NAS28_CAEEL
ID NAS28_CAEEL Reviewed; 497 AA.
AC P98061; Q7Z0P0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 4.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Zinc metalloproteinase nas-28;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 28;
DE Flags: Precursor;
GN Name=nas-28; ORFNames=F42A10.8;
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 67-404.
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-317, AND IDENTIFICATION BY MASS
RP 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD99197.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; FO080631; CCD65318.1; -; Genomic_DNA.
DR EMBL; AJ561217; CAD99197.1; ALT_FRAME; mRNA.
DR PIR; T30963; T30963.
DR RefSeq; NP_498342.3; NM_065941.3.
DR AlphaFoldDB; P98061; -.
DR SMR; P98061; -.
DR MEROPS; M12.A26; -.
DR iPTMnet; P98061; -.
DR PaxDb; P98061; -.
DR PeptideAtlas; P98061; -.
DR EnsemblMetazoa; F42A10.8.1; F42A10.8.1; WBGene00003546.
DR GeneID; 185658; -.
DR KEGG; cel:CELE_F42A10.8; -.
DR UCSC; F42A10.8; c. elegans.
DR CTD; 185658; -.
DR WormBase; F42A10.8; CE38958; WBGene00003546; nas-28.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_017286_1_5_1; -.
DR InParanoid; P98061; -.
DR OMA; FESDIML; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; P98061; -.
DR PRO; PR:P98061; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003546; Expressed in embryo and 3 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:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR017050; Metallopeptidase_nem.
DR InterPro; IPR031065; Nas-28.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR10127:SF793; PTHR10127:SF793; 1.
DR Pfam; PF01400; Astacin; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 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..14
FT /evidence="ECO:0000255"
FT PROPEP 15..120
FT /evidence="ECO:0000255"
FT /id="PRO_0000442675"
FT CHAIN 121..497
FT /note="Zinc metalloproteinase nas-28"
FT /id="PRO_0000028932"
FT DOMAIN 121..319
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 324..354
FT /note="EGF-like"
FT DOMAIN 364..483
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT ACT_SITE 215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 164..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 185..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 328..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 331..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 344..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 364..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 427..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT CONFLICT 339
FT /note="C -> G (in Ref. 2; CAD99197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 55786 MW; 7E348EB780FC0B64 CRC64;
MFFPVVFFIP FVLGAPTQKA LEKILVDNNP DSVTNREKIR GIIDKAFENR VPRVQGRQGV
APPVTFAALN YGPKNNQTKK FEELNQDINE YTFESDIMLN EKQAKHIATA IENGNYRSKR
QAIVDTTNFW SVSVPIFYQF DTKLSATNIA NVRKAIQFWN DNSCLSFKED NNAKNRLFLS
SAGGCWSYVG KQVDMPYQMV SVGPNCDTFG TATHELMHAI GFWHQQSRAD RDNYVYVDFS
NIIPSQAYNF QKMAVDQAQL LNLPYDYGSV MQYYPYAFAV DSSKYTILAK ENGFQNSMGQ
REAPAFSDII GVNKLYNCTS QCKIQMKCSN CGITDSRNCN QCKCPRYFTG ASCDSLPSGT
APNCNGAVLQ ATSSWETFDA KAGDPSSFSS STDNSTNCYW HIKAPEGQQI EFKMTKTPLA
AICMQECPWQ SIEVNLGKFD LFGMITCCDT ILNQVFTSEL NMIALRGIIR YNQLTFSIQY
RAVPSSKPAS TNACLNQ
