ID   NAS10_CAEEL             Reviewed;         540 AA.
AC   Q21388; B6EU59;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Zinc metalloproteinase nas-10;
DE            EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE   AltName: Full=Nematode astacin 10;
DE   Flags: Precursor;
GN   Name=nas-10 {ECO:0000312|WormBase:K09C8.3};
GN   ORFNames=K09C8.3 {ECO:0000312|WormBase:K09C8.3};
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   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};
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DR   EMBL; BX284606; CAR81375.1; -; Genomic_DNA.
DR   PIR; T23540; T23540.
DR   RefSeq; NP_001257125.1; NM_001270196.1.
DR   RefSeq; NP_001257126.1; NM_001270197.1.
DR   AlphaFoldDB; Q21388; -.
DR   SMR; Q21388; -.
DR   STRING; 6239.K09C8.3a; -.
DR   MEROPS; M12.A35; -.
DR   PaxDb; Q21388; -.
DR   EnsemblMetazoa; K09C8.3.1; K09C8.3.1; WBGene00003529.
DR   GeneID; 181287; -.
DR   KEGG; cel:CELE_K09C8.3; -.
DR   UCSC; K09C8.3; c. elegans.
DR   CTD; 181287; -.
DR   WormBase; K09C8.3; CE43056; WBGene00003529; nas-10.
DR   eggNOG; KOG3714; Eukaryota.
DR   GeneTree; ENSGT00970000196429; -.
DR   HOGENOM; CLU_030134_0_0_1; -.
DR   InParanoid; Q21388; -.
DR   OrthoDB; 681837at2759; -.
DR   PhylomeDB; Q21388; -.
DR   PRO; PR:Q21388; -.
DR   Proteomes; UP000001940; Chromosome X.
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; IPR017368; Peptidase_M12A_astacin-9/10/11.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR003582; ShKT_dom.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF01549; ShK; 1.
DR   PIRSF; PIRSF038055; Nas9/Nas10/Nas11; 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.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Zinc; Zymogen.
FT   PROPEP          1..?
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000442657"
FT   CHAIN           ?..540
FT                   /note="Zinc metalloproteinase nas-10"
FT                   /id="PRO_0000078185"
FT   DOMAIN          293..500
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DOMAIN          504..540
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   ACT_SITE        395
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         394
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         398
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         404
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        339..499
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        365..385
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        504..540
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        511..533
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        520..537
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ   SEQUENCE   540 AA;  60299 MW;  2D00CFE0E69C09E0 CRC64;
     MLSSKLFCVL FFCLGLSNGW PQFDFMNQMG FGGGFNNGPH PNSRPGSRPN SPLGDIFGNI
     NGMVKGITDQ IGKIAQGLDV NNDLGKMAHG PPPPQSEWVE HARRFCRRFP GHPKCRGQLP
     QFNDIGSMLN GILVDSGKWL PKVPFINIRD PLSGINSDLK NALNGIQVQF GQISQQFANN
     IRNICQQMNC KQQQQKNVQM KQAILKQTVD FEKKVFGNNV ADKMNLRFDR TLQLKQALLE
     KAQLKGVVAP EDNGVFDKDL LLTETQANFM LNELGKGGEG AIPMPGSAKA KRASIFFEQN
     LIQKWPSTSP IPYTFDSSLD NLDQNDVRGA ISEIEQKTCI RFKYFASPPK GNHINYQKVN
     SPSFCGLSYI GRVEPANPVY LSFQCGNGRG IAVHETMHAL GVNHQHLRMD RDKHIKVDWS
     NINPQQYDAF VVADSKLYTT YGVKYAYDSI MHYNAYTGAV NIAKPTMIPL VNQQANIGLL
     GQRAKMSNAD VEILNKMYCK SAGCDDKNVY CGAWALQDLC NNPNHNVWMR SNCRKSCNFC