NAS17_CAEEL
ID NAS17_CAEEL Reviewed; 429 AA.
AC Q21178;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Zinc metalloproteinase nas-17;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 17;
DE Flags: Precursor;
GN Name=nas-17; ORFNames=K03B8.2;
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; Z74039; CAA98501.1; -; Genomic_DNA.
DR PIR; T23263; T23263.
DR RefSeq; NP_505892.1; NM_073491.1.
DR AlphaFoldDB; Q21178; -.
DR SMR; Q21178; -.
DR STRING; 6239.K03B8.2; -.
DR MEROPS; M12.A31; -.
DR PaxDb; Q21178; -.
DR PeptideAtlas; Q21178; -.
DR EnsemblMetazoa; K03B8.2.1; K03B8.2.1; WBGene00003536.
DR GeneID; 186923; -.
DR KEGG; cel:CELE_K03B8.2; -.
DR UCSC; K03B8.2; c. elegans.
DR CTD; 186923; -.
DR WormBase; K03B8.2; CE06076; WBGene00003536; nas-17.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00970000196148; -.
DR HOGENOM; CLU_017286_1_1_1; -.
DR InParanoid; Q21178; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q21178; -.
DR PRO; PR:Q21178; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003536; Expressed in adult organism and 1 other tissue.
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:0018996; P:molting cycle, collagen and cuticulin-based cuticle; 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; IPR017050; Metallopeptidase_nem.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR Pfam; PF01400; Astacin; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442664"
FT CHAIN ?..429
FT /note="Zinc metalloproteinase nas-17"
FT /id="PRO_0000028921"
FT DOMAIN 62..251
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 245..284
FT /note="EGF-like"
FT ACT_SITE 153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 125..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 252..272
FT /evidence="ECO:0000250"
FT DISULFID 274..283
FT /evidence="ECO:0000250"
SQ SEQUENCE 429 AA; 48563 MW; D3C603863FD4C9BF CRC64;
MFLRPSTLLL TLFLALVAGS AIRKDVDEFD SNKGKDGIVD GDIMLTEAQL RILNGTAKRS
KRQITKIWKK WPDAKVFYYY ENEFTSLKRE LMSYAMAHIS SNTCVKFQES NSATNRIRFT
NTGGCASYIG MNGGEQTLWF GDGCLIFGTA VHEIMHSLGL FHTHSRFDRD NFLSVSYKDV
PENMVGNLEK ETEQTTYNAV PFEYGSTMLY RYNTFGEGTL VSKNEDYQKT MGLRRVSFYD
LVNINVRYSC GCAKSLTCEN GGYTNPSNCA TCVCPTGFAG TLCNEAPSNT IKLTAESYWK
GYWVNFGYST SIQTTNYYLA YLWITAPADK TIEVKIMDLS GFTCSYGCNY NGVEVKYMGD
PRITNPLRCC AQDTEYLNQV ISSKQNPTPI VMQQRYGSSK LTIHYRYVDT PLSSNKKSTN
GYDNYQYYV
