ID   NAS16_CAEEL             Reviewed;         451 AA.
AC   Q21180;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Zinc metalloproteinase nas-16;
DE            EC=3.4.24.21;
DE   AltName: Full=Nematode astacin 16;
DE   Flags: Precursor;
GN   Name=nas-16; ORFNames=K03B8.1;
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; CAA98503.1; -; Genomic_DNA.
DR   PIR; T23265; T23265.
DR   RefSeq; NP_505889.1; -.
DR   UniGene; Cel.32979; -.
DR   HSSP; P07584; 1IAE.
DR   MEROPS; M12.310; -.
DR   Ensembl; K03B8.1; Caenorhabditis elegans.
DR   GeneID; 186922; -.
DR   KEGG; cel:K03B8.1; -.
DR   NMPDR; fig|6239.3.peg.19715; -.
DR   WormBase; WBGene00003535; nas-16.
DR   WormPep; K03B8.1; CE06075.
DR   OMA; Q21180; CTISTRI.
DR   BRENDA; 3.4.24.21; 672.
DR   NextBio; 933468; -.
DR   ArrayExpress; Q21180; -.
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      ?       Potential.
FT   CHAIN         ?    451       Zinc metalloproteinase nas-16.
FT                                /FTId=PRO_0000028920.
FT   DOMAIN      267    306       EGF-like.
FT   ACT_SITE    176    176       By similarity.
FT   METAL       175    175       Zinc; catalytic (By similarity).
FT   METAL       179    179       Zinc; catalytic (By similarity).
FT   METAL       185    185       Zinc; catalytic (By similarity).
FT   CARBOHYD    133    133       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    363    363       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    438    438       N-linked (GlcNAc...) (Potential).
FT   DISULFID    272    280       By similarity.
FT   DISULFID    274    291       By similarity.
FT   DISULFID    296    305       By similarity.
SQ   SEQUENCE   451 AA;  51508 MW;  3F04B96F5606A5A6 CRC64;
     MGNLFKFSLN CIKYRSENLE KSKMFYQYFY FHLTLSIVLI YGSDIGKDAN EHMSSVPKKI
     IIEGTRQKRQ VVTKLFSPQW SNAKVFYCNA DSFSKLQLKK LKLKKNSDTV KRKLMKFAMN
     FISSQTCVTF EENCTISTRI KFVDSTFCAS YVGMINSVQE IYFPDWCMRF GSAVHELMHA
     LGVLHTHARF DRDNFLNVNL NKDDEDDSNF EIVSPPFSIN VVPYEYGSTL HYTADVSGTN
     SLLPKQMEYY RTLGNRRVTF YDMLTINTAY NCKCPSELLC ANGGYTNPSN CLECICPLGY
     GGVLCDRVVA CSVQLSADSY WKGSWISVGS SVLRDTTDPV KAFISINAPK DKIIEVKIVK
     IENFSCDSGC NNNGVEIKYM GDPRITNPII CCENQVDPSN KGYKAKLNPL LINIYTFLGK
     NKVTFHYRYV NERLSSYNKT TNGYDNYEYY A
//