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{
"metadata": {
"accession": "cd08376",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "cdd",
"member_databases": null,
"integrated": null,
"hierarchy": null,
"name": {
"name": "C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP)",
"short": "C2B_MCTP_PRT"
},
"description": [
{
"text": "<p>MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology. [[cite:PUB00081546], [cite:PUB00081547], [cite:PUB00005039], [cite:PUB00081548], [cite:PUB00035009], [cite:PUB00000918], [cite:PUB00035040], [cite:PUB00035039]]</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00035009": {
"PMID": 7791877,
"ISBN": null,
"volume": "375",
"issue": "6532",
"year": 1995,
"title": "Ca(2+)-dependent and -independent activities of neural and non-neural synaptotagmins.",
"URL": null,
"raw_pages": "594-9",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Li C",
"Ullrich B",
"Zhang JZ",
"Anderson RG",
"Brose N",
"Sudhof TC."
],
"DOI_URL": "http://dx.doi.org/10.1038/375594a0"
},
"PUB00035040": {
"PMID": 1589771,
"ISBN": null,
"volume": "256",
"issue": "5059",
"year": 1992,
"title": "Synaptotagmin: a calcium sensor on the synaptic vesicle surface.",
"URL": null,
"raw_pages": "1021-5",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Brose N",
"Petrenko AG",
"Sudhof TC",
"Jahn R."
],
"DOI_URL": "http://www.sciencemag.org/cgi/content/abstract/256/5059/1021"
},
"PUB00081548": {
"PMID": 8662510,
"ISBN": null,
"volume": "273",
"issue": "5272",
"year": 1996,
"title": "Bipartite Ca2+-binding motif in C2 domains of synaptotagmin and protein kinase C.",
"URL": null,
"raw_pages": "248-51",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Shao X",
"Davletov BA",
"Sutton RB",
"Sudhof TC",
"Rizo J."
],
"DOI_URL": "http://dx.doi.org/10.1126/science.273.5272.248"
},
"PUB00000918": {
"PMID": 7697723,
"ISBN": null,
"volume": "80",
"issue": "6",
"year": 1995,
"title": "Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold.",
"URL": null,
"raw_pages": "929-38",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Sutton RB",
"Davletov BA",
"Berghuis AM",
"Sudhof TC",
"Sprang SR."
],
"DOI_URL": "http://dx.doi.org/10.1016/0092-8674(95)90296-1"
},
"PUB00005039": {
"PMID": 8771209,
"ISBN": null,
"volume": "5",
"issue": "1",
"year": 1996,
"title": "Extending the C2 domain family: C2s in PKCs delta, epsilon, eta, theta, phospholipases, GAPs, and perforin.",
"URL": null,
"raw_pages": "162-6",
"medline_journal": "Protein Sci",
"ISO_journal": "Protein Sci.",
"authors": [
"Ponting CP",
"Parker PJ."
],
"DOI_URL": "http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=8771209&action=stream&blobtype=pdf"
},
"PUB00081547": {
"PMID": 8976547,
"ISBN": null,
"volume": "5",
"issue": "12",
"year": 1996,
"title": "The C2 domain calcium-binding motif: structural and functional diversity.",
"URL": null,
"raw_pages": "2375-90",
"medline_journal": "Protein Sci",
"ISO_journal": "Protein Sci.",
"authors": [
"Nalefski EA",
"Falke JJ."
],
"DOI_URL": "http://dx.doi.org/10.1002/pro.5560051201"
},
"PUB00081546": {
"PMID": 9632630,
"ISBN": null,
"volume": "273",
"issue": "26",
"year": 1998,
"title": "C2-domains, structure and function of a universal Ca2+-binding domain.",
"URL": null,
"raw_pages": "15879-82",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Rizo J",
"Sudhof TC."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.273.26.15879"
},
"PUB00035039": {
"PMID": 2333096,
"ISBN": null,
"volume": "345",
"issue": "6272",
"year": 1990,
"title": "Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C.",
"URL": null,
"raw_pages": "260-3",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Perin MS",
"Fried VA",
"Mignery GA",
"Jahn R",
"Sudhof TC."
],
"DOI_URL": "http://dx.doi.org/10.1038/345260a0"
}
},
"set_info": {
"accession": "cl14603",
"name": "C2"
},
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 4154,
"pathways": 0,
"proteins": 4154,
"proteomes": 925,
"sets": 1,
"structural_models": {
"alphafold": 3709,
"bfvd": 0
},
"structures": 0,
"taxa": 3359
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
