ID   NAS19_CAEEL             Reviewed;         479 AA.
AC   Q21181; Q7Z0N0;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Zinc metalloproteinase nas-19;
DE            EC=3.4.24.21;
DE   AltName: Full=Nematode astacin 19;
DE   Flags: Precursor;
GN   Name=nas-19; ORFNames=K03B8.5;
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 186-218, 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).
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; CAA98504.1; -; Genomic_DNA.
DR   EMBL; AJ561209; CAD99211.1; -; mRNA.
DR   PIR; T23266; T23266.
DR   RefSeq; NP_505893.1; -.
DR   UniGene; Cel.34468; -.
DR   HSSP; P01132; 1EGF.
DR   Ensembl; K03B8.5; Caenorhabditis elegans.
DR   GeneID; 186926; -.
DR   KEGG; cel:K03B8.5; -.
DR   NMPDR; fig|6239.3.peg.19719; -.
DR   WormBase; WBGene00003538; nas-19.
DR   WormPep; K03B8.5; CE06079.
DR   BRENDA; 3.4.24.21; 672.
DR   NextBio; 933484; -.
DR   ArrayExpress; Q21181; -.
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   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     17       Potential.
FT   CHAIN        18    479       Zinc metalloproteinase nas-19.
FT                                /FTId=PRO_0000028923.
FT   DOMAIN      308    347       EGF-like.
FT   ACT_SITE    222    222       By similarity.
FT   METAL       221    221       Zinc; catalytic (By similarity).
FT   METAL       225    225       Zinc; catalytic (By similarity).
FT   METAL       231    231       Zinc; catalytic (By similarity).
FT   CARBOHYD    162    162       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    393    393       N-linked (GlcNAc...) (Potential).
FT   DISULFID    313    321       By similarity.
FT   DISULFID    315    335       By similarity.
FT   DISULFID    337    346       By similarity.
SQ   SEQUENCE   479 AA;  54849 MW;  C1AE11ECC6951366 CRC64;
     MYLKIFRLLL EIKSSILKIC VYFSSKNYGI LSISFAFLLI YFDVLYEKFP TDLHIPLDFS
     YKNKVENGIN EHIAGGNIIQ HLEMVRLIHL IGAIILLFSY AYCGLSRLNE HDIEESYSHK
     RVKRQFERLG TKWSYGVVNY YYADKNNEIK EMVESAIAYI ANHTCIRFNE DQNAVQRVQI
     RMQQNWLCQS TVGAPGMSMS KPIGELSMLV QSCDTIGSIV HEFSHSLGRF HEHTRPDRDN
     FMKVTTTVHE ARPRPSGMTT MYGPFEHGSV MMYHADTYGP GTMDPLDMDY KQTMGNRRVT
     FYDMYKINQY YGCWCSKQLE CKNGGYTSPS DCSRCNCPKG FFGNLCDERQ QDSYELMAVN
     NLWQSITIPF AYKPEPGSDG FYSTFVYITG KANSTIEITL EGLQDVICTA GCTVNGVEIK
     FKEDSKITSP VVCCTDKPPY KNVFKSSHNP TIIELYSRTT LPSAVTFKYR FTNDKVVLG
//