ID NAS10_CAEEL Reviewed; 560 AA. AC Q21388; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 53. DE RecName: Full=Zinc metalloproteinase nas-10; DE EC=3.4.24.21; DE AltName: Full=Nematode astacin 10; GN Name=nas-10; ORFNames=K09C8.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [2] RP NOMENCLATURE. RX PubMed=14653817; DOI=10.1046/j.1432-1033.2003.03891.x; RA Moehrlen F., Hutter H., Zwilling R.; RT "The astacin protein family in Caenorhabditis elegans."; RL Eur. J. Biochem. 270:4909-4920(2003). CC -!- FUNCTION: Probable metalloprotease (By similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of peptide bonds in substrates CC containing five or more amino acids, preferentially with Ala in CC P1', and Pro in P2'. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SIMILARITY: Belongs to the peptidase M12A family. CC -!- SIMILARITY: Contains 1 SXC (ShKT) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z68006; CAA91996.1; -; Genomic_DNA. DR PIR; T23540; T23540. DR RefSeq; NP_509832.1; -. DR UniGene; Cel.696; -. DR HSSP; P07584; 1IAE. DR MEROPS; M12.323; -. DR Ensembl; K09C8.3; Caenorhabditis elegans. DR GeneID; 181287; -. DR KEGG; cel:K09C8.3; -. DR NMPDR; fig|6239.3.peg.24545; -. DR WormBase; WBGene00003529; nas-10. DR WormPep; K09C8.3; CE03479. DR OMA; Q21388; GRVEPAN. DR BRENDA; 3.4.24.21; 672. DR NextBio; 913288; -. DR ArrayExpress; Q21388; -. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR006025; Pept_M_Zn_BS. DR InterPro; IPR006026; Peptidase_M. DR InterPro; IPR001506; Peptidase_M12A. DR InterPro; IPR017368; Peptidase_M12A_astacin-9/10/11. DR InterPro; IPR003582; ShK_toxin. DR Pfam; PF01400; Astacin; 1. DR Pfam; PF01549; ShK; 1. DR PIRSF; PIRSF038055; Nas9/Nas10/Nas11; 1. DR PRINTS; PR00480; ASTACIN. DR SMART; SM00254; ShKT; 1. DR SMART; SM00235; ZnMc; 1. DR PROSITE; PS00142; ZINC_PROTEASE; FALSE_NEG. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Hydrolase; Metal-binding; KW Metalloprotease; Protease; Zinc. FT CHAIN 1 560 Zinc metalloproteinase nas-10. FT /FTId=PRO_0000078185. FT DOMAIN 524 560 SXC. FT COMPBIAS 111 114 Poly-Pro. FT COMPBIAS 187 227 Gln-rich. FT ACT_SITE 415 415 By similarity. FT METAL 414 414 Zinc; catalytic (By similarity). FT METAL 418 418 Zinc; catalytic (By similarity). FT METAL 424 424 Zinc; catalytic (By similarity). FT DISULFID 524 560 By similarity. FT DISULFID 531 553 By similarity. FT DISULFID 540 557 By similarity. SQ SEQUENCE 560 AA; 63041 MW; 4490B5456DA7256A CRC64; MYTITDLKTI NRKQKQAYLQ EKLICSRHCW LTHTTSKHIN IQWTTLIPHI RCRGFNNGPH PNSRPGSRPN SPLGDIFGNI NGMVKGITDQ IGKIAQGLDV NNDLGKMAHG PPPPQSEWVE HARRFCRRFP GHPKCRGQLP QFNDIGSMLN GILVDSGKWL PKVPFINIRD PLSGINSDLK NALNGIQVQF GQISQQFANN IRNICQQMNC KQQQQKNVQM KQAILKQTVD FEKKVFGNNV ADKMNLRFDR TLQLKQALLE KAQLKGVVAP EDNGVFDKDL LLTETQANFM LNELGKGGEG AIPMPGSAKA KRASIFFEQN LIQKWPSTSP IPYTFDSSLD NLDQNDVRGA ISEIEQKTCI RFKYFASPPK GNHINYQKVN SPSFCGLSYI GRVEPANPVY LSFQCGNGRG IAVHETMHAL GVNHQHLRMD RDKHIKVDWS NINPQQYDAF VVADSKLYTT YGVKYAYDSI MHYNAYTGAV NIAKPTMIPL VNQQANIGLL GQRAKMSNAD VEILNKMYCK SAGCDDKNVY CGAWALQDLC NNPNHNVWMR SNCRKSCNFC //