NAS19_CAEEL
ID NAS19_CAEEL Reviewed; 396 AA.
AC Q21181; Q7Z0N0;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Zinc metalloproteinase nas-19;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 19;
DE Flags: Precursor;
GN Name=nas-19; ORFNames=K03B8.5;
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 103-135, 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}.
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DR EMBL; Z74039; CAA98504.2; -; Genomic_DNA.
DR EMBL; AJ561209; CAD99211.1; -; mRNA.
DR PIR; T23266; T23266.
DR RefSeq; NP_505893.2; NM_073492.2.
DR AlphaFoldDB; Q21181; -.
DR SMR; Q21181; -.
DR STRING; 6239.K03B8.5; -.
DR MEROPS; M12.A33; -.
DR PaxDb; Q21181; -.
DR PeptideAtlas; Q21181; -.
DR EnsemblMetazoa; K03B8.5.1; K03B8.5.1; WBGene00003538.
DR GeneID; 186926; -.
DR KEGG; cel:CELE_K03B8.5; -.
DR UCSC; K03B8.5; c. elegans.
DR CTD; 186926; -.
DR WormBase; K03B8.5; CE47588; WBGene00003538; nas-19.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000169788; -.
DR HOGENOM; CLU_017286_1_1_1; -.
DR InParanoid; Q21181; -.
DR OMA; IRINIEF; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q21181; -.
DR PRO; PR:Q21181; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003538; Expressed in material anatomical entity 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 Gene3D; 3.40.390.10; -; 1.
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 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442666"
FT CHAIN ?..396
FT /note="Zinc metalloproteinase nas-19"
FT /id="PRO_0000028923"
FT DOMAIN 38..231
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 225..264
FT /note="EGF-like"
FT ACT_SITE 139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 105..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 232..252
FT /evidence="ECO:0000250"
FT DISULFID 254..263
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 45162 MW; 9CA113C33D81C137 CRC64;
MVRLIHLIGA IILLFSYAYC GLSRLNEHDI EESYSHKRVK RQFERLGTKW SYGVVNYYYA
DKNNEIKEMV ESAIAYIANH TCIRFNEDQN AVQRVQIRMQ QNWLCQSTVG APGMSMSKPI
GELSMLVQSC DTIGSIVHEF SHSLGRFHEH TRPDRDNFMK VTTTVHEARP RPSGMTTMYG
PFEHGSVMMY HADTYGPGTM DPLDMDYKQT MGNRRVTFYD MYKINQYYGC WCSKQLECKN
GGYTSPSDCS RCNCPKGFFG NLCDERQQDS YELMAVNNLW QSITIPFAYK PEPGSDGFYS
TFVYITGKAN STIEITLEGL QDVICTAGCT VNGVEIKFKE DSKITSPVVC CTDKPPYKNV
FKSSHNPTII ELYSRTTLPS AVTFKYRFTN DKVVLG
