NAS12_CAEEL
ID NAS12_CAEEL Reviewed; 384 AA.
AC Q9XTD6; Q70MT0;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Zinc metalloproteinase nas-12;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 12;
DE Flags: Precursor;
GN Name=nas-12; ORFNames=C24F3.3;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 279-351, 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).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=20109220; DOI=10.1186/1471-213x-10-14;
RA Park J.O., Pan J., Moehrlen F., Schupp M.O., Johnsen R., Baillie D.L.,
RA Zapf R., Moerman D.G., Hutter H.;
RT "Characterization of the astacin family of metalloproteases in C.
RT elegans.";
RL BMC Dev. Biol. 10:14-14(2010).
CC -!- FUNCTION: Metalloprotease. {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}.
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal glands.
CC {ECO:0000269|PubMed:20109220}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL022716; CAA18774.2; -; Genomic_DNA.
DR EMBL; Z81055; CAA18774.2; JOINED; Genomic_DNA.
DR EMBL; AJ561205; CAE47483.1; -; mRNA.
DR PIR; T19421; T19421.
DR RefSeq; NP_501871.2; NM_069470.2.
DR AlphaFoldDB; Q9XTD6; -.
DR SMR; Q9XTD6; -.
DR STRING; 6239.C24F3.3; -.
DR MEROPS; M12.A20; -.
DR EPD; Q9XTD6; -.
DR PaxDb; Q9XTD6; -.
DR PRIDE; Q9XTD6; -.
DR EnsemblMetazoa; C24F3.3.1; C24F3.3.1; WBGene00003531.
DR GeneID; 182848; -.
DR KEGG; cel:CELE_C24F3.3; -.
DR UCSC; C24F3.3; c. elegans.
DR CTD; 182848; -.
DR WormBase; C24F3.3; CE35408; WBGene00003531; nas-12.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00970000196593; -.
DR HOGENOM; CLU_017286_0_3_1; -.
DR InParanoid; Q9XTD6; -.
DR OMA; RWENNIV; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q9XTD6; -.
DR PRO; PR:Q9XTD6; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003531; Expressed in anatomical system and 4 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..25
FT /evidence="ECO:0000255"
FT PROPEP 26..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442659"
FT CHAIN ?..384
FT /note="Zinc metalloproteinase nas-12"
FT /id="PRO_0000028916"
FT DOMAIN 73..271
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 287..325
FT /note="ShKT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DOMAIN 348..384
FT /note="ShKT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT ACT_SITE 165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 137..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 287..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 296..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 305..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 348..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 355..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 364..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 384 AA; 44082 MW; 559AD6489B3B69CC CRC64;
MLYIPQFSIY FCLGYLLLFC KISNAVKQSW EINQELITEA NKEHTVFGDM LLTPAQLIRY
ENSKDSDLSI RGVSIKGSSM NRWSNNIVPY VISPQYSPAQ KQILVSSLRY FERVSCFKFV
ERTTQNDYLF IVPLDGCYSY VGKIGGRQTL SLAADCIADY IIWHEMMHAI GFEHEHQRPD
RDSFIRVDYA NVIPGQMINF DKLKTSHVEY PDIYDFKSIM HYDGYAFGRV DTARRVRLAT
MTPLKPGVTL EDNMKFTATD IEKLNRLGQC GARGGQYSNQ GVVASTCQDV ATAVSCEGNR
RRGMCKNPFY KQMMIKSCQK TCRLCSYTRM IDEDDDLTPN TTVKSVKCED KHPRCDIYSH
NGFCTLPFYD DVRYQLCAKT CNLC
