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SCW10_YEAST
ID   SCW10_YEAST             Reviewed;         389 AA.
AC   Q04951; D6W0D2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Probable family 17 glucosidase SCW10;
DE            EC=3.2.1.-;
DE   AltName: Full=Soluble cell wall protein 10;
DE   Flags: Precursor;
GN   Name=SCW10; OrderedLocusNames=YMR305C; ORFNames=YM9952.07C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   PROTEIN SEQUENCE OF 30-39, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 96099 / S288c / SEY6210;
RX   PubMed=9748433; DOI=10.1128/jb.180.19.5030-5037.1998;
RA   Cappellaro C., Mrsa V., Tanner W.;
RT   "New potential cell wall glucanases of Saccharomyces cerevisiae and their
RT   involvement in mating.";
RL   J. Bacteriol. 180:5030-5037(1998).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Glucanases possibly play a role in cell expansion during
CC       growth, in cell-cell fusion during mating, and in spore release during
CC       sporulation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9748433}.
CC   -!- PTM: Glycosylated.
CC   -!- MISCELLANEOUS: Present with 10500 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; Z49212; CAA89138.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10206.1; -; Genomic_DNA.
DR   PIR; S53975; S53975.
DR   RefSeq; NP_014035.1; NM_001182815.1.
DR   AlphaFoldDB; Q04951; -.
DR   SMR; Q04951; -.
DR   BioGRID; 35485; 50.
DR   DIP; DIP-3845N; -.
DR   IntAct; Q04951; 1.
DR   STRING; 4932.YMR305C; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   iPTMnet; Q04951; -.
DR   MaxQB; Q04951; -.
DR   PaxDb; Q04951; -.
DR   PRIDE; Q04951; -.
DR   EnsemblFungi; YMR305C_mRNA; YMR305C; YMR305C.
DR   GeneID; 855352; -.
DR   KEGG; sce:YMR305C; -.
DR   SGD; S000004921; SCW10.
DR   VEuPathDB; FungiDB:YMR305C; -.
DR   eggNOG; ENOG502QTKT; Eukaryota.
DR   GeneTree; ENSGT00940000176321; -.
DR   HOGENOM; CLU_027285_1_0_1; -.
DR   InParanoid; Q04951; -.
DR   OMA; GTDCDQT; -.
DR   BioCyc; YEAST:YMR305C-MON; -.
DR   PRO; PR:Q04951; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04951; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005576; C:extracellular region; IDA:SGD.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR   GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0015926; F:glucosidase activity; ISS:SGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR   GO; GO:0000747; P:conjugation with cellular fusion; IGI:SGD.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Cell wall biogenesis/degradation;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..29
FT                   /evidence="ECO:0000269|PubMed:9748433"
FT                   /id="PRO_0000011901"
FT   CHAIN           30..389
FT                   /note="Probable family 17 glucosidase SCW10"
FT                   /id="PRO_0000011902"
FT   REGION          70..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        326
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        38..39
FT                   /note="AQ -> QE (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   389 AA;  40469 MW;  21F394BD41337DE1 CRC64;
     MRFSNFLTVS ALLTGALGAP AVRHKHEKRD VVTATVHAQV TVVVSGNSGE TIVPVNENAV
     VATTSSTAVA SQATTSTLEP TTSANVVTSQ QQTSTLQSSE AASTVGSSTS SSPSSSSSTS
     SSASSSASSS ISASGAKGIT YSPYNDDGSC KSTAQVASDL EQLTGFDNIR LYGVDCSQVE
     NVLQAKTSSQ KLFLGIYYVD KIQDAVDTIK SAVESYGSWD DITTVSVGNE LVNGGSATTT
     QVGEYVSTAK SALTSAGYTG SVVSVDTFIA VINNPDLCNY SDYMAVNAHA YFDENTAAQD
     AGPWVLEQIE RVYTACGGKK DVVITETGWP SKGDTYGEAV PSKANQEAAI SSIKSSCGSS
     AYLFTAFNDL WKDDGQYGVE KYWGILSSD
 
 
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