDASAKPEQTFAQIVRIAKGTAELVELGRDITDKDVVLDRRFGGPEYGLPNEGTLESIRLCARLEGMLTDPVYEGKSMHGMIEKVRLGEFPAGSKVLYAHLGGVPALNAYSFLFRNG | Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
Q5E9H2 | MFTLPQKEFRMTTACPGSDSIQDLPSNKGDGLERECSRKPDQKLLKFYGVGDPAAELSSSSPYLSSRGSVIKWFWDSAEEGYRTYHMDEYDEDKNPSGIINLGTSENKLCFDLLSRRLSQSDMLQVEPALLQYPDWRGHLFLREEVARFLSFYCRSPAPLKPENVVVLNGCASLFSALATVLCEAGEAFLIPAPYYGAITQHVYLYGNVRLVCVYLDSEVTGLETRPFQLTVEKLEMALQGANSEGVKVKGLILINPQNPLGDIYSPGELQEYLEFAKRHELHVMVDEVYMLSVFEESAGYRSVLSLERLPDPQRTHVMWATSKDFGMSGLRFGTLYTENWAVATAVASLCRYHGLSGLVQYQMAQLLRDHDWINQVYLPENHARLKAAHTYVSEDLRALGIPFVSRGAGFFIWVDLRKYLPEATFEEEVLLWRRFLENKVLLSFGKAFECKEPGWFRLVFSDKTHRLHLGMQRVRQVLEGQPQLADGAPPHQIQEPQGPHR | Does not catalyze the synthesis of 1-aminocyclopropane-1-carboxylate but is capable of catalyzing the deamination of L-vinylglycine. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Similar to plant 1-aminocyclopropane-1-carboxylate synthases but lacks a number of residues which are necessary for activity. |
Q96LX5 | MFTLPQKDFRAPTTCLGPTCMQDLGSSHGEDLEGECSRKLDQKLPELRGVGDPAMISSDTSYLSSRGRMIKWFWDSAEEGYRTYHMDEYDEDKNPSGIINLGTSENKLCFDLLSWRLSQRDMQRVEPSLLQYADWRGHLFLREEVAKFLSFYCKSPVPLRPENVVVLNGGASLFSALATVLCEAGEAFLIPTPYYGAITQHVCLYGNIRLAYVYLDSEVTGLDTRPFQLTVEKLEMALREAHSEGVKVKGLILISPQNPLGDVYSPEELQEYLVFAKRHRLHVIVDEVYMLSVFEKSVGYRSVLSLERLPDPQRTHVMWATSKDFGMSGLRFGTLYTENQDVATAVASLCRYHGLSGLVQYQMAQLLRDRDWINQVYLPENHARLKAAHTYVSEELRALGIPFLSRGAGFFIWVDLRKYLPKGTFEEEMLLWRRFLDNKVLLSFGKAFECKEPGWFRFVFSDQVHRLCLGMQRVQQVLAGKSQVAEDPRPSQSQEPSDQRR | Does not catalyze the synthesis of 1-aminocyclopropane-1-carboxylate but is capable of catalyzing the deamination of L-vinylglycine. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Similar to plant 1-aminocyclopropane-1-carboxylate synthases but lacks a number of residues which are necessary for activity. |
Q8CHS6 | MFCLPQQESTAPTTCTGSASTQDMDSGYGDGLQGECLRKPDQTQPKLYGVGDPTATFSSDSSCLSSRGRVIKWFWDSAEEGYRTYHMDEYDEDKNPSGIINLGTSENKLCFDLLSWRLTQGDMLHVEPSLLQYPDWRGHLFLREEVAKFLSFYCKSPAPLKPENVVVLNGCASLFSALATVLCEAGEALLIPTPYYGAITQHIYLYGNVRLAYVYLDSKVTGLNTRPFQLTVEKLEMVLQGVSSEGVKVKGLILINPQNPLGDVYSPEELQDFLRFAMRHKLHVIMDEVYMLSVFEESLGYRSVLSLERLPDPQRTHVMWATSKDFGMSGLRFGVLYTENQHVATAVASLCRYHGLSGLVQHQMAQLLRDHDWISQVYLPENHARLKAAHTYVSEELRALGIPFVSRGAGFFIWVDLRKYLCKGTFEEEALLWRQFLDNKVLLSSGKTFECKEPGWFRVVFSDKENRLRLGMQRMRQVLEGQSQVVEDASPCHAQEPQSQPR | Does not catalyze the synthesis of 1-aminocyclopropane-1-carboxylate but is capable of catalyzing the deamination of L-vinylglycine. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Similar to plant 1-aminocyclopropane-1-carboxylate synthases but lacks a number of residues which are necessary for activity. |
Q9W698 | MLTEALVAVRQGTQTPAAQTTCAPSTMSSSSRPPLETLQAQSVSADETPGSALPACAQPCETARSATPTGGETPNRSRYLSHRGNSIRQQQGILQEGFLLYSLDKFHETDKPDGIINLGTSENKLCHDLLHERLTRPDMLLLDPPLLQYPDWSGHQFLREEVAKFLTDYCCSPKPLKAENVVVMNGCASLFSCIASVICDPKDAILISTPFYGAITEHLGLYSDVKLYHIHLDCEASGEDGRLFHLTVDKLEEGLRRAEHEGFIVRGLVLMNPHNPLADIYTPKEMVGFLEFAKRNELHTIVDEVYMLSVFDESVTFDSVLSLESVPDPQRTHVMWGLGKDFAMAGIRVGTLYSESRDLVEAVAKLGAFHGIPGTTQRQVAQLLQDREWIDTQYLPRNRSRLKAARSYVTGELRGLDVPYLDRSAAMFVWADLRKFLAEPSFEEEMRLWRHFLKHKVVLSCGQAFSCSTPGWFRIVFSDQDRRLKLGMKRIKEALEEYKDQITVTDCYSIKDGGPRVRASGKDSDNAAIVGSTLPQGKSSDMLEEKDHTVQAGLGADELVLRDCQPSKPAEGLDSLIGTLRHQIRSSDWLEKNTPELSAGEDPEILDVFKALLERARK | Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Similar to plant 1-aminocyclopropane-1-carboxylate synthases but lacks a number of residues which are necessary for activity. |
Q4AC99 | MSHRSDTLPVPSGQRRGRVPRDHSIYTQLLEITLHLQQAMTEHFVQLTSRQGLSLEERRHTEAICEHEALLSRLICRMINLLQSGAASGLELQVPLPSEDSRGDVRYGQRAQLSGQPDPVPQLSDCEAAFVNRDLSIRGIDISVFYQSSFQDYNAYQKDKYHKDKNTLGFINLGTSENKLCMDLMTERLQESDMNCIEDTLLQYPDWRGQPFLREEVARFLTYYCRAPTRLDPENVVVLNGCCSVFCALAMVLCDPGEAFLVPAPFYGGFAFSSRLYAKVELIPVHLESEVTVTNTHPFQLTVDKLEEALLEARLEGKKVRGLVLINPQNPLGDIYSPDSLMKYLEFAKRYNLHVIIDEIYMLSVFDESITFHSILSMKSLPDSNRTHVIWGTSKDFGISGFRFGALYTHNKEVASAVSAFGYLHSISGITQHKLCQLLQNTEWIDKVYLPTNCYRLREAHKYITAELKALEIPFHNRSSGLYVWINLKKYLDPCTFEEERLLYCRFLDNKLLLSRGKTYMCKEPGWFCLIFADELPRLKLAMRRFCDVLQEQKEALIVKQLEDAMRE | Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. While belonging to the class-I pyridoxal-phosphate-dependent aminotransferase family, it lacks a number of residues which are necessary for activity thus suggesting that it lacks enzymatic activity. |
Q3TQ30 | MSENRNEGSSQAAKANSDTQTPSHFKVTHPRLRDQLKKKSSKKKGFKFVQEKMLKFQHVIRNQFLQQISQQMQCVPPGDQQCTQTSRKRKKMGYLLSQMVNFLWSNTVKKLKFKVPLPCLDSRCGIKVGHQTLSPWQTGQSRPSLGGFEAALASCTLSKRGAGIYESYHLSFQSYEAYQADKYHKDKNPSGYINLSTSENKLCLDLITARLTQSDMNLLDEAQLQYSDWKGQPFLREELASFLTHYCKAPTPLDPENVVVLNGCSSVFASLAMVLCDPGDALLIPTPCYNGFVFSSHLYSKIELIPVHLESQVPRSNLDSFQLTVDKLKLALTQAKKKAKKVKGLVLINPQNPLGDVYTQSSLQEYLVFAKTHKLHVIMDEIYMLSVFEPSVTFHSVLSIKDLPDPNMTHMIWGTSKDFGMSGIRFGVLYTHNKEVASAMKAFGYHHGVSGITQYKLCRLLQDKEWISKVYLPKNHSRLQKAYSYITKILKDLKIPFYNGGSGLFVWINLKAYLSPCTFDQEQILHQRFRDKKLLLSSGKSYMCIEPGWFRLVFAETHLHLQVAMDRFCHVLAEHKKHEK | Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. While belonging to the class-I pyridoxal-phosphate-dependent aminotransferase family, it lacks a number of residues which are necessary for activity thus suggesting that it lacks enzymatic activity. |
Q96355 | MGRGRVQLKRIENKINRQVTFSKRRAGLFKKAHEISVLCDAEVALVVFSHKGKLFEYSTDSCMEKILERYERYSYAERQLIAPESDVNTNWSMEYNRLKAKIELLERNQRHYLGEDLQAMSPKELQNLEQQLDTALKHIRSRKNQLMYDSVNELQRKEKAIQEQNSMLSKQIKEREKVLMAQQEQWDQQNHGQNMPSPPPPQQHQIQHPYMLSHQPSPFLNMGGLYQEEDPMAMRRNDLDLSLEPVYNCNLGCFAA | Transcription factor that promotes early floral meristem identity in synergy with LEAFY. Displays a redundant function with CAULIFLOWER in the up-regulation of LEAFY. Required subsequently for the transition of an inflorescence meristem into a floral meristem, and for the normal development of sepals and petals in flowers. Regulates positively B class homeotic proteins (By similarity). Homodimer capable of binding to CArG-box sequences. Expressed in some of the meristems of arrest-stage broccoli heads. First observed in young floral meristem before organs initiation. Accumulates strongly in the sepals of the early stage bud. In more mature buds, expressed on the adaxial side of the sepals, in the petal primordia, and transiently in young stamen primordia. |
Q570B7 | MAMVDEPLYPIAVLIDELKNDDIQLRLNSIRRLSTIARALGEERTRKELIPFLSENSDDDDEVLLAMAEELGVFIPFVGGIEFAHVLLPPLESLCTVEETCVREKAVESLCKIGSQMKENDLVESFVPLVKRLAGGEWFAARVSACGIFHVAYQGCTDVLKTELRATYSQLCKDDMPMVRRAAASNLGKFATTVESTFLIAEIMTMFDDLTKDDQDSVRLLAVEGCAALGKLLEPQDCVARILPVIVNFSQDKSWRVRYMVANQLYELCEAVGPDCTRTDLVPAYVRLLRDNEAEVRIAAAGKVTKFCRLLNPELAIQHILPCVKELSSDSSQHVRSALASVIMGMAPILGKDSTIEHLLPIFLSLLKDEFPDVRLNIISKLDQVNQVIGIDLLSQSLLPAIVELAEDRHWRVRLAIIEYVPLLASQLGIGFFDDKLGALCMQWLQDKVYSIREAAANNLKRLAEEFGPEWAMQHLVPQVLDMVNNPHYLHRMMVLRAISLMAPVMGSEITCSKFLPVVVEASKDRVPNIKFNVAKLLQSLIPIVDQSVVDKTIRQCLVDLSEDPDVDVRYFANQALNSIDGSTAAQS | The A subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Seems to act as a positive regulator of PP2A catalytic activity. Confers resistance to phosphatase inhibitors such as okadaic acid and cantharidin. Involved during developmental process such as seedling and floral developments, root gravitropism, and stomatal opening regulation. Involved in the regulation of auxin efflux, especially during basipetal (tips to base) auxin transport in roots, and appears to contribute to the perception of auxin efflux inhibitors such as 1-N-naphthylphthalamic acid (NPA) and to semicarbazone I (substituted phenylsemicarbazone of 2-acetylarylcarboxylic acids) (SCB-I). Modulates the magnitude of ethylene response in the hypocotyl and stem, and functions as a general positive transducer of early ABA signaling. The holoenzyme composed of PP2AA1, PP2A4 and B'ZETA or B'ETA acts as negative regulator of plant innate immunity by controlling BAK1 phosphorylation state and activation in surface-localized immune receptor complexes (PubMed:25085430). PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (subunit A), that associates with a variety of regulatory subunits such as subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) and the regulatory subunits TON2. Interacts with CYP20-1/ROC7. Also interacts with phosphatidic acid (PA), a lipid signaling molecule. Interacts with CHIP. Interacts with SIC/RON3 (PubMed:26888284). Mostly expressed in cell-dividing tissues such as apical meristems. Ubiquitous, with higher levels in roots and flowers (at protein level). Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure (By similarity). Ubiquitinated. CHIP-mediated ubiquitination enhances phosphatase activity after an abiotic stress such as low temperature or darkness. Belongs to the phosphatase 2A regulatory subunit A family. |
Q32PI5 | MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELHKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCRENVIMTQILPCIKELVSDANQHVKSALASVIMGLSPILGKDSTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPVLEKLTQDQDVDVKYFAQEALTVLSLA | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT. Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis. PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD (PubMed:12912990). Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation sites (By similarity). Interacts with IPO9 (By similarity). Interacts with TP53 and SGO1 (By similarity). Interacts with PLA2G16; this interaction might decrease PP2A activity (By similarity). Interacts with CTTNBP2NL (By similarity). Interacts with GNA12; the interaction promotes protein phosphatase 2A activation causing dephosphorylation of MAPT (By similarity). Interacts with CIP2A; this interaction stabilizes CIP2A (By similarity). Interacts with PABIR1/FAM122A (By similarity). Interacts with ADCY8; antagonizes interaction between ADCY8 and calmodulin (By similarity). Interacts with CRTC3 (when phosphorylated at 'Ser-391') (By similarity). Interacts with SPRY2 (By similarity). Centromeric localization requires the presence of BUB1. Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure (By similarity). Belongs to the phosphatase 2A regulatory subunit A family. |
Q09543 | MSVVEEATDDALYPIAVLIDELRNEDVTLRLNSIRKLSTIALALGVERTRNELIQFLTDTIYDEDEVLLVLAEQLGNFTPLVGGPDHVHCLLLPLENLATVEETVVRDKAVESLRKIADKHSSASLEEHFVPMLRRLATGDWFTSRTSACGLFSVVYPRVSPAIKSELKSMFRTLCRDDTPMVRRAAAAKLGEFAKVFEKTAVIEGLHSSLTDLHVDEQDSVRLLTVESAIAFGTLLDKANKKKLIEPILIELFDDKSWRVRYMVAEKLIEIQNVLGEDMDTTHLVNMYTNLLKDPEGEVRCAATQRLQEFALNLPEDKRQNIICNSLLNVAKELVTDGNQLVKSELAGVIMGLAPLIGKEQTVSELLPIYMQLLNDQTPEVRLNIISSLDKVNEVIGAAQLSTSLLPAIVGLAEDGKWRVRLAIVQFMPLLASQLGQEFFDEKLLPLCLNWLTDHVFSIREASTLIMKELTQKFGGQWASTNIVPKMQKLQKDTNYLQRMTCLFCLNTLSEAMTQEQILKEIMPIVKDLVEDDVPNVRFNAAKSLKRIGKNLTPSTLTSEVKPLLEKLGKDSDFDVRYFSEEAKNSLGL | Acts as a scaffolding protein for phosphatase let-92 and its regulatory subunits (Probable). Probably together with let-92 and regulatory subunit sur-6, regulates centriole duplication, microtubule outgrowth and mitotic spindle stability during early embryonic cell division by preventing the degradation of sas-5 and kinase zyg-1 (PubMed:23336080, PubMed:17218259). During vulva development, may play a role with phosphatase let-92 and regulatory subunit sur-6 in the induction of vulva cell precursors by positively regulating let-60/Ras-MAP kinase signaling, probably by promoting lin-45 activation (PubMed:10521400). Plays a positive role in axon guidance probably by inhibiting phosphatase let-92 (PubMed:20392746). Part of a complex consisting of a common heterodimeric core enzyme, composed of catalytic subunit let-92 and constant regulatory subunit paa-1, that associates with a variety of regulatory subunits which confer distinct properties to the holoenzyme (PubMed:17218259, PubMed:21497766). Interacts with rsa-1 (PubMed:17218259). Localizes to P granules in embryonic cells. Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. RNAi-mediated knockdown causes severe embryonic lethality (PubMed:10521400, PubMed:23336080). Causes a failure to duplicate centrioles resulting in the formation of monopolar spindles at the 2-cell embryonic stage (PubMed:21497766, PubMed:23336080). sas-5 protein levels are reduced in embryos (PubMed:21497766). The few surviving animals lack a vulva resulting from defects in vulva cell induction, vulva precursor cell (VPC) generation and in vulval execution linage (PubMed:10521400). Partially suppresses multivulva formation in a let-60 n1046 mutant background (PubMed:10521400). Belongs to the phosphatase 2A regulatory subunit A family. |
Q23922 | MASINTESDDYHPIVILIDELKNEDIQLRLNSIKKLQSIAKALGPERTRTELIPYLQDSVLEDEDEVLVVLSEELGNLIEFVGGAEHAVCLLPPLQILAGAEELVVREKAVESLCKIAKEIPTSSFEESFLPLLFSLSKADWFTSRTSACGLFTVSYPRANAEMKKSLRKTFGGLCHDDTPMVKRAAATNLGSFAKQIEKESVKSEILPLFQSLSTDEQDSVRLLGVENCALLGSMLTNEENIQFILPTIKASSLDKSWRVRYMVARLLKELCESMGTEITKTELIGAFVKLLKDTEAEVRTEASLRIADVCSLLTKEMNIKTILPCVKDLVSDSSQHVRAALAQVIMSLAPIYGKEDTLTHLLELFLHLLKDDFPDVRLNIISKLDQVSKVIGIEMLSQSLLPAIVELAEDHQWRVRLAIIDYIPLLASQLGVEFFDEKLGNLCMTWLGDPVFSIREAATNNLKKLTEVFGVDWAKNNIIPKVLSLHSHPNYLYRMTTLFSISTLSTVVGGDVISSSMVPLLAKMVSDKVPNIRFNVAKTFQTIIPLLDSTIVQSRVKPLLVKLHEDTDKDVKFYASQALQLC | Scaffolding molecule which may coordinate the assembly of the catalytic subunit and a variable regulatory B subunit (PubMed:20493808). Component of the Sca1 complex, a regulator of cell motility, chemotaxis and signal relay (PubMed:20493808). The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells where it regulates F-actin dynamics and signal relay by controlling the activation of rasC and the downstream target of rapamycin complex 2 (TORC2)-Akt/protein kinase B (PKB) pathway (PubMed:20493808). Component of the Sca1 complex composed of at least gefA, gefH, scaA, phr, and the protein phosphatase 2A subunits pppA and pho2B (PubMed:20493808). The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells (PubMed:20493808). Membrane localization of the Sca1 complex is regulated by scaA phosphorylation by PKB and PKB-related PKBR1 (PubMed:20493808). Belongs to the phosphatase 2A regulatory subunit A family. |
Q9VLN3 | MAASDKSVDDSLYPIAVLIDELKNEDVQLRLNSIKKLSTIALALGEERTRSELIPFLTETIYDEDEVLLALADQLGNFTSLVGGPEFAMYLIPPLESLATVEETVVRDKAVESLRTVAAEHSAQDLEIHVVPTLQRLVSGDWFTSRTSACGLFSVCYPRVTQPVKAELRANFRKLCQDETPMVRRAAANKLGEFAKVVETEYLKSDLIPNFVQLAQDDQDSVRLLAVEACVSIAQLLPQDDVEHLVLPTLRQCASDSSWRVRYMVAEKFVDLQKAVGPEITRVDLVPAFQYLLKDAEAEVRAAVATKVKDFCANLDKVNQVQIILSSILPYVRDLVSDPNPHVKSALASVIMGLSPMLGAYQTVEQLLPLFLIQLKDECPEVRLNIISNLDCVNDVIGIQQLSQSLLPAIVELAEDSKWRVRLAIIEYMPALAGQLGQEFFDQKLRGLCMGWLNDHVYAIREAATLNMKKLVEQFGAPWAEQAIIPMILVMSRNKNYLHRMTCLFCLNVLAEVCGTDITTKLLLPTVLLLAADPVANVRFNVAKTLQKISPFLEASVIDAQVKPTLDKLNTDTDVDVKHFAAQAIAGIAAA | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa regulatory subunit (PR65) (subunit A). The core complex associates with a third, variable subunit (subunit B), which confers distinct properties to the holoenzyme. Expression varies in tissues throughout development. Highly distributed expression in early embryos. In late embryonal development, found at high levels in nervous system and gonads. In third instar larvae, found in brain, imaginal disks and salivary glands. Expressed both maternally and zygotically. Expressed at lower levels in larvae and adult. Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. Belongs to the phosphatase 2A regulatory subunit A family. Intron retention. |
Q96DH3 | MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCRENVIMSQILPCIKELVSDANQHVKSALASVIMGLSPILGKDNTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (PubMed:15525651). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (PubMed:16580887). PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation sites (By similarity). Interacts with IPO9 (PubMed:12670497). Interacts with TP53 and SGO1 (PubMed:17245430, PubMed:16580887). Interacts with PLA2G16; this interaction might decrease PP2A activity (PubMed:17374643). Interacts with CTTNBP2NL (PubMed:18782753). Interacts with GNA12; the interaction promotes protein phosphatase 2A activation causing dephosphorylation of MAPT (PubMed:15525651). Interacts with CIP2A; this interaction stabilizes CIP2A (PubMed:28174209). Interacts with PABIR1/FAM122A (PubMed:27588481). Interacts with ADCY8; antagonizes interaction between ADCY8 and calmodulin (By similarity). Interacts with CRTC3 (when phosphorylated at 'Ser-391') (PubMed:30611118). Interacts with SPRY2 (PubMed:17974561). (Microbial infection) Interacts with JC virus small t antigen; this interaction inhibits PPP2R1A activity. Centromeric localization requires the presence of BUB1. Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. The disease is caused by variants affecting the gene represented in this entry. Belongs to the phosphatase 2A regulatory subunit A family. |
Q76MZ3 | MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCRENVIMTQILPCIKELVSDANQHVKSALASVIMGLSPILGKDNTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit (PubMed:10100624). Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (By similarity). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (By similarity). PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation sites (PubMed:22417654). Interacts with IPO9 (By similarity). Interacts with TP53 and SGO1 (By similarity). Interacts with PLA2G16; this interaction might decrease PP2A activity (By similarity). Interacts with CTTNBP2NL (By similarity). Interacts with GNA12; the interaction promotes protein phosphatase 2A activation causing dephosphorylation of MAPT (By similarity).Interacts with CIP2A; this interaction stabilizes CIP2A (By similarity). Interacts with PABIR1/FAM122A (By similarity). Interacts with ADCY8; antagonizes interaction between ADCY8 and calmodulin (PubMed:16258073). Interacts with CRTC3 (when phosphorylated at 'Ser-391') (PubMed:30611118). Interacts with SPRY2 (By similarity). Centromeric localization requires the presence of BUB1. Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. Belongs to the phosphatase 2A regulatory subunit A family. |
P36875 | VEAAHLKTDIMSVFDDLTQDDQDSFRFLAVEGCAALGKLLEPQDCLAHILPVIVNFSQDKSWRVRYMVANQLYELCEAVGPDSTKTELVPAYVRLLRDNVAEVRIAAAGKVSKFSRILSPELAIQHILPCVKELSTDSSQHVRSALASVIMGMAPVLGKDATIEQLLPIFLSLLKDEFPDVRLNIISKLDQVNQVIGIDLLSQSLLPAIVELAEDRHWRVRLAIIEYIPLLASQLGVGFFDDKLGALIMQWLKDKEYSIRNAAANNVKRLAAEEFGPEWAMQHIIPQVLDMINDPHYLYRMTILHAISLLAPVLGSEITSTNLLPLVVNASKDRVPNIKFNVAKVLQSLIPIVDESVVESTIRPCLVELSEDPDVDVRFFASQALQSSDQVKMSS | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa regulatory subunit (PR65) (subunit A). The core complex associates with a third, variable subunit (subunit B), which confers distinct properties to the holoenzyme. Belongs to the phosphatase 2A regulatory subunit A family. |
P54612 | MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCRENVIMTQILPCIKELVSDANQHVKSALASVIMGLSPILGKDNTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT. Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis. PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation sites. Interacts with IPO9. Interacts with TP53 and SGO1. Interacts with PLA2G16; this interaction might decrease PP2A activity. Interacts with CTTNBP2NL. Interacts with GNA12; the interaction promotes protein phosphatase 2A activation causing dephosphorylation of MAPT. Interacts with CIP2A; this interaction stabilizes CIP2A (By similarity). Interacts with PABIR1/FAM122A (By similarity). Interacts with ADCY8; antagonizes interaction between ADCY8 and calmodulin (By similarity). Interacts with CRTC3 (when phosphorylated at 'Ser-391') (By similarity). Interacts with SPRY2 (By similarity). Centromeric localization requires the presence of BUB1. Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. Belongs to the phosphatase 2A regulatory subunit A family. |
Q10293 | MQTENQVNDLYPIAVLIDELKHDEITYRLNALERLSTIALALGPERTRDELIPFLDESIDDEDEVLSALADQLGNFVDYVGGPEYAHVLLSPLENLAATEETVVRDKAVDSLNKVCICLSQEQLEQYFVPLVQRLSTAEWFTSRASSAGLYCAAYSQSENPAVKVSLRQSFSHLCHDEAPMVRRPAATNCAKFVFLVTKQEAIDEFIPLFNSLSNDDQDSVRLLSFDIMVSLAEVLKSDSEIRHYLLQPLRSFVSDSSWRTRYMVAANFVKLAKVVGPSLIKDELIKPFVLLMKDTEQEVRRAIATQIPGFCELLDKRIVLEEIIPVIQELINDPAQHVRAALGMNIGALAPQLGKEKTTEYLLPMFLELLKDENPEVRLNIISKLEVVNKVVGIELLSQSLLPAIVTLAEDKQWRVRLAIIDYIPLLAQQLGVEFFNEKMGNLCMSWLEDHVYSIREAAIKNLRKLTEIFGLEWATETIIPKFLAMRSHPNYLYRMTTIFAISEIAPALNAEVIEKQILPTLEQLVNDPIPNIRFNVAKAFEVLKPVLAAGGDSTVYEQQIIPLLEQLTKDNDPDVQYFATQALEQTND | Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subsets of substrates (By similarity). PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa (PR65) (Subunit A) and a 55 kDa (PR55) (Subunit B) regulatory subunit. Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. Belongs to the phosphatase 2A regulatory subunit A family. |
D6VPK2 | MSGARSTTAGAVPSAATTSTTSTTSNSKDSDSNESLYPLALLMDELKHDDIANRVEAMKKLDTIALALGPERTRNELIPFLTEVAQDDEDEVFAVLAEQLGKFVPYIGGPQYATILLPVLEILASAEETLVREKAVDSLNNVAQELSQEQLFSDFVPLIEHLATADWFSSKVSACGLFKSVIVRIKDDSLRKNILALYLQLAQDDTPMVKRAVGKNLPILIDLLTQNLGLSTDEDWDYISNIFQKIINDNQDSVKFLAVDCLISILKFFNAKGDESHTQDLLNSAVKLIGDEAWRVRYMAADRFSDLASQFSSNQAYIDELVQPFLNLCEDNEGDVREAVAKQVSGFAKFLNDPSIILNKILPAVQNLSMDESETVRSALASKITNIVLLLNKDQVINNFLPILLNMLRDEFPDVRLNIIASLKVVNDVIGIELLSDSLLPAITELAKDVNWRVRMAIIEYIPILAEQLGMQFFDQQLSDLCLSWLWDTVYSIREAAVNNLKRLTEIFGSDWCRDEIISRLLKFDLQLLENFVSRFTILSALTTLVPVVSLDVVTEQLLPFISHLADDGVPNIRFNVAKSYAVIVKVLIKDEAKYDALIKNTILPSLQTLCQDEDVDVKYFAKKSLAECQELLKN | Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subsets of substrates. PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa regulatory subunit (PR65) (subunit A). The core complex associates with a third, variable subunit (subunit B), which confers distinct properties to the holoenzyme. Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. Present with 16900 molecules/cell in log phase SD medium. Belongs to the phosphatase 2A regulatory subunit A family. |
Q9LRZ9 | MSMIDEPLYPIAVLIDELKNDDIQLRLNSIRRLSTIARALGEERTRKELIPFLSENNDDDDEVLLAMAEELGVFIPYVGGVEYAHVLLPPLETLSTVEETCVREKAVESLCRVGSQMRESDLVDHFISLVKRLAAGEWFTARVSACGVFHIAYPSAPDMLKTELRSLYTQLCQDDMPMVRRAAATNLGKFAATVESAHLKTDVMSMFEDLTQDDQDSVRLLAVEGCAALGKLLEPQDCVQHILPVIVNFSQDKSWRVRYMVANQLYELCEAVGPEPTRTELVPAYVRLLRDNEAEVRIAAAGKVTKFCRILNPEIAIQHILPCVKELSSDSSQHVRSALASVIMGMAPVLGKDATIEHLLPIFLSLLKDEFPDVRLNIISKLDQVNQVIGIDLLSQSLLPAIVELAEDRHWRVRLAIIEYIPLLASQLGVGFFDDKLGALCMQWLQDKVHSIRDAAANNLKRLAEEFGPEWAMQHIVPQVLEMVNNPHYLYRMTILRAVSLLAPVMGSEITCSKLLPVVMTASKDRVPNIKFNVAKVLQSLIPIVDQSVVEKTIRPGLVELSEDPDVDVRFFANQALQSIDNVMMSS | The A subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Involved during developmental process such as seedling and floral developments. Seems to act as a negative regulator of PP2A catalytic activity. Associates with the serine/threonine-protein phosphatase PP2A catalytic subunit C and regulatory subunit B' to positively regulates beta-oxidation of fatty acids and protoauxins in peroxisomes by dephosphorylating peroxisomal beta-oxidation-related proteins (PubMed:25489022). PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (subunit A), that associates with a variety of regulatory subunits such as subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) (By similarity). Interacts with B'THETA (PubMed:25489022). Interacts with SRK2E/OST1 (PubMed:26175513). Interacts with SIC/RON3 (PubMed:26888284). Interacts with B'THETA in the cytosol and peroxisomal import occurs by a piggybacking transport. A number of isoforms are produced. According to EST sequences. Ubiquitous, with higher levels in roots and flowers (at protein level). Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure (By similarity). Belongs to the phosphatase 2A regulatory subunit A family. |
Q8NHV8 | MAGASELGTGPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLENLATVEETVVRDKAVESLRQISQEHTPVALEAYFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQQFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKSEIVPLFTSLASDEQDSVRLLAVEACVSIAQLLSQDDLETLVMPTLRQAAEDKSWRVRYMVADRFSELQKAMGPKITLNDLIPAFQNLLKDCEAEVRAAAAHKVKELGENLPIEDRETIIMNQILPYIKELVSDTNQHVKSALASVIMGLSTILGKENTIEHLLPLFLAQLKDECPDVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATNNLMKLVQKFGTEWAQNTIVPKVLVMANDPNYLHRMTTLFCINALSEACGQEITTKQMLPIVLKMAGDQVANVRFNVAKSLQKIGPILDTNALQGEVKPVLQKLGQDEDMDVKYFAQEAISVLALA | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with IPO9. Interacts with SGO1. Interacts with RAF1. Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. Belongs to the phosphatase 2A regulatory subunit A family. Contaminating sequence. Sequence of unknown origin in the N-terminal part. |
E9QNJ1 | MAGAAGPGSGPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRTELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLESLATVEETVVRDKAVESLRQISQEHTPVALEAHFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQHFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKTEIVPLFTNLASDEQDSVRLLAVEACVSIAQLLSQEDLEALVMPTLRQAAEDKSWRVRYMVADKFSELQKAVGPKIALSDLIPAFQSLLRDCEAEVRAAAAHKVRELCENLPAEGRETVIMNQILPYIKELVSDTNQHVKSALASVIMGLSTVLGKENTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATNNLMKLVQKFGTEWAQNTIVPKVLVMANDPNYLHRMTTLFCINALSEACGKEITTKQMLPIVLKMAGDQVANVRFNVAKSLQKIGPILDTNALQGEVKPVLQKLGQDEDMDVKYFAQEAISVLALA | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with IPO9 (By similarity). Interacts with SGO1 (By similarity). Interacts with RAF1 (By similarity). Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. Belongs to the phosphatase 2A regulatory subunit A family. |
P54613 | NSAGAAAPGTGPVAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRTELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLESLATVEETVVRDKAVESLRQISQEHTPVALEAHFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQHFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKSEIVPLFTNLASDEQDSVRLLAVEACVSIAQLLSQDDLEALVMPTLRQAAEDKSWRVRYMVADKFSELQRAVGPKITLNDLIPAFQNLLKDCEAEVRAAAAHKVKELCENLPIEGRETIIMNQILPCIKELVSDTNQHVKSALASVIMGLSTILGKENTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATNNLMKLVQKFGTEWAQNTIVPKVLVMANDPNYLHRMTTLFCINVLSEACGQEITTKQMLPIVLKMAGDQVANVRFNVAKSLQKIGPILDTDALQEEVKPVLQKLGQDEDMDVKYFAQEAISVLALA | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa regulatory subunit (PR65) (subunit A). The core complex associates with a third, variable subunit (subunit B), which confers distinct properties to the holoenzyme. Interacts with IPO9 (By similarity). Interacts with SGO1 (By similarity). Interacts with RAF1 (By similarity). Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. Belongs to the phosphatase 2A regulatory subunit A family. |
Q4QQT4 | MAGAAGPGTVPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRTELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLESLATVEETVVRDKAVESLRQISQEHTPVALEAHFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQHFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKTEIVPLFTNLASDEQDSVRLLAVEACVSIAQLLSQDDLEALVMPTLRQAAEDKSWRVRYMVADKFSELQKAVGPKIALSDLIPAFQSLLRDCEAEVRAAAAHKVRELCENLPTEGRETVIMNQILPYIKELVSDTNQHVKSALASVIMGLSTVLGKENTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATNNLMKLVQKFGTEWAQNTIVPKVLVMANDPNYLHRMTTLFCINALSEACGKEITTKQMLPIVLKMAGDQVANVRFNVAKSLQKIGPILDTNALQGEVKPVLQKLGQDEDMDVKYFAQEAISVLALA | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with IPO9 (By similarity). Interacts with SGO1 (By similarity). Interacts with RAF1 (By similarity). Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. Belongs to the phosphatase 2A regulatory subunit A family. |
Q9FX65 | MSMVDEPLYPIAVLIDELKNDDIQRRLNSIKRLSIIARALGEERTRKELIPFLSENNDDDDEVLLAMAEELGGFILYVGGVEYAYVLLPPLETLSTVEETCVREKAVDSLCRIGAQMRESDLVEHFTPLAKRLSAGEWFTARVSACGIFHIAYPSAPDVLKTELRSIYGQLCQDDMPMVRRAAATNLGKFAATIESAHLKTDIMSMFEDLTQDDQDSVRLLAVEGCAALGKLLEPQDCVAHILPVIVNFSQDKSWRVRYMVANQLYELCEAVGPEPTRTDLVPAYARLLCDNEAEVRIAAAGKVTKFCRILNPELAIQHILPCVKELSSDSSQHVRSALASVIMGMAPVLGKDATIEHLLPIFLSLLKDEFPDVRLNIISKLDQVNQVIGIDLLSQSLLPAIVELAEDRHWRVRLAIIEYIPLLASQLGVGFFDEKLGALCMQWLQDKVHSIREAAANNLKRLAEEFGPEWAMQHIVPQVLEMINNPHYLYRMTILRAVSLLAPVMGSEITCSKLLPAVITASKDRVPNIKFNVAKMMQSLIPIVDQAVVENMIRPCLVELSEDPDVDVRYFANQALQSIDNVMMSS | The A subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Involved during developmental process such as seedling and floral developments. Seems to act as a negative regulator of PP2A catalytic activity. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (subunit A), that associates with a variety of regulatory subunits such as subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) (By similarity). Interacts with CHIP (PubMed:16640601). Interacts with SRK2E/OST1 (PubMed:26175513). A number of isoforms are produced. According to EST sequences. Expressed ubiquitously at stable levels. However, higher protein levels in roots and flowers (at protein level). Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure (By similarity). Ubiquitinated. CHIP-mediated ubiquitination enhances phosphatase activity after an abiotic stress such as low temperature or darkness. Due to the stability of its transcription, PubMed:16166256 proposed this gene as a reference gene for transcript normalization. Belongs to the phosphatase 2A regulatory subunit A family. |
G5EDR3 | MVMEVDEPAVAATTSQNQPQEHANDFDMDTSEGPIENDETFEPVDQINWKFNQVKGNIDADVHTEADVISCVEFSHDGEYLATGDKGGRVVIFQRDQSGKYVKGVRSREYNVYSTFQSHEPEFDYLKSLEIDEKINQIRWLKKKNAANFILSTNDKTIKLWKISERERKIGDDAWNLPRTNRINTSSFRGRLQIPSIVPMELIVEASPRRVYGNAHTYHVNSISVNSDQETFLSADDLRVNLWNLEITNESFNIVDIKPANMEELTEVITAAEFHPTQCNWFVYSSSKGSIRLCDMRDRALCDAYAKIFEEPEDPQSRSFFSEIIASVSDVKFSHNGRYLLTRDYLTVKVWDLNMESQPVETYPVHNYLRTKLCALYENDSIFDKFECDWSGDDKHILTGSYHNLFRSYARGNNQDAKTWEARPQEPHSQLRSRFVVPSAKRKRNNLSSSGETTEEDLSSDQLQFDRKILHTAWHPKDNIIALAATNNLYIFSDV | Probable regulatory subunit of serine/threonine phosphatase let-92. Together with let-92 and constant regulatory subunit paa-1, positively regulates centriole duplication during early embryonic cell divisions by preventing the degradation of sas-5 and kinase zyg-1 (PubMed:21497766). In addition, during vulva development, may play a role with phosphatase let-92 and regulatory subunit paa-1 in the induction of vulva cell precursors by positively regulating let-60/Ras-MAP kinase signaling, probably by promoting lin-45 activation (PubMed:10521400, PubMed:14724126). In intestinal epithelial cells, may play a role in the late secretory pathway probably by regulating the exocyst, a protein complex involved in targeting secretory vesicles to the plasma membrane (PubMed:24192838). Part of a complex consisting of a common heterodimeric core enzyme, composed of catalytic subunit let-92 and constant regulatory subunit paa-1, that associates with a variety of regulatory subunits which confer distinct properties to the holoenzyme (Probable). Interacts with let-92 (PubMed:21497766). RNAi-mediated knockdown causes severe embryonic lethality (PubMed:10521400). In mutants, during the first embryonic divisions, P1 cell initiates division prior to AB cell, spindles appear abnormal or collapse during anaphase and chromatin bridges and supernumerary centrosomes are often detected (PubMed:14724126). In addition, RNAi-mediated knockdown causes a partial defect in centriole duplication during the first embryonic divisions where 24% of spindles are monopolar and 47% have asymmetric spindles, a decrease in the spindle protein sas-5 levels and occasional bridging of chromatin with no obvious defects in cell cycle progression or mitotic exit (PubMed:21497766). The few surviving animals of RNAi-mediated knockdown lack a vulva resulting from defects in vulva cell induction, vulva precursor cell (VPC) generation and in vulval execution lineage, and are slightly uncoordinated (PubMed:10521400). In L4 larvae mutants, somatic mpk-1/ERK phosphorylation is also severely reduced (PubMed:14724126). In intestinal epithelial cells, RNAi-mediated knockdown causes an accumulation of SNARE proteins including snb-1, snap-29 and syx-4 (PubMed:24192838). RNAi-mediated knockdown at the L1 larval stage in the exocyst component exoc-8 (ok2523) mutant background results in lethality (PubMed:24192838). Belongs to the phosphatase 2A regulatory subunit B family. |
Q9XGR4 | MEIDGGNDVQILDPELLQLPGLSPVSLKENPHIAEELFSQWLSLPETGRLVKSLIDDTKSSTPVSVSKNCTSLNVACGSALPSVFLNSGTPPLSPRGSPGSPRFSRQKTSPSLQSPLKSVREPKRQLIPQFYFQHGRPPAKELREQCISMVDQFFSNYIDGLHMDEFKSITKEVCKLPSFLSSVLFRKIDTSGTGIVTRDAFIKYWVDGHMLAMDVASQIYNILRQPGCKYLRQADFKPVLDELLTTHPGLEFLRNTPEFQERYAETVIYRIFYYINRSGTGCITLRELKRGNLITAMQQVDEEDDINKVIRYFSYEHFYVIYCRFWELDGDHDFLIDKENLIKYGNHALTYRIVDRIFSQVPRKFTSKVEGKMSYEDFAYFILAEEDKSSEPSLEYWFKCIDLDGDGVITPNEMQFFYEEQLHRMECITQEPVLFEDILCQIFDMIKPEKENCITLQDLKASKLSGNIFNILFNLNKFMAFETRDPFLIRQERENPTLTEWDRFAQREYVRLSMEEDVEEVSNGSADVWDEPLESPF | Regulatory subunit of type 2A protein phosphatase. Not involved in HMGR regulation in seedlings grown in standard medium, but negatively regulates root growth in response to salt. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) and cell signaling molecules. Interacts with HMGR1L and HMGR1S (via N-terminus), but not with HMG2. Interacts with PP2AA1. No visible phenotype. |
Q940C6 | MVDTVIPGDMACLDADLLQLQEMSSFVLNSKPGFTQKLFDQWLSLPEAQRQVGSLLKDAVAGAPINVTGSASGSNSATIPSMFPAGSAPPLSPRSCGSPRTTKQRAPSNLGSTLKVVNEPVKEPIPQFYFQNGRPPPSEIKEQCMFRINHFFYGHMDGLQIQEFKLVTREICKLPSFFSTSLFRKIDLNNTGFVTRDAFIDFWVNGNMLIMDTTTQIFKILKQKDQSFIVKDDFKPLLKELLATHPGLEFLQSTPEFQERYAETVTYRIFYYINRSGNGRITFRELKRGNLIDAMLHADEEEDINKVLRYFSYEHFYVIYCKFWELDTDHDFLIDKENLMRYGNHALTYRIVDRIFSQVARKFTSKVEGKMGYEDFVYFILAEEDKSSVPSLEYWFKCIDLDANGIITRNEMQFFYEEQLHRMECMAQEAVLFEDILCQMIDMIGPENESHITLHDLKGSKLSGNVFNILFNLNKFMAFETRDPFLIRQERENPTLTDWDRFAHREYIRLSMEEDVEDASNGSAEVWDDSSLEAPF | Regulatory subunit of type 2A protein phosphatase. Involved in post-transcriptional regulation of HMGR but not in root growth regulation in response to salt. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) and cell signaling molecules. Interacts with HMGR1L and HMGR1S (via N-terminus), but not with HMG2. Interacts with PP2AA1. No visible phenotype. Truncated N-terminus. |
Q9V8M6 | MSLRVMSPAMLNAWSQTLVRAMSTQGGAKNIGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDASYDEMTADGVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHCGVYGMGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDANVFAEIINSSTGRCWASEIYNPVPGVCPSAPANRDYAGGFSSALITKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVVYDLMKKEKFSV | 3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. Extended N-terminus. |
Q9UDN3 | MAASLRLLGAASGLRYWSRRLRPAAGSFAAVCSRSVASKTPVGFIGLGNMGNPMAKNLMKHGYPLIIYDVFPDACKEFQDAGEQVVSSPADVAEKADRIITMLPTSINAIEAYSGANGILKKVKKGSLLIDSSTIDPAVSKELAKEVEKMGAVFMDAPVSGGVGAARSGNLTFMVGGVEDEFAAAQELLGCMGSNVVYCGAVGTGQAAKICNNMLLAISMIGTAEAMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMDGVPSANNYQGGFGTTLMAKDLGLAQDSATSTKSPILLGSLAHQIYRMMCAKGYSKKDFSSVFQFLREEETF | 3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Homodimer. Detected in skin fibroblasts. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. |
P86199 | TPVGFIGLGNMGNPMAKADRIITMLPSSMNSIEVYSGANGILKEVEKMGAVFMDAPVSGGVGAARICNNMLLAISMIGTAEAMNLGIRDLGLAQDSATSTKTPILLGSVAHQIYRDFSSVFQYLREEETF | 3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Homodimer. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. |
Q8BJY2 | MAASLGFRGAASGLWYWSGRRRPVGSLAAVCSRSMASKTPVGFIGLGNMGNPMAKNLMKHGYPLILYDVFPDVCKEFKEAGEQVASSPAEVAEKADRIITMLPSSMNAVEVYSGANGILKKVKKGSLLIDSSTIDPSVSKELAKEVEKMGAVFMDAPVSGGVGAARSGNLTFMVGGVEDEFAAAQELLECMGSNVVYCGAVGTGQSAKICNNMLLAISMIGTAEAMNLGIRSGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMHGVPSSNNYQGGFGTTLMAKDLGLAQDSATSTKTPILLGSLAHQIYRMMCSKGYSKKDFSSVFQYLREEEPF | 3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Homodimer. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. |
Q5R5E7 | MAASLRLLGAASGLRYWSRRLRPAAGSFAAVCSRSVASKTPVGFIGLGNMGNPMAKNLMKHGYPLIIYDVFPDACKEFQDAGEQVVSSPADVAEKADRIITMLPTSINAIEAYSGANGILKKVKKGSLLIDSSTIDPAVSKELAKEVEKMGAVFMDAPVSGGVGAARSGNLTFMVGGVEDEFAAAQELLGCMGSNVVYCGAVGTGQAAKICNNMLLAISMIGTAEAMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMDGVPSANNYQGGFGATLMAKDLGLAQDSATSTKSPILLGSLAHQIYRMMCAKGYSKKDFSSVFQFLREEETF | 3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Homodimer. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. |