NAS13_CAEEL
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 03-AUG-2022, entry version 133.
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;
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}.
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_078148.3.
DR AlphaFoldDB; Q20191; -.
DR SMR; Q20191; -.
DR STRING; 6239.F39D8.4; -.
DR MEROPS; M12.A38; -.
DR PaxDb; Q20191; -.
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 CTD; 185492; -.
DR WormBase; F39D8.4; CE43112; WBGene00003532; nas-13.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000171035; -.
DR HOGENOM; CLU_017286_0_1_1; -.
DR InParanoid; Q20191; -.
DR OMA; VNDSAMY; -.
DR OrthoDB; 681837at2759; -.
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 tissues.
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 CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; -; 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 Pfam; PF01400; Astacin; 1.
DR Pfam; PF01549; ShK; 2.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00254; ShKT; 2.
DR SMART; SM00235; ZnMc; 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
