Hypothetical model of the<unk>  function<unk> s are a family of membrane proteins found in all multicellular eukaryotes.<unk> s, also referred to as the transmembrane 4 superfamily (TM4SF) proteins, have four transmembrane alpha-helices and two extracellular domains, one short (called the small extracellular domain or loop, SED/SEL or EC1) and one longer, typically 100 amino acid residues (the large extracellular domain/loop, LED/LEL or EC2). Although several protein families have four transmembrane alpha-helices,<unk> s are defined by conserved amino acid sequences including four or more cysteine residues in the EC2 domain, with two in a highly conserved 'CCG' motif.<unk> s are often thought to act as scaffolding proteins, anchoring multiple proteins to one area of the cell membrane.<unk> s are highly conserved between species. Some<unk> s can have N-linked glycosylations on the long extracellular loop (LEL, EC2) and palmitoylations at a CXXC motif in their transmembrane region. There are 34<unk> s in mammals, 33 of which have also been identified in humans.<unk> s display numerous properties that indicate their physiological importance in cell adhesion, motility, activation, and proliferation, as well as their contribution to pathological conditions such as metastasis or viral infection. A role for<unk> s in platelets was demonstrated by the bleeding phenotypes of CD151- and TSSC6-deficient mice, which exhibit impaired "outside-in" signalling through αIIbβ3, the major platelet integrin. it is hypothesized that<unk> s interact with and regulate other platelet receptors.
Tetraspanin
Peripherin
Dystrophin
Neurofilament light polypeptide
Apamin
Trabectome
Embelin
Retapamulin