ID   NAS13_CAEEL             Reviewed;         450 AA.
AC   Q20191; Q21661; Q7Z0N3;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 5.
DT   04-NOV-2026, entry version 149.
DE   RecName: Full=Zinc metalloproteinase nas-13;
DE            EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE   AltName: Full=Nematode astacin 13;
DE   Flags: Precursor;
GN   Name=nas-13; ORFNames=F39D8.4;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 36-71, 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: Metalloprotease. {ECO:0000250|UniProtKB:A8Q2D1}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU01211};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD99208.1; Type=Miscellaneous discrepancy; Note=Deletion of several nucleotides that changes the frame.; Evidence={ECO:0000305};
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DR   EMBL; Z69791; CAA93663.4; -; Genomic_DNA.
DR   EMBL; Z69793; CAA93663.4; JOINED; Genomic_DNA.
DR   EMBL; AJ561206; CAD99208.1; ALT_SEQ; mRNA.
DR   PIR; T23864; T23864.
DR   RefSeq; NP_510549.3; NM_078148.6.
DR   AlphaFoldDB; Q20191; -.
DR   SMR; Q20191; -.
DR   FunCoup; Q20191; 2.
DR   STRING; 6239.F39D8.4.1; -.
DR   MEROPS; M12.A38; -.
DR   GlyCosmos; Q20191; 3 sites, No reported glycans.
DR   PaxDb; 6239-F39D8.4.1; -.
DR   PeptideAtlas; Q20191; -.
DR   EnsemblMetazoa; F39D8.4.1; F39D8.4.1; WBGene00003532.
DR   GeneID; 185492; -.
DR   KEGG; cel:CELE_F39D8.4; -.
DR   UCSC; F39D8.4; c. elegans.
DR   AGR; WB:WBGene00003532; -.
DR   CTD; 185492; -.
DR   WormBase; F39D8.4; CE43112; WBGene00003532; nas-13.
DR   eggNOG; KOG3714; Eukaryota.
DR   HOGENOM; CLU_017286_0_1_1; -.
DR   InParanoid; Q20191; -.
DR   OMA; ACADNNH; -.
DR   OrthoDB; 291007at2759; -.
DR   PhylomeDB; Q20191; -.
DR   PRO; PR:Q20191; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00003532; Expressed in pharyngeal muscle cell (C elegans) and 2 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
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:InterPro.
DR   CDD; cd04280; ZnMc_astacin_like; 1.
DR   FunFam; 3.40.390.10:FF:000015; Meprin A subunit; 1.
DR   FunFam; 1.10.10.1940:FF:000003; Metalloendopeptidase; 1.
DR   FunFam; 1.10.10.1940:FF:000004; Metalloendopeptidase; 1.
DR   Gene3D; 1.10.10.1940; -; 2.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR003582; ShKT_dom.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF890; ZINC METALLOPROTEINASE NAS-13; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF01549; ShK; 2.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00254; ShKT; 2.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS51670; SHKT; 2.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   PROPEP          32..?
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000442660"
FT   CHAIN           ?..450
FT                   /note="Zinc metalloproteinase nas-13"
FT                   /id="PRO_0000028917"
FT   DOMAIN          110..303
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DOMAIN          368..404
FT                   /note="ShKT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DOMAIN          414..450
FT                   /note="ShKT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   MOTIF           349..351
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         205
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        431
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        152..302
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        174..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        368..404
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        375..397
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        384..401
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        414..450
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        421..443
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        430..447
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ   SEQUENCE   450 AA;  50760 MW;  EBEC8772AD008F06 CRC64;
     MPSPTSSSAS VFSSHLFFVF CIFSQIAQSY AQFNRFFDPS IPEQETVLTD YDYNMIGHFR
     ENDQWFVNDS AMYNPLRFEG DIANSGLNSR SINTFFGDSP LFGIFGVQRN AVRQTYLKWE
     QARIPYTISS QYSSYSRSKI AEAIEEYRKK TCIDFSPKSA GDLDYIHIVP DDGCYSLVGR
     IGGKQPVSLG DGCIQKGIII HELMHAVGFF HEQSRADRDE YVKINWSNVE AGLQDQFDKY
     SLNMIDHLGT KYDYGSVMHY APTAFSKNGK PTIEPIEKNV EIGQRAGFSE NDIYKINMLY
     NCPTFTATTL APENTKRVKS ITKKVTSATG SPLSKKGEIG SSIGDKGDRG DNSVLSSLIS
     IHSGLGKCED RRKDCEFLAR AGHCESRFSI RFMTENCANS CGKCIAEEKR KEVCEDARTW
     CERWANSGMC NQTVFKDYMR QKCAKSCNFC
//