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{
"metadata": {
"accession": "IPR007810",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF05131": "Pep3/Vps18/deep orange beta-propeller domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR007810",
"name": "Pep3/Vps18, beta-propeller domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Pep3/Vps18, beta-propeller domain",
"short": "Pep3/Vps18_beta-prop"
},
"description": [
{
"text": "<p>This domain is found N-terminal in a number of proteins involved in Golgi function and vacuolar sorting Vps18 [[cite:PUB00161517], [cite:PUB00073490], [cite:PUB00161675], [cite:PUB00161676], [cite:PUB00097428]] and Pep3 [[cite:PUB00073491], [cite:PUB00062954]]. The molecular function of this region is unknown. Some proteins containing this domain also contain a C-terminal ring finger domain.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Vacuolar sorting protein 18 (Vps18) and Vacuolar membrane protein pep3 (Pep3) are involved in vesicle-mediated protein trafficking to lysosomal compartments, playing a crucial role in endocytic membrane transport and autophagic pathways. They act as a core component of the HOPS and CORVET endosomal tethering complexes, facilitating the conversion of Rab5 to Rab7 endosomes and mediating tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is recruited to Rab7 on the late endosomal membrane, regulating late endocytic, phagocytic, and autophagic traffic towards lysosomes. The CORVET complex functions as a Rab5 effector, mediating early endosome fusion. These proteins are essential for processes such as vacuolar biogenesis, lysosome biogenesis, and the degradation of apoptotic cells. They also play roles in embryogenesis, root development, and dendrite development in various organisms [[cite:PUB00161515], [cite:PUB00161516]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00161515": {
"PMID": 24501423,
"ISBN": null,
"volume": "25",
"issue": "7",
"year": 2014,
"title": "Caenorhabditis elegans HOPS and CCZ-1 mediate trafficking to lysosome-related organelles independently of RAB-7 and SAND-1.",
"URL": null,
"raw_pages": "1073-96",
"medline_journal": "Mol Biol Cell",
"ISO_journal": "Mol Biol Cell",
"authors": [
"Delahaye JL",
"Foster OK",
"Vine A",
"Saxton DS",
"Curtin TP",
"Somhegyi H",
"Salesky R",
"Hermann GJ."
],
"DOI_URL": "https://doi.org/10.1091/mbc.E13-09-0521"
},
"PUB00161516": {
"PMID": 25273556,
"ISBN": null,
"volume": "25",
"issue": "24",
"year": 2014,
"title": "Loss of the Sec1/Munc18-family proteins VPS-33.2 and VPS-33.1 bypasses a block in endosome maturation in Caenorhabditis elegans.",
"URL": null,
"raw_pages": "3909-25",
"medline_journal": "Mol Biol Cell",
"ISO_journal": "Mol Biol Cell",
"authors": [
"Solinger JA",
"Spang A."
],
"DOI_URL": "https://doi.org/10.1091/mbc.E13-12-0710"
},
"PUB00161517": {
"PMID": 29463724,
"ISBN": null,
"volume": "115",
"issue": "10",
"year": 2018,
"title": "Distinct sets of tethering complexes, SNARE complexes, and Rab GTPases mediate membrane fusion at the vacuole in Arabidopsis.",
"URL": null,
"raw_pages": "E2457-E2466",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc Natl Acad Sci U S A",
"authors": [
"Takemoto K",
"Ebine K",
"Askani JC",
"Kruger F",
"Gonzalez ZA",
"Ito E",
"Goh T",
"Schumacher K",
"Nakano A",
"Ueda T."
],
"DOI_URL": "https://doi.org/10.1073/pnas.1717839115"
},
"PUB00073490": {
"PMID": 11382755,
"ISBN": null,
"volume": "276",
"issue": "31",
"year": 2001,
"title": "Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7.",
"URL": null,
"raw_pages": "29393-402",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Kim BY",
"Kramer H",
"Yamamoto A",
"Kominami E",
"Kohsaka S",
"Akazawa C."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M101778200"
},
"PUB00161675": {
"PMID": 23351085,
"ISBN": null,
"volume": "280",
"issue": "12",
"year": 2013,
"title": "Tethering complexes in the endocytic pathway: CORVET and HOPS.",
"URL": null,
"raw_pages": "2743-57",
"medline_journal": "FEBS J",
"ISO_journal": "FEBS J",
"authors": [
"Solinger JA",
"Spang A."
],
"DOI_URL": "https://doi.org/10.1111/febs.12151"
},
"PUB00073491": {
"PMID": 10978279,
"ISBN": null,
"volume": "156",
"issue": "1",
"year": 2000,
"title": "Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae.",
"URL": null,
"raw_pages": "105-22",
"medline_journal": "Genetics",
"ISO_journal": "Genetics",
"authors": [
"Srivastava A",
"Woolford CA",
"Jones EW."
],
"DOI_URL": null
},
"PUB00161676": {
"PMID": 24554770,
"ISBN": null,
"volume": "25",
"issue": "8",
"year": 2014,
"title": "The HOPS complex mediates autophagosome-lysosome fusion through interaction with syntaxin 17.",
"URL": null,
"raw_pages": "1327-37",
"medline_journal": "Mol Biol Cell",
"ISO_journal": "Mol Biol Cell",
"authors": [
"Jiang P",
"Nishimura T",
"Sakamaki Y",
"Itakura E",
"Hatta T",
"Natsume T",
"Mizushima N."
],
"DOI_URL": "https://doi.org/10.1091/mbc.E13-08-0447"
},
"PUB00097428": {
"PMID": 25783203,
"ISBN": null,
"volume": "16",
"issue": "7",
"year": 2015,
"title": "Recruitment of VPS33A to HOPS by VPS16 Is Required for Lysosome Fusion with Endosomes and Autophagosomes.",
"URL": null,
"raw_pages": "727-42",
"medline_journal": "Traffic",
"ISO_journal": "Traffic",
"authors": [
"Wartosch L",
"Gunesdogan U",
"Graham SC",
"Luzio JP."
],
"DOI_URL": null
},
"PUB00062954": {
"PMID": 16601699,
"ISBN": null,
"volume": "25",
"issue": "8",
"year": 2006,
"title": "Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p.",
"URL": null,
"raw_pages": "1579-89",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Stroupe C",
"Collins KM",
"Fratti RA",
"Wickner W."
],
"DOI_URL": "http://dx.doi.org/10.1038/sj.emboj.7601051"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 70,
"interactions": 0,
"matches": 5117,
"pathways": 1,
"proteins": 4936,
"proteomes": 3174,
"sets": 0,
"structural_models": {
"alphafold": 4253,
"bfvd": 0
},
"structures": 4,
"taxa": 9336
},
"entry_annotations": {
"alignment:seed": 84,
"alignment:full": 3166
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
