ID   NAS20_CAEEL             Reviewed;         379 AA.
AC   Q22396; Q7Z0M9;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Zinc metalloproteinase nas-20;
DE            EC=3.4.24.21;
DE   AltName: Full=Nematode astacin 20;
DE   Flags: Precursor;
GN   Name=nas-20; ORFNames=T11F9.3;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 158-308, AND NOMENCLATURE.
RC   STRAIN=Bristol N2;
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).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185 AND ASN-337, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
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 EGF-like domain.
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DR   EMBL; Z74042; CAA98528.2; -; Genomic_DNA.
DR   EMBL; AJ561210; CAD99212.1; -; mRNA.
DR   PIR; T24836; T24836.
DR   RefSeq; NP_505906.2; -.
DR   UniGene; Cel.34453; -.
DR   MEROPS; M12.310; -.
DR   Ensembl; T11F9.3; Caenorhabditis elegans.
DR   GeneID; 188420; -.
DR   KEGG; cel:T11F9.3; -.
DR   NMPDR; fig|6239.3.peg.19736; -.
DR   WormBase; WBGene00003539; nas-20.
DR   WormPep; T11F9.3; CE35907.
DR   OMA; Q22396; FEFEYRY.
DR   BRENDA; 3.4.24.21; 672.
DR   NextBio; 938732; -.
DR   ArrayExpress; Q22396; -.
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; 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   Pfam; PF01400; Astacin; 1.
DR   PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; FALSE_NEG.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein 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    379       Zinc metalloproteinase nas-20.
FT                                /FTId=PRO_0000028924.
FT   DOMAIN      203    244       EGF-like.
FT   ACT_SITE    120    120       By similarity.
FT   METAL       119    119       Zinc; catalytic (By similarity).
FT   METAL       123    123       Zinc; catalytic (By similarity).
FT   METAL       129    129       Zinc; catalytic (By similarity).
FT   CARBOHYD     67     67       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    185    185       N-linked (GlcNAc...).
FT   CARBOHYD    337    337       N-linked (GlcNAc...).
FT   CARBOHYD    370    370       N-linked (GlcNAc...) (Potential).
FT   DISULFID    207    218       By similarity.
FT   DISULFID    209    229       By similarity.
FT   DISULFID    234    243       By similarity.
SQ   SEQUENCE   379 AA;  43378 MW;  E79F82C99226FB51 CRC64;
     MKITVNFLLV ALIGVPSVLS DRHITRDKRQ AMRDYAKWEN NKMSLFFYNL PLEMQAMFRD
     AINYLENHTC LKFEYNENAE TAVRIRKGNG CYSLYGMHAG EVQDLTLDYN CASFGTAVHE
     IMHALGIAHG QARSDRDDYL IVDSTNSNDG IENTENLVPF DYGSVMLYAR DPHSDKRIPI
     DPEYNFTMGS LRVAFYDMVL LNKFYGCNCD NHPRKLDCKN GGYQNPANCE ECLCTDGFNG
     QLCDQHEGVY VLEAKKEWDA SGVRNNYRKG IETNTMPEYT YFALTAPEGS TIEVRITKLS
     GFFCQHTCDY NGVELKYKTD RRIVSPLVCC DNDNLWNKTR SSTNNPFIIA KYGNNRTPHF
     EFEYRYIPGN ATAAPEENN
//