ID   NAS17_CAEEL             Reviewed;         429 AA.
AC   Q21178;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Zinc metalloproteinase nas-17;
DE            EC=3.4.24.21;
DE   AltName: Full=Nematode astacin 17;
DE   Flags: Precursor;
GN   Name=nas-17; ORFNames=K03B8.2;
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, 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 EGF-like domain.
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DR   EMBL; Z74039; CAA98501.1; -; Genomic_DNA.
DR   PIR; T23263; T23263.
DR   UniGene; Cel.32978; -.
DR   MEROPS; M12.310; -.
DR   Ensembl; K03B8.2; Caenorhabditis elegans.
DR   NMPDR; fig|6239.3.peg.19718; -.
DR   WormBase; WBGene00003536; nas-17.
DR   WormPep; K03B8.2; CE06076.
DR   BRENDA; 3.4.24.21; 672.
DR   ArrayExpress; Q21178; -.
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; IPR006210; EGF-like.
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; SM00181; EGF; 1.
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   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     21       Potential.
FT   CHAIN        22    429       Zinc metalloproteinase nas-17.
FT                                /FTId=PRO_0000028921.
FT   DOMAIN      245    284       EGF-like.
FT   ACT_SITE    153    153       By similarity.
FT   METAL       152    152       Zinc; catalytic (By similarity).
FT   METAL       156    156       Zinc; catalytic (By similarity).
FT   METAL       162    162       Zinc; catalytic (By similarity).
FT   CARBOHYD     54     54       N-linked (GlcNAc...) (Potential).
FT   DISULFID    250    258       By similarity.
FT   DISULFID    252    272       By similarity.
FT   DISULFID    274    283       By similarity.
SQ   SEQUENCE   429 AA;  48563 MW;  D3C603863FD4C9BF CRC64;
     MFLRPSTLLL TLFLALVAGS AIRKDVDEFD SNKGKDGIVD GDIMLTEAQL RILNGTAKRS
     KRQITKIWKK WPDAKVFYYY ENEFTSLKRE LMSYAMAHIS SNTCVKFQES NSATNRIRFT
     NTGGCASYIG MNGGEQTLWF GDGCLIFGTA VHEIMHSLGL FHTHSRFDRD NFLSVSYKDV
     PENMVGNLEK ETEQTTYNAV PFEYGSTMLY RYNTFGEGTL VSKNEDYQKT MGLRRVSFYD
     LVNINVRYSC GCAKSLTCEN GGYTNPSNCA TCVCPTGFAG TLCNEAPSNT IKLTAESYWK
     GYWVNFGYST SIQTTNYYLA YLWITAPADK TIEVKIMDLS GFTCSYGCNY NGVEVKYMGD
     PRITNPLRCC AQDTEYLNQV ISSKQNPTPI VMQQRYGSSK LTIHYRYVDT PLSSNKKSTN
     GYDNYQYYV
//