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CSR1_YEAST
ID   CSR1_YEAST              Reviewed;         408 AA.
AC   Q06705; D6VZ15; Q6B265;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Phosphatidylinositol transfer protein CSR1;
DE   AltName: Full=CHS5 SPA2 rescue protein 1;
DE   AltName: Full=SEC14 homolog protein 2;
GN   Name=CSR1; Synonyms=SFH2; OrderedLocusNames=YLR380W;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   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.
RX   PubMed=10679005; DOI=10.1091/mbc.11.2.435;
RA   Santos B., Snyder M.;
RT   "Sbe2p and sbe22p, two homologous Golgi proteins involved in yeast cell
RT   wall formation.";
RL   Mol. Biol. Cell 11:435-452(2000).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, PHOSPHATIDYLINOSITOL-BINDING, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=10848624; DOI=10.1091/mbc.11.6.1989;
RA   Li X., Routt S.M., Xie Z., Cui X., Fang M., Kearns M.A., Bard M.,
RA   Kirsch D.R., Bankaitis V.A.;
RT   "Identification of a novel family of nonclassic yeast phosphatidylinositol
RT   transfer proteins whose function modulates phospholipase D activity and
RT   Sec14p-independent cell growth.";
RL   Mol. Biol. Cell 11:1989-2005(2000).
RN   [6]
RP   FUNCTION.
RX   PubMed=12435498; DOI=10.1111/j.1574-6968.2002.tb11431.x;
RA   Regnacq M., Ferreira T., Puard J., Berges T.;
RT   "SUT1 suppresses sec14-1 through upregulation of CSR1 in Saccharomyces
RT   cerevisiae.";
RL   FEMS Microbiol. Lett. 216:165-170(2002).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12869188; DOI=10.1046/j.1432-1033.2003.03688.x;
RA   Schnabl M., Oskolkova O.V., Holic R., Brezna B., Pichler H., Zagorsek M.,
RA   Kohlwein S.D., Paltauf F., Daum G., Griac P.;
RT   "Subcellular localization of yeast Sec14 homologues and their involvement
RT   in regulation of phospholipid turnover.";
RL   Eur. J. Biochem. 270:3133-3145(2003).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH TSA2.
RX   PubMed=12824182; DOI=10.1074/jbc.m301819200;
RA   Cha M.-K., Hong S.-K., Oh Y.-M., Kim I.-H.;
RT   "The protein interaction of Saccharomyces cerevisiae cytoplasmic thiol
RT   peroxidase II with SFH2p and its in vivo function.";
RL   J. Biol. Chem. 278:34952-34958(2003).
RN   [9]
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).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP   ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [11]
RP   FUNCTION.
RX   PubMed=16126894; DOI=10.1073/pnas.0506156102;
RA   Wong T.A., Fairn G.D., Poon P.P., Shmulevitz M., McMaster C.R.,
RA   Singer R.A., Johnston G.C.;
RT   "Membrane metabolism mediated by Sec14 family members influences Arf GTPase
RT   activating protein activity for transport from the trans-Golgi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12777-12782(2005).
RN   [12]
RP   FUNCTION.
RX   PubMed=16262726; DOI=10.1111/j.1600-0854.2005.00350.x;
RA   Routt S.M., Ryan M.M., Tyeryar K., Rizzieri K.E., Mousley C., Roumanie O.,
RA   Brennwald P.J., Bankaitis V.A.;
RT   "Nonclassical PITPs activate PLD via the Stt4p PtdIns-4-kinase and modulate
RT   function of late stages of exocytosis in vegetative yeast.";
RL   Traffic 6:1157-1172(2005).
RN   [13]
RP   FUNCTION.
RX   PubMed=17803462; DOI=10.1042/bj20071028;
RA   Desfougeres T., Ferreira T., Berges T., Regnacq M.;
RT   "SFH2 regulates fatty acid synthase activity in the yeast Saccharomyces
RT   cerevisiae and is critical to prevent saturated fatty acid accumulation in
RT   response to haem and oleic acid depletion.";
RL   Biochem. J. 409:299-309(2008).
CC   -!- FUNCTION: Non-classical phosphatidylinositol (PtdIns) transfer protein
CC       (PITP), which exhibits PtdIns-binding/transfer activity in the absence
CC       of detectable PtdCho-binding/transfer activity. Activates SPO14/PLD1
CC       (phospholipase D1) by stimulating phosphoinositide synthesis via the
CC       STT4 PtdIns 4-kinase. Modulates ArfGAP function through effects on
CC       SPO14 activity. Inhibits phosphatidylcholine degradation by PLB1
CC       (phospholipase B1). May also regulate post-Golgi membrane-trafficking
CC       events and have a role resistance to oxidative stress. Inhibits fatty
CC       acid synthase activity in response to heme depletion and oleic acid
CC       starvation, preventing saturated fatty acid (SFA) accumulation
CC       (PubMed:17803462). {ECO:0000269|PubMed:10679005,
CC       ECO:0000269|PubMed:10848624, ECO:0000269|PubMed:12435498,
CC       ECO:0000269|PubMed:12824182, ECO:0000269|PubMed:12869188,
CC       ECO:0000269|PubMed:16126894, ECO:0000269|PubMed:16262726,
CC       ECO:0000269|PubMed:17803462}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a
CC         1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out);
CC         Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880;
CC         Evidence={ECO:0000269|PubMed:10848624};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC         Evidence={ECO:0000269|PubMed:10848624};
CC   -!- SUBUNIT: Forms a complex with 2 TSA2 subunits. Binds
CC       phosphatidylinositol (PtdIns).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12869188}.
CC       Microsome {ECO:0000269|PubMed:12869188}. Endosome
CC       {ECO:0000269|PubMed:10848624}.
CC   -!- MISCELLANEOUS: Present with 9600 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PITP family. {ECO:0000305}.
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DR   EMBL; U19104; AAB67275.1; -; Genomic_DNA.
DR   EMBL; AY692865; AAT92884.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09681.1; -; Genomic_DNA.
DR   PIR; S51467; S51467.
DR   RefSeq; NP_013484.3; NM_001182269.3.
DR   AlphaFoldDB; Q06705; -.
DR   SMR; Q06705; -.
DR   BioGRID; 31639; 48.
DR   IntAct; Q06705; 2.
DR   MINT; Q06705; -.
DR   STRING; 4932.YLR380W; -.
DR   SwissLipids; SLP:000000355; -.
DR   iPTMnet; Q06705; -.
DR   MaxQB; Q06705; -.
DR   PaxDb; Q06705; -.
DR   PRIDE; Q06705; -.
DR   EnsemblFungi; YLR380W_mRNA; YLR380W; YLR380W.
DR   GeneID; 851096; -.
DR   KEGG; sce:YLR380W; -.
DR   SGD; S000004372; CSR1.
DR   VEuPathDB; FungiDB:YLR380W; -.
DR   eggNOG; KOG1470; Eukaryota.
DR   GeneTree; ENSGT00670000098638; -.
DR   HOGENOM; CLU_016665_2_0_1; -.
DR   InParanoid; Q06705; -.
DR   OMA; VWRVKEM; -.
DR   BioCyc; YEAST:G3O-32446-MON; -.
DR   PRO; PR:Q06705; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q06705; protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005768; C:endosome; IDA:SGD.
DR   GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR   GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:SGD.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IGI:SGD.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IGI:SGD.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IDA:SGD.
DR   GO; GO:1901352; P:negative regulation of phosphatidylglycerol biosynthetic process; IGI:SGD.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IGI:SGD.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0015914; P:phospholipid transport; IDA:SGD.
DR   GO; GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; IGI:SGD.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; -; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR011074; CRAL/TRIO_N_dom.
DR   InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   SMART; SM01100; CRAL_TRIO_N; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF46938; SSF46938; 1.
DR   SUPFAM; SSF52087; SSF52087; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Endoplasmic reticulum; Endosome; Lipid degradation;
KW   Lipid metabolism; Lipid transport; Microsome; Phospholipid degradation;
KW   Phospholipid metabolism; Phosphoprotein; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:15665377"
FT   CHAIN           2..408
FT                   /note="Phosphatidylinositol transfer protein CSR1"
FT                   /id="PRO_0000228155"
FT   DOMAIN          157..317
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:15665377"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377"
FT   CONFLICT        6
FT                   /note="Q -> H (in Ref. 3; AAT92884)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   408 AA;  47463 MW;  BCFBA27D22AC6212 CRC64;
     MSFDRQLTED QEVVLKQIWT HLFHLWQVPV DGTHIFPNNS LHSSSTPAKK KKSSWFSKLQ
     SSDHTQDSSE AAEAAHLYEK GKIHKALANL DPQTTKKQFW HDIKNETPDA TILKFIRARK
     WNADKTIAML GHDLYWRKDT INKIINGGER AVYENNETGV IKNLELQKAT IQGYDNDMRP
     VILVRPRLHH SSDQTEQELE KFSLLVIEQS KLFFKENYPA STTILFDLNG FSMSNMDYAP
     VKFLITCFEA HYPESLGHLL IHKAPWIFNP IWNIIKNWLD PVVASKIVFT KNIDELHKFI
     QPQYIPRYLG GENDNDLDHY TPPDGSLDVH LKDTETRAMI EKEREELVEQ FLTVTAQWIE
     HQPLNDPAYI QLQEKRVQLS TALCENYSKL DPYIRSRSVY DYNGSLKV
 
 
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