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CHS7_YEAST
ID   CHS7_YEAST              Reviewed;         316 AA.
AC   P38843; D3DL91;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Chitin synthase export chaperone;
GN   Name=CHS7; OrderedLocusNames=YHR142W;
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=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10366589; DOI=10.1083/jcb.145.6.1153;
RA   Trilla J.A., Duran A., Roncero C.;
RT   "Chs7p, a new protein involved in the control of protein export from the
RT   endoplasmic reticulum that is specifically engaged in the regulation of
RT   chitin synthesis in Saccharomyces cerevisiae.";
RL   J. Cell Biol. 145:1153-1163(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=11895440; DOI=10.1046/j.1432-1327.2002.02814.x;
RA   Lagorce A., Le Berre-Anton V., Aguilar-Uscanga B., Martin-Yken H.,
RA   Dagkessamanskaia A., Francois J.;
RT   "Involvement of GFA1, which encodes glutamine-fructose-6-phosphate
RT   amidotransferase, in the activation of the chitin synthesis pathway in
RT   response to cell-wall defects in Saccharomyces cerevisiae.";
RL   Eur. J. Biochem. 269:1697-1707(2002).
RN   [6]
RP   FUNCTION.
RX   PubMed=12237852; DOI=10.1002/yea.905;
RA   Carotti C., Ferrario L., Roncero C., Valdivieso M.-H., Duran A., Popolo L.;
RT   "Maintenance of cell integrity in the gas1 mutant of Saccharomyces
RT   cerevisiae requires the Chs3p-targeting and activation pathway and involves
RT   an unusual Chs3p localization.";
RL   Yeast 19:1113-1124(2002).
RN   [7]
RP   FUNCTION.
RX   PubMed=15623581; DOI=10.1083/jcb.200408106;
RA   Kota J., Ljungdahl P.O.;
RT   "Specialized membrane-localized chaperones prevent aggregation of polytopic
RT   proteins in the ER.";
RL   J. Cell Biol. 168:79-88(2005).
RN   [8]
RP   INTERACTION WITH CHS3.
RX   PubMed=16818716; DOI=10.1083/jcb.200602049;
RA   Lam K.K.Y., Davey M., Sun B., Roth A.F., Davis N.G., Conibear E.;
RT   "Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3.";
RL   J. Cell Biol. 174:19-25(2006).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28346351; DOI=10.3390/ijms18040702;
RA   Gohlke S., Muthukrishnan S., Merzendorfer H.;
RT   "In Vitro and In Vivo Studies on the Structural Organization of Chs3 from
RT   Saccharomyces cerevisiae.";
RL   Int. J. Mol. Sci. 18:0-0(2017).
CC   -!- FUNCTION: Chaperone required for the export of the chitin synthase CHS3
CC       from the endoplasmic reticulum. {ECO:0000269|PubMed:10366589,
CC       ECO:0000269|PubMed:11895440, ECO:0000269|PubMed:12237852,
CC       ECO:0000269|PubMed:15623581, ECO:0000269|PubMed:28346351}.
CC   -!- SUBUNIT: Interacts with CHS3. {ECO:0000269|PubMed:16818716}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:10366589}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:10366589}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes CHS3 localization to the bud neck with
CC       increased protein localization to the ER membrane.
CC       {ECO:0000269|PubMed:28346351}.
CC   -!- SIMILARITY: Belongs to the CHS7 family. {ECO:0000305}.
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DR   EMBL; U10397; AAB68984.1; -; Genomic_DNA.
DR   EMBL; AY692978; AAT92997.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06835.1; -; Genomic_DNA.
DR   PIR; S46761; S46761.
DR   RefSeq; NP_012011.1; NM_001179272.1.
DR   AlphaFoldDB; P38843; -.
DR   BioGRID; 36575; 233.
DR   DIP; DIP-5238N; -.
DR   IntAct; P38843; 4.
DR   MINT; P38843; -.
DR   STRING; 4932.YHR142W; -.
DR   MaxQB; P38843; -.
DR   PaxDb; P38843; -.
DR   PRIDE; P38843; -.
DR   EnsemblFungi; YHR142W_mRNA; YHR142W; YHR142W.
DR   GeneID; 856545; -.
DR   KEGG; sce:YHR142W; -.
DR   SGD; S000001184; CHS7.
DR   VEuPathDB; FungiDB:YHR142W; -.
DR   eggNOG; ENOG502QRVH; Eukaryota.
DR   HOGENOM; CLU_050424_1_1_1; -.
DR   InParanoid; P38843; -.
DR   OMA; SKATVWE; -.
DR   BioCyc; YEAST:G3O-31178-MON; -.
DR   PRO; PR:P38843; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38843; protein.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0005934; C:cellular bud tip; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR   GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:SGD.
DR   GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IMP:SGD.
DR   GO; GO:0006457; P:protein folding; IMP:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR022057; Chs7.
DR   PANTHER; PTHR35329; PTHR35329; 1.
DR   Pfam; PF12271; Chs7; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Endoplasmic reticulum; Membrane;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..316
FT                   /note="Chitin synthase export chaperone"
FT                   /id="PRO_0000202922"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   316 AA;  34898 MW;  9DA1EAFA181B2409 CRC64;
     MAFSDFAAIC SKTPLPLCSV IKSKTHLILS NSTIIHDFDP LNLNVGVLPR CYARSIDLAN
     TVIFDVGNAF INIGALGVIL IILYNIRQKY TAIGRSEYLY FFQLTLLLII FTLVVDCGVS
     PPGSGSYPYF VAIQIGLAGA CCWALLIIGF LGFNLWEDGT TKSMLLVRGT SMLGFIANFL
     ASILTFKAWI TDHKVATMNA SGMIVVVYII NAIFLFVFVI CQLLVSLLVV RNLWVTGAIF
     LGLFFFVAGQ VLVYAFSTQI CEGFKHYLDG LFFGSICNVF TLMMVYKTWD MTTDDDLEFG
     VSVSKDGDVV YDNGFM
 
 
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