ID   NAS3_CAEEL              Reviewed;         292 AA.
AC   Q21252; Q7Z0P2;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Zinc metalloproteinase nas-3;
DE            EC=3.4.24.21;
DE   AltName: Full=Nematode astacin 3;
DE   Flags: Precursor;
GN   Name=nas-3; ORFNames=K06A4.1;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 128-207, 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.
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DR   EMBL; Z70755; CAA94781.2; -; Genomic_DNA.
DR   EMBL; AJ561200; CAD99180.1; -; mRNA.
DR   PIR; T23354; T23354.
DR   RefSeq; NP_505445.2; -.
DR   UniGene; Cel.3128; -.
DR   HSSP; P07584; 1QJJ.
DR   MEROPS; M12.001; -.
DR   Ensembl; K06A4.1; Caenorhabditis elegans.
DR   GeneID; 187045; -.
DR   KEGG; cel:K06A4.1; -.
DR   NMPDR; fig|6239.3.peg.19110; -.
DR   WormBase; WBGene00003522; nas-3.
DR   WormPep; K06A4.1; CE35894.
DR   OMA; Q21252; HYTATER.
DR   BRENDA; 3.4.24.21; 672.
DR   NextBio; 933896; -.
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; IPR006025; Pept_M_Zn_BS.
DR   InterPro; IPR006026; Peptidase_M.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Zinc.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17    292       Zinc metalloproteinase nas-3.
FT                                /FTId=PRO_0000028908.
FT   ACT_SITE    170    170       By similarity.
FT   METAL       169    169       Zinc; catalytic (By similarity).
FT   METAL       173    173       Zinc; catalytic (By similarity).
FT   METAL       179    179       Zinc; catalytic (By similarity).
SQ   SEQUENCE   292 AA;  34400 MW;  0CDC6A600AB5EC48 CRC64;
     MYRFIIFFSL LALTASKVSE PEKDDEIAVK IPTKRSVSEP PKDDDIAVKI PMRKKRGIAI
     HPWQWESHLW PNAEVPYDIA SHYTATERGI ILSAMEAFRD VTCVRFRPRR STDKHYLQIN
     KHYQLERCFS YIGRQSSRWL FGTRDGKVET RMKLDPSCLL YNGRGTVMHE LMHILGFYHE
     HQRDDRDRRI GGSASHYNFK IYQRAKSYYM GGYDANSIMH YNFGSVPWQK RDYFSPSDIR
     NINTLYKCNN RVVSKFPSTI PSTSTTTTKA PQFELFEKKQ IESNSLFRRR RS
//