NAS8_CAEEL
ID NAS8_CAEEL Reviewed; 403 AA.
AC Q18439; Q7Z0N4;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Zinc metalloproteinase nas-8;
DE EC=3.4.24.21 {ECO:0000250|UniProtKB:P07584};
DE AltName: Full=Nematode astacin 8;
DE Flags: Precursor;
GN Name=nas-8; ORFNames=C34D4.9;
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 159-195, 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:P07584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of peptide bonds in substrates containing five or
CC more amino acids, preferentially with Ala in P1', and Pro in P2'.;
CC EC=3.4.24.21; Evidence={ECO:0000250|UniProtKB:P07584};
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; FO080770; CCD66603.1; -; Genomic_DNA.
DR EMBL; AJ561204; CAD99207.1; -; mRNA.
DR PIR; T29277; T29277.
DR RefSeq; NP_501114.2; NM_068713.6.
DR AlphaFoldDB; Q18439; -.
DR SMR; Q18439; -.
DR STRING; 6239.C34D4.9; -.
DR MEROPS; M12.A21; -.
DR PaxDb; Q18439; -.
DR EnsemblMetazoa; C34D4.9.1; C34D4.9.1; WBGene00003527.
DR EnsemblMetazoa; C34D4.9.2; C34D4.9.2; WBGene00003527.
DR GeneID; 183207; -.
DR KEGG; cel:CELE_C34D4.9; -.
DR UCSC; C34D4.9; c. elegans.
DR CTD; 183207; -.
DR WormBase; C34D4.9; CE31327; WBGene00003527; nas-8.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00970000196428; -.
DR HOGENOM; CLU_017286_0_0_1; -.
DR InParanoid; Q18439; -.
DR OMA; AAWKLKT; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q18439; -.
DR PRO; PR:Q18439; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003527; Expressed in larva 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; IPR017367; Caenorhab_nas-7/8.
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; 1.
DR PIRSF; PIRSF038054; Nas7/Nas8_prd; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00254; ShKT; 1.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS51670; SHKT; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
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..29
FT /evidence="ECO:0000255"
FT PROPEP 30..111
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442265"
FT CHAIN 112..403
FT /note="Zinc metalloproteinase nas-8"
FT /id="PRO_0000028913"
FT DOMAIN 112..307
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 338..372
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT ACT_SITE 204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 154..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 176..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 338..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 345..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 352..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 403 AA; 46095 MW; F1C02C8CE1428981 CRC64;
MRRNDLLNNK ITIFLSSLSL FVIIIPIYAA EKDLLPPSTS SETFLTDEDF LRPLNDDETF
LTEKDFKNGE KLGEDHVPAG SILWKQVYKK GDIRGKAAWK LDPKNSESLR RNGVITGTRK
WPNGRIPYVI SNQYNDRERA VLARSFQAYH DKTCVRFVPR TAVDNDYLYI GKIDGCYSDV
GRAGGRQELS LDNGCLQYDT AIHELMHSVG FYHEHERWDR DEHITILWHN IDREAYDQFG
KVDLAESSYY GQLYDYYSIM HYDSLAFSKN GFETMVAKQS EMTAVIGAAI DFSPIDILKM
NLMYQCSDVK LPPTVVGTTD KTIVPVPAPS VTVVEDDCRD RTNLCWRWID RCKSFFFEQI
MKEFCSLSCG YCTPKALQTA KASPPNYSNT LLTKSSTSYL QHG
