NAS20_CAEEL
ID NAS20_CAEEL Reviewed; 379 AA.
AC Q22396; Q7Z0M9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Zinc metalloproteinase nas-20;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 20;
DE Flags: Precursor;
GN Name=nas-20; ORFNames=T11F9.3;
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 158-308, 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185 AND ASN-337, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
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; Z74042; CAA98528.2; -; Genomic_DNA.
DR EMBL; AJ561210; CAD99212.1; -; mRNA.
DR PIR; T24836; T24836.
DR RefSeq; NP_505906.2; NM_073505.6.
DR AlphaFoldDB; Q22396; -.
DR SMR; Q22396; -.
DR STRING; 6239.T11F9.3; -.
DR MEROPS; M12.A42; -.
DR iPTMnet; Q22396; -.
DR EPD; Q22396; -.
DR PaxDb; Q22396; -.
DR PeptideAtlas; Q22396; -.
DR EnsemblMetazoa; T11F9.3.1; T11F9.3.1; WBGene00003539.
DR GeneID; 188420; -.
DR KEGG; cel:CELE_T11F9.3; -.
DR UCSC; T11F9.3; c. elegans.
DR CTD; 188420; -.
DR WormBase; T11F9.3; CE35907; WBGene00003539; nas-20.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000169788; -.
DR HOGENOM; CLU_017286_1_1_1; -.
DR InParanoid; Q22396; -.
DR OMA; MQAMFRD; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q22396; -.
DR PRO; PR:Q22396; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003539; 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 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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..29
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442667"
FT CHAIN 30..379
FT /note="Zinc metalloproteinase nas-20"
FT /id="PRO_0000028924"
FT DOMAIN 30..208
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 203..244
FT /note="EGF-like"
FT ACT_SITE 120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 91..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 209..229
FT /evidence="ECO:0000250"
FT DISULFID 234..243
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 43378 MW; E79F82C99226FB51 CRC64;
MKITVNFLLV ALIGVPSVLS DRHITRDKRQ AMRDYAKWEN NKMSLFFYNL PLEMQAMFRD
AINYLENHTC LKFEYNENAE TAVRIRKGNG CYSLYGMHAG EVQDLTLDYN CASFGTAVHE
IMHALGIAHG QARSDRDDYL IVDSTNSNDG IENTENLVPF DYGSVMLYAR DPHSDKRIPI
DPEYNFTMGS LRVAFYDMVL LNKFYGCNCD NHPRKLDCKN GGYQNPANCE ECLCTDGFNG
QLCDQHEGVY VLEAKKEWDA SGVRNNYRKG IETNTMPEYT YFALTAPEGS TIEVRITKLS
GFFCQHTCDY NGVELKYKTD RRIVSPLVCC DNDNLWNKTR SSTNNPFIIA KYGNNRTPHF
EFEYRYIPGN ATAAPEENN
