ID NAS26_CAEEL Reviewed; 414 AA. AC Q22710; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 4. DT 16-JUN-2009, entry version 57. DE RecName: Full=Zinc metalloproteinase nas-26; DE EC=3.4.24.21; DE AltName: Full=Nematode astacin 26; DE AltName: Full=Tollish protein 1; DE Flags: Precursor; GN Name=toh-1; Synonyms=nas-26; ORFNames=T24A11.3; 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 IDENTIFICATION. RA Finelli A.L., Savage C., Cho S.H., Padgett R.W.; RT "Tollish genes in C. elegans."; RL (er) Worm Breeder's Gazette 14(2):46(1996). RN [3] RP IDENTIFICATION, AND 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 -!- SUBCELLULAR LOCATION: Secreted (Potential). CC -!- SIMILARITY: Belongs to the peptidase M12A family. CC -!- SIMILARITY: Contains 1 CUB domain. CC -!- SIMILARITY: Contains 1 EGF-like 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; Z49072; CAA88882.4; -; Genomic_DNA. DR PIR; T25213; T25213. DR RefSeq; NP_497769.3; -. DR UniGene; Cel.22628; -. DR HSSP; P07584; 1AST. DR Ensembl; T24A11.3; Caenorhabditis elegans. DR GeneID; 175491; -. DR KEGG; cel:T24A11.3; -. DR NMPDR; fig|6239.3.peg.9220; -. DR WormBase; WBGene00006591; toh-1. DR WormPep; T24A11.3; CE35909. DR OMA; Q22710; AKVINDI. DR BRENDA; 3.4.24.21; 672. DR NextBio; 888382; -. DR ArrayExpress; Q22710; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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; IPR000859; CUB. DR InterPro; IPR013032; EGF-like_reg_CS. DR InterPro; IPR006025; Pept_M_Zn_BS. DR InterPro; IPR006026; Peptidase_M. DR InterPro; IPR001506; Peptidase_M12A. DR InterPro; IPR017050; Peptidase_M12A_nem. DR Gene3D; G3DSA:2.60.120.290; CUB; 1. DR Pfam; PF01400; Astacin; 1. DR Pfam; PF00431; CUB; 1. DR PIRSF; PIRSF036365; Astacin_nematoda; 1. DR PRINTS; PR00480; ASTACIN. DR SMART; SM00042; CUB; 1. DR SMART; SM00235; ZnMc; 1. DR PROSITE; PS01180; CUB; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; FALSE_NEG. DR PROSITE; PS50026; EGF_3; FALSE_NEG. DR PROSITE; PS00142; ZINC_PROTEASE; FALSE_NEG. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein; KW Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal; KW Zinc. FT SIGNAL 1 20 Potential. FT CHAIN 21 414 Zinc metalloproteinase nas-26. FT /FTId=PRO_0000028930. FT DOMAIN 251 307 EGF-like. FT DOMAIN 308 414 CUB. FT ACT_SITE 155 155 By similarity. FT METAL 154 154 Zinc; catalytic (By similarity). FT METAL 158 158 Zinc; catalytic (By similarity). FT METAL 164 164 Zinc; catalytic (By similarity). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT DISULFID 263 275 By similarity. FT DISULFID 267 286 By similarity. FT DISULFID 289 300 By similarity. FT DISULFID 308 331 By similarity. FT DISULFID 358 378 By similarity. SQ SEQUENCE 414 AA; 47140 MW; B8B381B421239D1B CRC64; MTSSLVLILA PLALVAIGEA AFGNSSKIFE IPGLEVMASD KYPHFTTIET VSRTKVHRHR REVIAGQIYD WNSYEIPFQI WGGDYNFQSL IRRGIRMWED STCLRFKENQ QSRDAIRYVL EKGDSCFTEY IGRNGGHQDI IIGSECAEEY VVAHETGHAL GFWHTHQRPD RDRHISINWK NVMEEATASF MPFRSMLQAF GIRQVSPRRV PYDYGSLMHY HAVAHAVKVS DFTIVPKELK YVTTMGTEKM AFLDAKVIND IYCPNACQGR NHLNCLAGGY PDPNNCNVCR CPEGLGGPDC GRLQPSPCGG EIHASDQWQT LSSPSGRDVH CYWRISVPEG SRVRFRLSDG EFPCSYGCQS YVEIKHKLDV RLTGFRSCCY RPKEDTVSES NQIFVIYHPN GRTARFSLRF RRQA //