in the present invention , a dna having the nucleotide sequence coding for the precursor protein of human pacap38 or mature pacap38 and for a promoter of human pacap38 can be prepared , for example , by the following process : ( i ) human cell dna is extracted and treated with restriction enzyme such as ecori or sali , and is introduced into a phage or a plasmid ; ( ii ) the recombinant phage or plasmid thus obtained is introduced into an appropriate host cell to produce a transformant ; ( iii ) after cultivation of the transformant thus obtained , the plasmid or the phage containing the desired dna is isolated from the transformant by an appropriate method such as hybridization with a dna probe coding for a portion of pacap38 ; and ( iv ) the desired cloned dna is cut out from the recombinant dna . methods for cloning the pacap38 dna from the human dna library include , for example , the plaque hybridization method [ t . maniatis et al ., molecular cloning , cold spring harbor laboratory ( 1982 )] using as a probe an oligonucleotide chemically synthesized reflecting phage vector λgt11 or embl and the amino acid sequence of pacap38 , or the cdna of pacap38 . the pacap38 cdna thus cloned is subcloned to a plasmid such as pbr322 , puc12 , puc13 , puc18 , puc19 , puc118 , puc119 or the like to obtain the human pacap38 dna , if necessary . the nucleotide sequence of the dna thus obtained is determined , for example , by the maxam - gilbert method [ a . m . maxam and w . gilbert , proc . natl . acad . sci ., u . s . a . 74 , 560 ( 1977 )] or the dideoxy method [ j . messing et al ., nucleic acids research 9 , 309 ( 1981 )], and the existence of the human pacap38 dna is confirmed in comparison with the known amino acid sequence . as described above , the dna ( fig2 seq id no : 1 ) containing a dna fragment coding for a portion of the precursor protein of human pacap38 is obtained . the restriction enzyme fragment map of the dna coding for the precursor protein of human pacap38 is shown in fig1 . the nucleotide sequence of the dna determined by the dideoxy method and the amino acid sequence deduced from that nucleotide sequence are shown in fig2 . a dna coding for a precursor protein of human pacap38 cloned as described above is compared with a cdna of human pacap38 previously cloned , and then the relationship of introns and exsons of the gene is determined and a promoter region essential for an expression of the gene is deduced . a dna sequence essential as a promoter is determined from the portion which covers a promoter region of human pacap38 . for example , a region containing a dna sequence of seq id no : 3 can be used as the promoter . the promoter can be obtained from phpr10neo obtainable from the transformant , escherichia coli mv1184 / phpr10 neo ( ferm bp - 4084 ) according to a method of example 3 . a dna fragment having a dna sequence of the promoter of the present invention can be synthesized using the phosphoamidide method using standard dna synthesizing equipment ( applied biosystems co . ltd .). the plasmids into which the dna is introduced include , for example , pbr322 [ gene 2 , 95 ( 1977 )], pbr325 [ gene 4 , 121 ( 1978 )], puc12 [ gene 19 , 259 ( 1982 )] and puc13 [ gene 19 , 259 ( 1982 )], each derived from escherichia coli , and pub110 derived from bacillus subtilis [ biochemical and biophysical research communication 112 , 678 ( 1983 )]. however , any other plasmid can be used as long as it is replicable and viable in the host . the phage vectors into which the dna is introduced include , for example , λgt11 [ r . young and r . davis , proc . natl . acad . sci ., u . s . a . 80 , 1194 ( 1983 )] and embl3 [ prischauf et al ., j . mol . biol . 170 , 827 ( 1983 )]. however , any other phage vector can be used as long as it is replicable and viable in the host . methods for introducing the dna into the plasmid include , for example , the method described in t . maniatis et al ., molecular cloning , p . 239 , cold spring laboratory , ( 1982 ). methods for introducing the dna into the phage vector include , for example , the method of t . v . hyunh et al . [ dna cloning , a practical approach 1 , 49 ( 1985 )]. the plasmid thus obtained is introduced into the appropriate host cells such as escherichia and bacillus . examples of escherichia described above include escherichia coli k12dh1 [ proc . natl . acad . sci . u . s . a . 60 , 160 ( 1968 )], m103 [ nucleic acids research 9 , 309 ( 1981 )], ja221 [ journal of molecular biology 120 , 517 , ( 1978 )], hb101 [ journal of molecular biology 41 , 459 ( 1969 )] and c600 [ genetics 39 , 440 ( 1954 )]. examples of bacillus described above include bacillus subtilis mi114 [ gene 24 , 255 ( 1983 )] and 207 - 21 [ journal of biochemistry 95 , 87 ( 1984 )]. methods for transforming the host with the plasmid include , for example , the calcium chloride method and the calcium chloride / rubidium chloride method described in t . maniatis et al ., molecular cloning , p . 249 , cold spring harbor laboratory , ( 1982 ). when the phage vector is used , for example , the phage vector can be transduced into proliferated e . coli , using the in vitro packaging method . in the present invention , an expression vector containing a dna having the nucleotide sequence coding for the precursor protein of human pacap38 , mature pacap38 or other protein can be prepared , for example , by the following process : ( i ) human cell dna is extracted and treated with restriction enzyme such as ecori or sali , and is introduced into a phage or a plasmid ; ( ii ) the recombinant phage or plasmid thus obtained is introduced into an appropriate host cell to produce a transformant ; ( iii ) after cultivation of the transformant thus obtained , the plasmid or the phage containing the desired dna is isolated from the transformant by an appropriate method such as hybridization with a dna probe coding for a portion of pacap38 ; ( iv ) the desired cloned dna is cut out from the recombinant dna ; and ( v ) the cloned dna or a portion thereof is ligated downstream from a promoter in a vector suitable for expression , whereby an expression vector can be obtained . expressible proteins other than pacap38 , include nerve cell - derived proteins such as neuro growth factor ( ngf ), brain derived neurotrophin - 3 ( bdnt - 3 ) and etc . in obtaining a structural gene to be expressed , plasmids into which a dna is incorporated , incorporation methods , hosts , transformation methods which are similar with the above - described ones can be used . the region intended to be expressed is cut out from the cloned dna and ligated downstream from the promoter in a vehicle ( vector ) suitable for expression , whereby the expression vector can be obtained . the dna has atg as a translation initiating codon at the 5 &# 39 ;- terminus thereof and may have taa , tga or tag as a translation terminating codon at the 3 &# 39 ;- terminus . further , a consensus sequence reactive to cyclic amp is observed upstream from atg of the 5 &# 39 ;- terminus . these translation initiating codons and translation terminating codon may be added by use of an appropriate synthetic dna adaptor such as adaptor containing a translation initiating codon atg or a translation terminating codon taa , tag or tga . the vectors include the above plasmids derived from e . coli such as pbr322 , pbr325 , puc12 and puc13 , plasmids derived from bacillus subtilis such as pub110 , ptp5 and pc194 , plasmids derived from yeast such as psh19 and psh15 , bacteriophages such as λ phage , and animal viruses such as retroviruses and vaccinia viruses . as a promoter , a promoter of the present invention containing a dna sequence of seq id no : 3 can be used . the promoter can be obtained from phpr10neo obtainable from the transformant , escherichia coli mv1184 / phpr10 neo ( ferm bp - 4084 ) according to a method of example 3 . further , phpr9 . 5neo , phpr8 . 8neo , phpr8 . 1neo , phpr4 . 9neo , phpr4 . 1neo and phpr2 . 6neo as shown in fig5 can also be used . when the host is an animal cell , a sv40 - derived promoter , a retrovirus promoter , a metallothionein promoter , a heat shock promoter or the like can be used . the use of an enhancer such as an sv40 - derived enhancer , a retrovirus - derived enhancer , is also effective for expression . by using a vector containing the dna coding for the precursor protein of human pacap38 , the mature peptide pacap38 or other protein thus constructed , the transformant is prepared . hosts for transformants include escherichia and bacillus described above , and animal cells . examples of the animal cells include monkey cell cos - 7 , vero , chinese hamster cell ( cho ), mouse l cell , human fl cell and human nerve cell 1mr - 32 . the transformation of escherichia described above is conducted , for example , according to the method described in proc . natl . acad . sci . u . s . a ., 69 , 2110 ( 1972 ), gene , 17 , 107 ( 1982 ) or the like . the transformation of animal cells is carried out , for example , according to the method described in virology , 52 , 456 ( 1973 ). thus , the transformant transformed with the expression vector containing the dna coding for the precursor protein of human pacap38 or the mature peptide ( pacap38 ) is obtained . when the animal cell transformants are cultivated , examples of the media which can be used include mem medium containing about 5 to 20 % fetal calf serum [ science , 122 , 501 ( 1952 )], dmem medium [ virology , 8 , 396 ( 1959 )], rpmi1640 medium [ the journal of the american medical association , 199 , 519 ( 1967 )] and 199 medium [ proceeding of the society for the biological medicine , 73 , 1 ( 1950 )]. the ph is preferably about 6 to about 8 . the cultivation is usually carried out at about 30 ° to 40 ° c . for about 15 to about 60 hours , with aeration or agitation if necessary . the gene product accumulated in a culture broth can be isolated and purified from the culture broth , for example , by the following method . the collected cells are suspended in an appropriate buffer solution and disrupted by lysozyme such as zymolyace ( kirin beer co . ltd ) and / or mechanical disruption method using glass beads , and the desired substances are extracted . the buffer solution may contain a protein denaturant such as urea or guanidine hydrochloride , or a surface - active agent such as triton x - 100 for easier extraction . the isolation and purification of the human pacap38 precursor protein , mature peptide or other proteins contained in the culture supernatant or the exctracted solution thus obtained can be performed by an appropriate combination of isolating and purifying methods known in the art . the known isolating and purifying methods include methods utilizing solubility such as salt precipitation and solvent precipitation , methods mainly utilizing a difference in molecular weight such as dialysis , ultrafiltration , gel filtration and sds - polyacrylamide gel electrophoresis , methods utilizing a difference in electric charge such as ion - exchange column chromatography , methods utilizing specific affinity such as affinity chromatography , methods utilizing a difference in hydrophobicity such as reverse phase high performance liquid chromatography and methods utilizing a difference in isoelectric point such as isoelectro - focussing electrophoresis . examples of the purification methods for proteins such as pacap include a method described in biochemical and biophyrical research communications , 164 ,, no . 1 , p . 567 - 574 ( 1989 ). a system having a promoter of the present invention can express proteins specific to nerve cells or can be used to screen proteins specific to nerve cells . further , using an induction substance ( chemical substance ) for the pacap gene , the amount of pacap produced can be determined , for example , by the use of the sandwich eia method . furthermore , by using this assay system , it is possible to screen for chemical substances , e . g ., drugs that are necessary for , or increase , production of pacap . substances showing promise during screening may be then given to experimental animals to understand their action , particularly on brain functions , more particularly on brain functions due to hormones . moreover , the information thus obtained provides information which serves to elucidate human brain functions . such induction substances can also be screened in an assay using the promoter of the present invention operably linked in a vector to a gene encoding a marker protein such as chloramphenicol acetytransferase ( cat ). other suitable marker proteins include luciferase and alkaline phosphatase . host cells , such as imr - 32 cells , are transformed with the vector using standard precedures . the resulting transformed cells are then exposed to a pre - determined induction substance , such as a drug or chemical , and the level of marker protein production is measured using methods standard for each marker . substances capable of inducing or increasing marker protein expression can then be further evaluated . the above methods may also be used to screen for substances that inhibit or decrease pacap or marker protein expression . the system employing a promoter of the present invention can express effectively pacap38 . human pacap38 , including pacap27 , results in an increase in camp activity , and therefore can be utilized as therapeutic agents for growth and maintenance of human brain nerves . there were hereinbefore described in detail the cloning of the dna coding for human pacap38 , the preparation of the promoter activity expression vectors , the preparation of the transformants thereby , the production of a portion of human pacap38 and the mature peptides by use of the transformants , and the utility thereof . when the amino acids are capable of existing as optical isomers , it is understood that the l - forms are represented unless otherwise specified . when nucleotides , amino acids and so on are indicated by abbreviations in the specification and drawings , the abbreviations adopted by the iupac - iub commission on biochemical nomenclature or those commonly used in the art are employed . accordingly , the following abbreviations are used . with respect to the human pacap38 precursor proteins or the mature peptide of the present invention , a portion of the amino acid sequence may be modified , through addition , elimination of amino acid ( s ) or substitution with other amino acid ( s ). the present invention will be described in more detail with the following reference examples and examples . it is understood of course that these reference examples and examples are not intended to limit the scope of the invention . transformants e . coli mv1184 / phgp2312 and mv1184 / phgp2306 obtained in example 2 described below were deposited with the fermentation research institute , the agency of industrial science and technology , the ministry of international trade and industry , japan ( fri ) under the accession number ferm bp - 3054 on aug . 10 , 1990 , and under the accession number ferm bp - 3033 on jul . 30 , 1990 , respectively . these microorganisms were also deposited with the institute for fermentation , osaka , japan ( ifo ) under the accession numbers ifo 15068 and ifo 15067 , respectively , on jul . 24 , 1990 . transformant e . coli mv1184 / pgpr10neo in example 3 described below was deposited with fri under the accession number ferm bp - 4084 on nov . 26 , 1992 . the amino acid sequence of sheep pacap38 is believed to be identical to that of human pacap38 . when pacap38 purified from sheep hypothalami ( hereinafter , &# 34 ; nat . 38p &# 34 ;) and synthesized pacap38 ( hereinafter , &# 34 ; syn . 38p &# 34 ;) were allowed to act on rat pituicytes in vitro , an increase in adenylate cyclase activity was identified by observing an increase of camp observed . the result is shown in table 1 . the minimum effective amount was 10 - 12 m , and it was shown that the activity increased with increasing concentration . further , similar activity was also observed for synthesized 27 - nh 2 , the amino acids situated in the 132nd to 158th positions of fig2 ( hereinafter , &# 34 ; syn . 27p - nh 2 &# 34 ;). in contrast , a similar increase in activity could not be observed for a synthesized porcine vasoactive intestinal polypeptide ( hereinafter , syn . pvip ). table 1______________________________________adenylate cyclase stimulating test in rat pituicyte culture camp p mol / ml ( m ± sem ) ______________________________________experiment 1syn . pvip 10 . sup .- 12 m 1 . 35 ± 0 . 05syn . pvip 10 . sup .- 11 m 1 . 40 ± 0 . 00syn . pvip 10 . sup .- 10 m 1 . 45 ± 0 . 15syn . pvip 10 . sup .- 9 m 1 . 75 ± 0 . 05syn . pvip 10 . sup .- 8 m 2 . 55 ± 0 . 25syn . pvip 10 . sup .- 7 m 3 . 30 ± 0 . 20control ( blank ) 1 . 55 ± 0 . 15experiment 2syn . 27p - nh . sub . 2 10 . sup .- 12 m 2 . 05 ± 0 . 15syn . 27p - nh . sub . 2 10 . sup .- 11 m 2 . 55 ± 0 . 15syn . 27p - nh . sub . 2 10 . sup .- 10 m 4 . 00 ± 0 . 20syn . 27p - nh . sub . 2 10 . sup .- 9 m 7 . 90 ± 0 . 30syn . 27p - nh . sub . 2 10 . sup .- 8 m 9 . 20 ± 0 . 00syn . 27p - nh . sub . 2 10 . sup .- 7 m 9 . 20 ± 0 . 20syn . 38p 10 . sup .- 12 m 2 . 15 ± 0 . 05syn . 38p 10 . sup .- 11 m 3 . 05 ± 0 . 35syn . 38p 10 . sup .- 10 m 4 . 60 ± 0 . 20syn . 38p 10 . sup .- 9 m 6 . 20 ± 0 . 10syn . 38p 10 . sup .- 8 m 8 . 60 ± 0 . 20syn . 38p 10 . sup .- 7 m 8 . 70 ± 0 . 20nat . 38p 10 . sup .- 12 m 1 . 50 ± 0 . 10nat . 38p 10 . sup .- 11 m 1 . 75 ± 0 . 05nat . 38p 10 . sup .- 10 m 2 . 60 ± 0 . 10nat . 38p 10 . sup .- 9 m 4 . 60 ± 0 . 00nat . 38p 10 . sup .- 8 m 8 . 05 ± 0 . 35control ( blank ) 1 . 35 ± 0 . 05______________________________________ the materials used in reference example 1 were similarly allowed to act on rat pituicytes in vitro . as a result , the releasing activity of prolactin ( prl ), acth and gh was confirmed therein . the cdna of cloned human pacap38 was labelled by the random prime method using 32 p - dctp for use in screening of the human genomic dna library . isolation of human pacap genomic dna and determination of nucleotide sequence thereof e . coli le392 was infected with a human leukocyte - derived dna library ( clontech laboratories , inc ., catalog no . hl1006d ) and plated to cause phage plaques to appear . a portion of plaque dna was transferred to a nitrocellulose film according to the method of w . benton and r . davis [ science 196 , 180 - 182 ( 1977 )] and hybridized with the cdna probe labeled with 32 p in example 1 . hybridization was carried out in the absence of formaldehyde at 60 ° c . clones positive to hybridization were isolated . then , a cdna portion of λhgp23 , which was one of the clones described above , was cut out with sali and recloned into the sali site of plasmid puc18 to prepare plasmids phgp2312 and phgp2306 . by transforming e . coli mv1184 with these plasmids , transformants e . coli mv1184 / phgp2312 ( ferm bp - 3054 ) and e . coli mv1184 / phgp2306 ( ferm bp - 3033 ) were obtained . the cdna portions included in these plasmids were 11 . 1 kbp and 6 kbp , respectively . the simplified restriction enzyme maps thereof are shown in fig1 . in the figure , black box () shows a mature human pacap38 code region . the nucleotide sequence of this dna portion was determined by the method of sanger [ proc . natl . acad . sci . u . s . a . 74 , 5463 - 5467 ( 1977 )]. this nucleotide sequence is shown in fig2 . the region from amino acid nos . 132 to 169 is the mature peptide portion of human pacap38 . referring to fig2 the 7540th to 7650th nucleotides form the first exon , which codes for amino acid residues m ( 1 ) to r ( 37 ) in the lower row . the amino acid numbers are designated in parentheses . the 9814th to 9945th nucleotides form the second exon , which codes for amino acid residues p ( 38 ) to r ( 81 ). the 10421st to 10519th nucleotides form the third exon , which codes for amino acid residues d ( 82 ) to g ( 114 ). the 11602nd to 11787th nucleotides form the fourth exon , which codes for amino acid residues g ( 115 ) to l ( 176 ). analysis of the genomic dna revealed that the precursor of human pacap38 consisted of 176 amino acid residues ( seq id no : 2 ). plasmid phgp 2312 into which 5 &# 39 ;- region of a genomic dna of the cloned human pacap had been incorporated was digested with ecori and eco47iii to obtain a dna fragment of 2 . 5 kb ( 4646 to 7159 nucleotides ). the dna fragment was inserted into puc118 at the sites of ecori and smai . a terminater of sv40 of 519 bp ( to 0 . 52 kbp ) was incorporated at the sites of bamhi and sali of the above described plasmid , and then a gene of chloramphenicol acetytransferase was incorporated into bamhi site of the plasmid . a dna fragment ( pmcineo . polya , stragene , usa ) which has a promoter of thymidine kinase and a polya signal . neomycin resistance gene was linked at sali site of the above - described plasmid to construct a plasmid of fig3 . fig3 shows a plasmid into which a 2 . 5 kb of pacap gene . the plasmids which have each 2 . 2 kb , 1 . 5 kb and 1 kb of pacap gene were named phpr22neo , phpr15neo . and phpr10neo , respectively . each 50 μg of the purified plasmids was applied to imr - 32 cells , neuroblastoma , grown up in a petri dish of 9 cm diameter with calcium phosphate method ( graham , pl1973 , virology 52 , 456 - 457 ), which were cultivated in eagles &# 39 ; mem ( emem ) medium with 10 % serum containing 0 . 5mg / ml of g418 . the survived cells were further cultivated . the cat assay according to gorman et al ( mol . cell . biol ., 2 , 1044 ) was used . each plasmid was applied to imr - 32 cells and cat produced in the cells was assayed . the results are shown in fig4 . the black bands indicated by an arrow show cat amount expressed . the stronger the black is , the more cat is expressed , which means stronger promoter activity . plasmids into which dna fragments of 2 . 5 kb to 1 . 0 kb of pacap were incorporated respectively were found to produce cat . among them , the plasmid which has a 1 kb fragment had the highest activity and a promoter on the gene of human pacap was shown to be located in a 17 kb nucleotide sequence of 6143rd to 7159th previously cloned . a plasmid into which a further shortened pacap gene was incorporated was constructed and the resulting plasmid was applied to imr - 32 cells to assay cat produced . the plasmid phprneo6 . 6 ( 657 bp , 6503rd to 7159th nucleotides )( seq id no : 3 ) had the highest activity as shown in fig5 . the above results show that the promoter region is located in an ecori to eco47iii region of the pacap gene ( 4644th to 7159th nucleotides ). the promoter region deduced from the results can be used for an expression system utilizing nerve cells . pacap38 nh 2 was synthesized by using 1 . 04 g ( 0 . 5 mmole ) of a commercially available p - methyl bha resin ( applied biosystems inc ., california usa ) and a peptide synthesizer ( model 430a , applied biosystems inc .). a starting amino acid , boc - lys ( cl - z ), was activated with hobt / dcc and then condensed to the resin . thereafter , the boc group on the resin was treated with 50 % trifluoroacetic acid / methylene chloride to deprotect the amino group . to this free amino group , the following protected amino acids activated with hobt / dcc were reacted in turn according to the amino acid sequence of pacap3 : after the completion of each reaction , the residual amino groups were acetylated with acetic anhydride to obtain 2 . 42 g of a protected pacap38 nh 2 resin . 0 . 51 g of the resulting protected pacap38 nh 2 resin was treated with 5 ml of hydrogen fluoride in the presence of 0 . 6 g of p - cresol at 0 ° c . for 60 minutes , followed by removal of excess hydrogen fluoride by distillation under reduced pressure . the treated resin was washed twice with 5 ml of ethyl ether , and then extracted with 6 ml of 50 % aqueous acetic acid . the insoluble material was removed by filtration and washed with 5 ml of 50 % aqueous acetic acid . the filtrate and the washings were combined , and the combined solution was concentrated under reduced pressure to 2 to 3 ml . the concentrated solution was applied to a sephadex lh - 20 column ( 2 × 90 cm ) for elution with 50 % acetic acid . the main fractions were collected , and then removed by distillation under reduced pressure . then , the residue was dissolved in 100 ml of 0 . 1 % aqueous trifluoroacetic acid . the resulting solution was subjected to a ymc - ods am120 s - 50 resin column ( 2 . 6 × 7 cm ) and eluted by a linear gradient of 0 . 1 % aqueous trifluoroacetic acid and 50 % acetonitrile containing 0 . 1 % trifluoroacetic acid . the main fractions were combined , followed by lyophilization . thus , 60 mg of a white powder was obtained . this powder was dissolved in 20 ml of 0 . 05m aqueous ammonium acetate . the resulting solution was subjected to a cm - cellulofine resin column ( 1 × 6 cm ) and eluted by a linear gradient of ammonium acetate from 0 . 05m to 1m . the main fractions were combined . the combined solution was subjected to a ymc - ods column ( 2 . 6 × 7 cm ) again and eluted by a linear gradient of from 0 % to 40 % aqueous acetonitrile containing 0 . 1 % trifluoroacetic acid . the fractions of 28 % to 30 % acetonitrile were collected , followed by lyophilization . 21 . 6 mg of a white powder was obtained . anal . of amino acids : a linear gradient elution from the eluent a to the eluent b for 50 minutes pacap27 nh 2 was synthesized by using 1 . 04 g ( 0 . 5 mmole ) of a commercially available p - methyl bha resin ( applied biosystems inc .) and a peptide synthesizer ( model 430a , applied biosystems inc .). a starting amino acid , boc - leu , was activated with hobt / dcc and then condensed to the resin . thereafter , the boc group on the resin was treated with 50 % trifluoroacetic acid / methylene chloride to deprotect the amino group . to this free amino group , the following protected amino acids activated with hobt / dcc were reacted in turn according to the amino acid sequence of pacap38 ( 1 - 27 ): boc - val , boc - ala , boc - leu , boc - tyr ( br - z ), boc - lys ( cl - z ), boc - met , boc - gln , boc - arg ( tos ), boc - ser ( bzl ), boc - asp ( obzl ), boc - thr ( bzl ), boc - phe , boc - ile and boc - his ( tos ) after the completion of each reaction , the residual amino groups were acetylated with acetic anhydride to obtain 2 . 31 g of a protected pacap27 nh 2 resin . 0 . 50 g of the resulting protected pacap27 nh 2 resin was treated with 5 ml of hydrogen fluoride in the presence of 0 . 6 g of p - cresol at 0 ° c . for 60 minutes , followed by removal of excess hydrogen fluoride by distillation under reduced pressure . the treated resin was washed twice with 5 ml of ethyl ether , and then extracted with 6 ml of 50 % aqueous acetic acid . the insoluble material was removed by filtration and washed with 5 ml of 50 % aqueous acetic acid . the filtrate and the washings were combined , and the combined solution was concentrated under reduced pressure to 2 to 3 ml . the concentrated solution was applied on a sephadex lh - 20 column ( 2 × 90 cm ) for elution with 50 % acetic acid . the main fractions were collected , followed by removal by distillation under reduced pressure . 129 mg of a white powder was obtained . this powder was dissolved in 5 ml of 0 . 1 % aqueous trifluoroacetic acid . the resulting solution was subjected to a tsk - gel ( ods - 120t ) column ( 21 . 5 × 300 mm ) and eluted with 27 % acetonitrile containing 0 . 1 % aqueous trifluoroacetic acid . the main fractions were collected , followed by lyophilization . 17 . 2 mg of a white powder was obtained . anal . for amino acids : a linear gradient elution from the eluent a to the eluent b for 50 minutes using male wistar rats having a body weight of 350 g under nembutal anesthesia , the hypotensive activity was measured . the value shows the decrease from normal value . the results are shown in table 2 . table 2______________________________________hypotensive activity of pacap dosage ( n mole / kg ) compound 0 . 3 1 . 0 3 . 0______________________________________pacap38 nh . sub . 2 3 . 2 ± 1 . 9 17 . 4 ± 2 . 4 29 . 8 ± 3 . 6 ( n = 6 ) ( n = 6 ) ( n = 6 ) pacap27 nh . sub . 2 14 . 5 ± 3 . 1 51 . 9 ± 9 . 6 4 . 1 ( n = 5 ) ( n = 5 ) ( n = 1 ) ______________________________________ unit : mm hg the following references , which are referred to for their disclosures at various points in this application , are incorporated herein by reference . __________________________________________________________________________sequence listing ( 1 ) general information :( iii ) number of sequences : 3 ( 2 ) information for seq id no : 1 :( i ) sequence characteristics :( a ) length : 17041 base pairs ( b ) type : nucleic acid ( c ) strandedness : double ( d ) topology : linear ( ii ) molecule type : dna ( genomic )( ix ) feature : ( a ) name / key : cds ( b ) location : join ( 7540 .. 7650 , 9814 .. 9945 , 10421 .. 10519 , 11602 .. 11787 )( xi ) sequence description : seq id no : 1 : gatcacgaggtcacgagatcgagaccatcctggccaacatggtgaaaccccatctctact60aaaaatacaaaaaatagctgggcatggtggcccatgcctgtagtcc cagctactcgggag120gctgaggcaggagaattgcttaaacccgggaagcggaggttgcagtgagccaagatcgca180ccactgcctcccagcctggtgatggagtgagactccatctcaaaaaaaaaaaaaaaaaat240tcctagagaaaataaatatg ccagtataacatattatagtcattaagactgtctggagtc300attgagacttgaatctgaagttcagcattacaatgtagcagctgtgtaactttggataag360gtacctgagctcttttagtcccgatttcttgtctgtaaaatggaggtaataacagtgcct4 20acaaagaagtttgttgtgagggaaaggaaataagtagtcaagcacttagcccaggaagtg480ttcattaaacagttgttgctgttgctgttattcactggtgaataacaaaaccatacagtc540cctttggaaggaaggatttaaaataatttaaacaaataa tcactaaaaatttcaaccagt600acatttatgacaaatgtaatagtattccaagcagatgatagtttttaaaaatttatgcct660gtgtatatttgggtagagacaaaggattatttaaaaagtattttcaggttgggcacactg720gctcatccttgca acccctgcactttgggaggcttgagtccaggagtttgtgaccagcct780gggcaacacagggagaccttgtctctgcaaagtaataataataacaataataataaataa840aattagccaggcatggtggtggcatgtgcctgtagtcccaggtattcaagaggttga ggc900aggagtctcacttaagcccaagagtttgaggttgctgtgagctatgaatgcactactgca960ctccagcctgggtgaccgaggaagactcagtaaaaacaaaacaaaacaaacaaacaaaca1020aaaactgcaaagccgtgattaccatacagtg ctagtaataatgataataaaaacaaaggc1080tccaaaattattacatgtaaacctatattcacaggtagataatgccaagcctgagcccaa1140agggaagagggatgctaggggctcacagaggaagaccttcttttgattttacacacaaaa1200accttg ttttattttgcatatagattccccttccaacattttctgaagtggtctcaaaag1260cttatttaggatattggttttcctggatcctgtccaagcttttccttctgcatttaagcc1320ttatgtcagcagaggatttagactaagtagagagaagactttcttctcct tggcttttta1380gaggaggtgctctggaatttggaagatgctacacagtgaagtctgggatatacatttttg1440gtacccagtaaactcatgttcagagaataaggccttagtagagccatatatgtgagatat1500ttggaatcatccaaacctgtagca aaggttagatcctggtttttgtttctcagatgtctg1560ctttatatctcaaaacaacaagcaaaatttcttggctctgtgaatatgcaattctgttct1620tagattagagagaagctttactcatgtggtttggaaggcttcctttcctagttgttttca1680gtgtgtgagaagcactacattttgaaggtcagagaagtcatgacacattataggtaagct1740catcagcttcttacttcacagtgagttctgaaaggcatgatgcatgcagtccagtaagtg1800atggtcatgatgttctggttcagaacatttgggtttccctac aggtgtaatcggtatgaa1860gtgagtcattagtcattgcattttctggaaaagtcggtagagaaaagtttaagtgaaatg1920taatacagtgttataattcacttttgtcactcacaggagaggatgatgttttgcatcagg1980cttgtttactgaaaaag cttattatagcctggttcttatgctaagtactggctaaaaaag2040aatagaatgtgccaggcacggtggctcacgcctgtaatcccattactttgaaaggctgag2100gcaggtggatcacaaggtcaggagttcgagaccagcctggcgaacacggtgaaactctgt 2160ctgtactaaaaatacaaaaattagcagggtgtggtggtgggtgcctgtagtcccagctgc2220ttgggaggctgagacaggagaatcacttgaacctgggaggcggaggtggcagtgagccga2280gattgtgccactgcactccagcctgggggacagag 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cctgagtcctgtgta13767taggatcaatcttcctttaattccgcagtctcctcaggcaatgtgacacgggatgcagtt13827tgcagctttagtgcctttcttcgccttttaaattgccacgaatcacagatggctatttag13887tggccctacaatgctgcaac acatcagcttgcattttagtcttaattatttgtttcttgg13947ataatgggcagagttttctgtatttgtatcgactgttagtggtgaaatagggctctagtt14007aaccttttatttatgaagtctaatttagtgttcccgtggctagttgcaagcattttacag14 067tgatcacccagtttaatcttttgtatactttttagaaatgccaagagccttactaaactg14127aagcagatttatgatatagtgataatttaggtagatgttagtcttgaagctcttattttg14187tgtgcaactgattataaaaacaccttaaccaagtatta ttacacacatgatatctataac14247taggactttgataactgttatataaagtgtgtaaaatttgtatgaataaatttttgtaaa14307caatgcaacttggtctaatgtttgggaaaaaagacattcaggaaataattactttaaaat14367ctcttaaagtat tatatttctttagcaaccataagatttttttacgtctggaatatatat14427ctatctaagcacccttgtattttcatgaactgcactttaataattgatgggcaactggat14487tctgctaaaaatttaaagtagctactcagatggagatgcctaagaaggttttaagc tcat14547aaacaggcatgatgttgcaacattataagacacacaatttagattaatttccatccccta14607gtgtgtatatactttgctcaatattcagaaagttactaggtagtagtgggagacaatgct14667ggagcattagttacacatctaaaatagcaa tctaacattgttcttttattttttatttta14727gtggccaggtctcactatgttgcccaggctggtcttgctcaagcgatcctcccacctcag14787cctcccaaagtgctgggattacaggcgtgagccaccacacccagcctaaaatagggatct14847aacat tgttcttatacaagtaactctgcagactaaacttgtcttgataaaattttgtata14907aaatgatctaaataatcagtttttggaggttttaaaatgtatttagagacatacaaacta14967ctgtctctgattaaaatgctttaggtagaaggaacgtgaacatgagtaa gtaaagagtta15027attagatgcctttaaaagaaaatgtactttgaagtccaggaagaaacacaagaagtcatt15087tgtggattgtatgctttcttagttcatatttacaaactttagggcaaagctttcatacga15147aattccttcaaattccgtagtgg tgtgtgttttggcacctttgactatttctggcttaga15207aaatgtatagaaagtcacacaataattgacataccatttaatttaaaatgccagggtttc15267atcctaaaaattaatggtctcaattagtaaatcaataaatatgttacgatagaattaaag15327gatgagtgaggattctaaaattatcttcagaatttagctcagtatttaaggcctagaatc15387aaatagggaggagcccacagtctagaaatcccgtttgtagtcaatgaaaaaatgaatcca15447gtacagttcatatttgcatttgattttattggataaggaat ttttcttctccatctttaa15507ctgcccctctttgtccttgaagacatagtgtggtagatgaaaaaatgaagaagactttat15567tcggttggggctaggctaatgacttgtcaagaacataaagataaaccccagacttggctg15627acttcaagtgaatttc atgtatttagcaacttgccatattatcttcggtgataactcaaa15687ttacatctttttaaaggcagacttgatacatatgggtattcaagaagctgtaataggtgc15747cttaatgctgttagggcggagaacacacttattcaatacaatgcacacttattgaacaca 15807tgaaatgggccaccgcactggtcgagagagcttgactaacacctgggagctcaggtagta15867tttttttcagaatgtttttctgaaatgtgatcatctttggggcggggggagcttaaaaat15927gcaaaattgtagggctctgccagatccagtgaat ctgcattttaaataaaaaccctagat15987tactgtgcactaaaatttgagactgcctagatttagaattggtgacatatgtaggcatac16047atatgtgctggtctgaatgtttttttcatatgaaataagcaaaaggtcatgttacctgca16107tacagtaat aaatacataactgtgccatattcttccaagatatctggtcattaagctctt16167tgacaatttcagtatttcctttaggtcactaaaactactagttagcattattttacttgt16227acagtctggttggacctctcctacaggagcttgtggaaggagagtgatcctc taagttgg16287gtccaaaatattcaatcacaggactaagagattatggctataatgaggagaacttgtgca16347gctagctagccataattctggggatccagaagtcaacttccagttgcattatatcccaat16407ttggtttgaatgtatttactgctcccc aactgtttacatgatggtttctcttggatggct16467cactatgaccttcaacccaaccctactgttcacatgatcacaagattggaagccaagatc16527aagtcatccctcttctcttttgttgccactcttttttgtagaagggagatgccagctgcc16587c ctgctgctgcagattgcatcactgctggattcttacattggtttgtagttggtcatcct16647ggtcacttcccctgcaaccacatagttttagctccatcttagtatcatgtccctctgatc16707agatgttccagagtagcttccattgtcaaagggttaaagggttta aggtaatcagtagtc16767aattttacctctctgttcttcaacacgatccttcctcttttttttgttttgagaaagggt16827cttactctgttgcccaggctggagtgcagtggcacgatctcggctcactgcaacctctgc16887ctcccgggtttaagcgattc tcctgtctcaacctcccgagtagctgggattacaggtgca16947tgccaacgcgcccggctaatttttgtatttttagtagagacggggtttcactgtgttggc17007caggctggtcttggactcttgtccccaaatgatc17 041 ( 2 ) information for seq id no : 2 :( i ) sequence characteristics :( a ) length : 176 amino acids ( b ) type : amino acid ( d ) topology : linear ( ii ) molecule type : protein ( xi ) sequence description : seq id no : 2 : metthrmetcysserglyalaargleualaleuleuvaltyrglyile1 51015ilemethisserservaltyrserserproalaalaalaglyleuarg202530pheproglyileargpro glugluglualatyrglygluaspglyasn354045proleuproasppheglyglysergluproproglyalaglyserpro5055 60alaseralaproargalaalaalaalatrptyrargproalaglyarg65707580argaspvalalahisglyileleuasnglualatyrarg lysvalleu859095aspglnleuseralaglylyshisleuglnserleuvalalaarggly100105110valglyglyserleuglyglyglyalaglyaspaspalagluproleu115120125serlysarghisseraspglyilephethraspsertyrserargtyr130 135140arglysglnmetalavallyslystyrleualaalavalleuglylys145150155160argtyrlysglnargvallys asnlysglyargargilealatyrleu165170175 ( 2 ) information for seq id no : 3 :( i ) sequence characteristics :( a ) length : 657 base pairs ( b ) type : nucleic acid ( c ) strandedness : double ( d ) topology : linear ( ii ) molecule type : dna ( genomic )( xi ) sequence description : seq id no : 3 : tgagaaaaaaaaaaaggaagtcatttcatgaataaaaatcggagcgcaacagtgcaacaa60aatattctgtacttaaaggcaacaggcaggcagatgttgacaaagagggctctccaaaaa120ccatgttcgg atagatttttgcgaactgcacagataaataggagcagaaggccggtcacc180tctgtaaccagcggtagcagcagcagaagccgcagcttcagaggcagccggagagacctc240ggagcagagaaggcgccgccgaccctcgcggctgcctggcccgcggctcctaca aaggcg300ggctagccgcccgccctctcccttgccttcctccccttcttttctgactttccctctttc360ccttaatcgcctgcttcttcctccgggtggacttacggccaccttgctcctccgcgcttc420acctcatcgccccctctttctttcttctg cctctctctctgcgcccccttctctccgtgt480cacgctccctcctggttctgcgcgtctacaaacttttgagcagaacacgagcctcggcaa540acgagtcccgcagctcctcctgctgctcccgctggttcctgcggcttctgctcagacacc600aac gccagacggcgatgcctctcgggtggtgactccagcgcaggaacttgaagaagc657