ID   NAS25_CAEEL             Reviewed;         399 AA.
AC   Q20459; Q7Z0M5;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 3.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Zinc metalloproteinase nas-25;
DE            EC=3.4.24.21;
DE   AltName: Full=Nematode astacin 25;
DE   Flags: Precursor;
GN   Name=nas-25; ORFNames=F46C5.3;
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 208-260, 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; Z54281; CAA91045.3; -; Genomic_DNA.
DR   EMBL; AJ561215; CAD99216.1; -; mRNA.
DR   PIR; T22300; T22300.
DR   RefSeq; NP_495880.1; -.
DR   UniGene; Cel.15073; -.
DR   HSSP; P07584; 1IAE.
DR   MEROPS; M12.310; -.
DR   Ensembl; F46C5.3; Caenorhabditis elegans.
DR   GeneID; 174412; -.
DR   KEGG; cel:F46C5.3; -.
DR   NMPDR; fig|6239.3.peg.6739; -.
DR   WormBase; WBGene00003544; nas-25.
DR   WormPep; F46C5.3; CE28935.
DR   OMA; Q20459; ANCANGG.
DR   BRENDA; 3.4.24.21; 672.
DR   NextBio; 883914; -.
DR   ArrayExpress; Q20459; -.
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     20       Potential.
FT   CHAIN        21    399       Zinc metalloproteinase nas-25.
FT                                /FTId=PRO_0000028929.
FT   DOMAIN      232    275       EGF-like.
FT   ACT_SITE    135    135       By similarity.
FT   METAL       134    134       Zinc; catalytic (By similarity).
FT   METAL       138    138       Zinc; catalytic (By similarity).
FT   METAL       144    144       Zinc; catalytic (By similarity).
FT   CARBOHYD     52     52       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     61     61       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    371    371       N-linked (GlcNAc...) (Potential).
FT   DISULFID    236    249       By similarity.
FT   DISULFID    240    260       By similarity.
FT   DISULFID    265    274       By similarity.
SQ   SEQUENCE   399 AA;  45456 MW;  38EA62319A2CF172 CRC64;
     MQIYLGITIC LVAFLTVIDC AIPYYRTHSN FGSLGRRKVR QVQRDLTYRW PNNTVPYYVG
     NVTSTIKKSV RLAIEELQAW TCIRFQNVNE KYSDGDSVRI VDLGSCSSPI GRQQIGTQDV
     SLTKNCWGMG TAIHELMHAI GIEHTQSRSD RNRYLDILAQ NIDNRDLPNF ELLSPRLWAN
     LVPYDYGSVM HYSADSFSNK DDEQTMLPKD RSFIETMGSM IPNFYDFDQI NQYYQCYDSC
     RNAGQLANCA NGGIPNPNNC QVCNCPMGYG GDLCDQRPEG CGSTLVATDR WQKQKLSVRF
     SRNDDQYFTF CNSWIVGPSD RTLQVIYEIT SDSIRRQICS FGCYEGGIEV KHLQDPRITN
     DRDCCLNTPL NLTTTVNPLP VILYTSGATV TYDFSYRYV
//