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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR001506",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0004222",
"name": "metalloendopeptidase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006508",
"name": "proteolysis",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"profile": {
"PS51864": "Astacin-like domain profile"
},
"pfam": {
"PF01400": "Astacin (Peptidase family M12A)"
},
"prints": {
"PR00480": "ASTACIN"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR006026",
"name": "Peptidase, metallopeptidase",
"type": "Domain",
"children": [
{
"accession": "IPR001506",
"name": "Peptidase M12A",
"type": "Domain",
"children": [
{
"accession": "IPR034035",
"name": "Astacin-like metallopeptidase domain",
"type": "Domain",
"children": []
},
{
"accession": "IPR034036",
"name": "Tolloid/BMP1 peptidase domain",
"type": "Domain",
"children": []
},
{
"accession": "IPR034038",
"name": "Meprin peptidase domain",
"type": "Domain",
"children": []
},
{
"accession": "IPR034039",
"name": "Hatching enzyme, peptidase domain",
"type": "Domain",
"children": []
}
]
},
{
"accession": "IPR001818",
"name": "Peptidase M10, metallopeptidase",
"type": "Domain",
"children": [
{
"accession": "IPR033739",
"name": "Peptidase M10A, catalytic domain",
"type": "Domain",
"children": []
},
{
"accession": "IPR034033",
"name": "Serralysin-like metallopeptidase domain",
"type": "Domain",
"children": []
}
]
}
]
},
"name": {
"name": "Peptidase M12A",
"short": "Peptidase_M12A"
},
"description": [
{
"text": "<p>This group of metallopeptidases belong to the MEROPS peptidase family M12, subfamily M12A (astacin family, clan MA(M)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA and the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH [[cite:PUB00003579]].</p>\n\n<p>The astacin ([ec:3.4.24.21]) family of metalloendopeptidases encompasses a range of proteins found in hydra to humans, in mature and developmental systems [[cite:PUB00005025], [cite:PUB00074412]]. Their functions include activation of growth factors, degradation of polypeptides, and processing of extracellular proteins [[cite:PUB00005025]]. The proteins are synthesised with N-terminal signal and pro-enzyme sequences, and many contain multiple domains C-terminal to the protease domain. They are either secreted from cells, or are associated with the plasma membrane [[cite:PUB00097277]].</p>\n\n<p>The astacin molecule adopts a kidney shape, with a deep active-site cleft between its N- and C-terminal domains [[cite:PUB00003300]]. The zinc ion, which lies at the bottom of the cleft, exhibits a unique penta-coordinated mode of binding, involving 3 histidine residues, a tyrosine and a water molecule (which is also bound to the carboxylate side chain of Glu93) [[cite:PUB00003300]]. The N-terminal domain comprises 2 α-helices and a 5-stranded β-sheet. The overall topology of this domain is shared by the archetypal zinc-endopeptidase thermolysin. Astacin protease domains also share common features with serralysins, matrix metalloendopeptidases, and snake venom proteases; they cleave peptide bonds in polypeptides such as insulin B chain and bradykinin, and in proteins such as casein and gelatin; and they have arylamidase activity [[cite:PUB00005025]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00005025": {
"PMID": 7670368,
"ISBN": null,
"volume": "4",
"issue": "7",
"year": 1995,
"title": "The astacin family of metalloendopeptidases.",
"URL": null,
"raw_pages": "1247-61",
"medline_journal": "Protein Sci",
"ISO_journal": "Protein Sci.",
"authors": [
"Bond JS",
"Beynon RJ."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=7670368"
},
"PUB00003300": {
"PMID": 8445658,
"ISBN": null,
"volume": "229",
"issue": "4",
"year": 1993,
"title": "Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin.",
"URL": null,
"raw_pages": "945-68",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Gomis-Ruth FX",
"Stocker W",
"Huber R",
"Zwilling R",
"Bode W."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.1993.1098"
},
"PUB00003579": {
"PMID": 7674922,
"ISBN": null,
"volume": "248",
"issue": null,
"year": 1995,
"title": "Evolutionary families of metallopeptidases.",
"URL": null,
"raw_pages": "183-228",
"medline_journal": "Methods Enzymol",
"ISO_journal": "Meth. Enzymol.",
"authors": [
"Rawlings ND",
"Barrett AJ."
],
"DOI_URL": "http://dx.doi.org/10.1016/0076-6879(95)48015-3"
},
"PUB00097277": {
"PMID": 23092796,
"ISBN": null,
"volume": "393",
"issue": "10",
"year": 2012,
"title": "Functional and structural insights into astacin metallopeptidases.",
"URL": null,
"raw_pages": "1027-41",
"medline_journal": "Biol Chem",
"ISO_journal": "Biol Chem",
"authors": [
"Gomis-Ruth FX",
"Trillo-Muyo S",
"Stocker W."
],
"DOI_URL": null
},
"PUB00074412": {
"PMID": 20109220,
"ISBN": null,
"volume": "10",
"issue": null,
"year": 2010,
"title": "Characterization of the astacin family of metalloproteases in C. elegans.",
"URL": null,
"raw_pages": "14",
"medline_journal": "BMC Dev Biol",
"ISO_journal": "BMC Dev. Biol.",
"authors": [
"Park JO",
"Pan J",
"Mohrlen F",
"Schupp MO",
"Johnsen R",
"Baillie DL",
"Zapf R",
"Moerman DG",
"Hutter H."
],
"DOI_URL": "http://dx.doi.org/10.1186/1471-213X-10-14"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR024079",
"name": "Metallopeptidase, catalytic domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 1161,
"interactions": 0,
"matches": 36125,
"pathways": 18,
"proteins": 34807,
"proteomes": 2962,
"sets": 0,
"structural_models": {
"alphafold": 30805,
"bfvd": 1
},
"structures": 35,
"taxa": 8116
},
"entry_annotations": {
"alignment:seed": 22,
"alignment:full": 22907
},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "3.4.24",
"url": "https://enzyme.expasy.org/EC/3.4.24"
},
{
"accession": "3.4.24.-",
"url": "https://enzyme.expasy.org/EC/3.4.24.-"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3lqb",
"name": "Crystal structure of the hatching enzyme ZHE1 from the zebrafish Danio rerio"
}
}
}
