GenomeNet

Database: UniProt
Entry: P98061
LinkDB: P98061
Original site: P98061 
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   16-JAN-2019, entry version 134.
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
RT   investigating 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
RP   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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD99197.1; Type=Frameshift; Positions=145; Evidence={ECO:0000305};
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   UniGene; Cel.10496; -.
DR   ProteinModelPortal; P98061; -.
DR   MEROPS; M12.A26; -.
DR   iPTMnet; P98061; -.
DR   PaxDb; P98061; -.
DR   PeptideAtlas; P98061; -.
DR   EnsemblMetazoa; F42A10.8; F42A10.8; 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   eggNOG; ENOG410ZPX7; LUCA.
DR   HOGENOM; HOG000022017; -.
DR   InParanoid; P98061; -.
DR   KO; K08076; -.
DR   OMA; QREAPAF; -.
DR   OrthoDB; 681837at2759; -.
DR   PhylomeDB; P98061; -.
DR   PRO; PR:P98061; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003546; Expressed in 4 organ(s), highest expression level in multi-cellular organism.
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   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; PTHR45240:SF3; PTHR45240:SF3; 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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW   Zymogen.
FT   SIGNAL        1     14       {ECO:0000255}.
FT   PROPEP       15    120       {ECO:0000255}.
FT                                /FTId=PRO_0000442675.
FT   CHAIN       121    497       Zinc metalloproteinase nas-28.
FT                                /FTId=PRO_0000028932.
FT   DOMAIN      121    319       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      324    354       EGF-like.
FT   DOMAIN      364    483       CUB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   ACT_SITE    215    215       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       214    214       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       218    218       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       224    224       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   CARBOHYD     76     76       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    317    317       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    394    394       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    164    318       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    185    206       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    328    339       {ECO:0000255|PROSITE-ProRule:PRU00059}.
FT   DISULFID    331    342       {ECO:0000255|PROSITE-ProRule:PRU00059}.
FT   DISULFID    344    353       {ECO:0000255|PROSITE-ProRule:PRU00059}.
FT   DISULFID    364    398       {ECO:0000255|PROSITE-ProRule:PRU00059}.
FT   DISULFID    427    447       {ECO:0000255|PROSITE-ProRule:PRU00059}.
FT   CONFLICT    339    339       C -> G (in Ref. 2; CAD99197).
FT                                {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
//
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