ID   NAS2_CAEEL              Reviewed;         293 AA.
AC   Q9N5R0;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 3.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Zinc metalloproteinase nas-2;
DE            EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE   AltName: Full=Nematode astacin 2;
DE   Flags: Precursor;
GN   Name=nas-2; ORFNames=F56A4.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   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 investigating
RT   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: Metalloprotease. {ECO:0000250|UniProtKB:A8Q2D1}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU01211};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; FO080246; CCD62311.1; -; Genomic_DNA.
DR   RefSeq; NP_503652.3; NM_071251.3.
DR   RefSeq; NP_503678.3; NM_071277.3.
DR   AlphaFoldDB; Q9N5R0; -.
DR   SMR; Q9N5R0; -.
DR   STRING; 6239.F56A4.1; -.
DR   MEROPS; M12.A15; -.
DR   PaxDb; Q9N5R0; -.
DR   EnsemblMetazoa; F56A4.1.1; F56A4.1.1; WBGene00003521.
DR   GeneID; 186345; -.
DR   GeneID; 189484; -.
DR   KEGG; cel:CELE_F56A4.1; -.
DR   KEGG; cel:CELE_Y19D10A.6; -.
DR   UCSC; F56A4.1; c. elegans.
DR   CTD; 186345; -.
DR   CTD; 189484; -.
DR   WormBase; F56A4.1; CE51070; WBGene00003521; nas-2.
DR   eggNOG; KOG3714; Eukaryota.
DR   GeneTree; ENSGT00940000154856; -.
DR   HOGENOM; CLU_998309_0_0_1; -.
DR   InParanoid; Q9N5R0; -.
DR   OMA; HELMFAL; -.
DR   OrthoDB; 681837at2759; -.
DR   PhylomeDB; Q9N5R0; -.
DR   PRO; PR:Q9N5R0; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..67
FT                   /evidence="ECO:0000250|UniProtKB:P13497"
FT                   /id="PRO_0000442650"
FT   CHAIN           68..293
FT                   /note="Zinc metalloproteinase nas-2"
FT                   /id="PRO_0000028907"
FT   DOMAIN          67..260
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        114..259
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        139..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   293 AA;  33942 MW;  48C81627DC0F779E CRC64;
     MIFPLLLTLI LPNFVAPKVL EPEKDDEIAV STQREKTFFD MKLILTKLPT FEPSKYGHIN
     IPLRKKRGIA LHPLQWASYL WPNAEVPYDI ATHYTSTEKS IILSAMEAFK NVTCVRFRPR
     AATDKHYLQI NKYFNVERCF SYIGRQSSRT LFGTPEGNVE TRMRLDPACL RGNGRGIVMH
     ELMHILGFYH EHQRDDRDRR IVGSAVHYNF KIYRRAKTLY MGAYDANSIM HYNFQNLPWQ
     RRDHFSTSDI ININTFYKCK NLLSSKLAPK VPISPTSTST TAITTTNTTT TKL