ID Q3B826_HUMAN Unreviewed; 430 AA. AC Q3B826; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 86. DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183}; DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183}; DE Flags: Fragment; GN Name=ASTL {ECO:0000313|EMBL:AAI07127.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAI07127.1}; RN [1] {ECO:0000313|EMBL:AAI07127.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE- CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}; CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC107126; AAI07127.1; -; mRNA. DR AlphaFoldDB; Q3B826; -. DR SMR; Q3B826; -. DR MEROPS; M12.245; -. DR PeptideAtlas; Q3B826; -. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001506; Peptidase_M12A. DR InterPro; IPR006026; Peptidase_Metallo. DR PANTHER; PTHR10127:SF887; ASTACIN-LIKE METALLOENDOPEPTIDASE; 1. DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1. DR Pfam; PF01400; Astacin; 1. DR PRINTS; PR00480; ASTACIN. DR SMART; SM00235; ZnMc; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS51864; ASTACIN; 1. PE 2: Evidence at transcript level; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211, KW ECO:0000256|RuleBase:RU361183}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211, KW ECO:0000256|RuleBase:RU361183}; KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211, KW ECO:0000256|RuleBase:RU361183}; KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211, KW ECO:0000256|RuleBase:RU361183}; Signal {ECO:0000256|RuleBase:RU361183}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|RuleBase:RU361183" FT CHAIN 23..430 FT /note="Metalloendopeptidase" FT /evidence="ECO:0000256|RuleBase:RU361183" FT /id="PRO_5005143152" FT DOMAIN 84..281 FT /note="Peptidase M12A" FT /evidence="ECO:0000259|PROSITE:PS51864" FT REGION 282..303 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 316..430 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 385..405 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 182 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" FT BINDING 181 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" FT BINDING 185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAI07127.1" SQ SEQUENCE 430 AA; 45833 MW; 619ED8B901CA279D CRC64; EGVGGLWPWV LGLLSLPGVI LGAPLASSCA GACGTSFPDG LTPEGTQASG DKDIPAINQG LILEETPESS FLIEGDIIRP SPFRLLSATS NKWPMGGSGV VEVPFLLSSK YDEPSRQVIL EALAEFERST CIRFVTYQDQ RDFISIIPMY GCFSSVGRSG GMQVVSLAPT CLQKGRGIVL HELMHVLGFW HEHTRADRDR YIRVNWNEIL PGFEINFIKS RSSNMLTPYD YSSVMHYGRL AFSRRGLPTI TPLWAPSVHI GQRWNLSASD ITRVLQLYGC SPSGPRPRGR GSHAHSTGRS PAPASLSLQR LLEALSAESR SPDPSGSSAG GQPVPAGPGE SPHGWESPAL KKLSAEASAR QPQTLASSPR SRPGAGAPGV AQEQSWLAGV STKPTVPSSE AGIQPVPVQG SPALPGGCVP RNHFKGMSED //