KES1_YEAST
ID KES1_YEAST Reviewed; 434 AA.
AC P35844; D6W3M4; E9P8U8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Oxysterol-binding protein homolog 4 {ECO:0000303|PubMed:11238399};
DE AltName: Full=Bypass SECl4 recessive protein 3 {ECO:0000303|PubMed:8978672};
DE AltName: Full=KRE11-1 suppressor protein 1 {ECO:0000303|PubMed:8017104};
DE Short=Protein KES1 {ECO:0000303|PubMed:8017104};
DE AltName: Full=Oxysterol-binding protein-related protein 4;
DE Short=ORP 4;
DE Short=OSBP-related protein 4;
GN Name=KES1 {ECO:0000303|PubMed:8017104};
GN Synonyms=BSR3 {ECO:0000303|PubMed:8978672},
GN OSH4 {ECO:0000303|PubMed:11238399};
GN OrderedLocusNames=YPL145C {ECO:0000312|SGD:S000006066};
GN ORFNames=LPI3C, P2614;
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 [GENOMIC DNA].
RX PubMed=8017104; DOI=10.1002/yea.320100307;
RA Jiang B., Brown J.L., Sheraton J., Fortin N., Bussey H.;
RT "A new family of yeast genes implicated in ergosterol synthesis is related
RT to the human oxysterol binding protein.";
RL Yeast 10:341-353(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8978672; DOI=10.1002/j.1460-2075.1996.tb01036.x;
RA Fang M., Kearns B.G., Gedvilaite A., Kagiwada S., Kearns M., Fung M.K.,
RA Bankaitis V.A.;
RT "Kes1p shares homology with human oxysterol binding protein and
RT participates in a novel regulatory pathway for yeast Golgi-derived
RT transport vesicle biogenesis.";
RL EMBO J. 15:6447-6459(1996).
RN [7]
RP GENETIC ANALYSIS.
RX PubMed=11238399; DOI=10.1093/genetics/157.3.1117;
RA Beh C.T., Cool L., Phillips J., Rine J.;
RT "Overlapping functions of the yeast oxysterol-binding protein homologues.";
RL Genetics 157:1117-1140(2001).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11916983; DOI=10.1083/jcb.200201037;
RA Li X., Rivas M.P., Fang M., Marchena J., Mehrotra B., Chaudhary A.,
RA Feng L., Prestwich G.D., Bankaitis V.A.;
RT "Analysis of oxysterol binding protein homologue Kes1p function in
RT regulation of Sec14p-dependent protein transport from the yeast Golgi
RT complex.";
RL J. Cell Biol. 157:63-77(2002).
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 FUNCTION.
RX PubMed=15173322; DOI=10.1242/jcs.01157;
RA Beh C.T., Rine J.;
RT "A role for yeast oxysterol-binding protein homologs in endocytosis and in
RT the maintenance of intracellular sterol-lipid distribution.";
RL J. Cell Sci. 117:2983-2996(2004).
RN [11]
RP FUNCTION.
RX PubMed=16585271; DOI=10.1083/jcb.200510084;
RA Raychaudhuri S., Im Y.J., Hurley J.H., Prinz W.A.;
RT "Nonvesicular sterol movement from plasma membrane to ER requires
RT oxysterol-binding protein-related proteins and phosphoinositides.";
RL J. Cell Biol. 173:107-119(2006).
RN [12]
RP DOMAIN.
RX PubMed=17220896; DOI=10.1038/nsmb1194;
RA Drin G., Casella J.F., Gautier R., Boehmer T., Schwartz T.U., Antonny B.;
RT "A general amphipathic alpha-helical motif for sensing membrane
RT curvature.";
RL Nat. Struct. Mol. Biol. 14:138-146(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP FUNCTION, AND DOMAIN.
RX PubMed=20008566; DOI=10.1083/jcb.200905007;
RA Schulz T.A., Choi M.G., Raychaudhuri S., Mears J.A., Ghirlando R.,
RA Hinshaw J.E., Prinz W.A.;
RT "Lipid-regulated sterol transfer between closely apposed membranes by
RT oxysterol-binding protein homologues.";
RL J. Cell Biol. 187:889-903(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-370, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [16]
RP FUNCTION.
RX PubMed=24213531; DOI=10.1242/jcs.132001;
RA Kajiwara K., Ikeda A., Aguilera-Romero A., Castillon G.A., Kagiwada S.,
RA Hanada K., Riezman H., Muniz M., Funato K.;
RT "Osh proteins regulate COPII-mediated vesicular transport of ceramide from
RT the endoplasmic reticulum in budding yeast.";
RL J. Cell Sci. 127:376-387(2014).
RN [17]
RP FUNCTION.
RX PubMed=25849868; DOI=10.1038/ncomms7671;
RA Moser von Filseck J., Vanni S., Mesmin B., Antonny B., Drin G.;
RT "A phosphatidylinositol-4-phosphate powered exchange mechanism to create a
RT lipid gradient between membranes.";
RL Nat. Commun. 6:6671-6671(2015).
RN [18]
RP MUTAGENESIS OF 143-HIS-HIS-144.
RX PubMed=26206936; DOI=10.1126/science.aab1346;
RA Moser von Filseck J., Copic A., Delfosse V., Vanni S., Jackson C.L.,
RA Bourguet W., Drin G.;
RT "Phosphatidylserine transport by ORP/Osh proteins is driven by
RT phosphatidylinositol 4-phosphate.";
RL Science 349:432-436(2015).
RN [19]
RP FUNCTION.
RX PubMed=29487131; DOI=10.1074/jbc.ra117.000596;
RA Tian S., Ohta A., Horiuchi H., Fukuda R.;
RT "Oxysterol-binding protein homologs mediate sterol transport from the
RT endoplasmic reticulum to mitochondria in yeast.";
RL J. Biol. Chem. 293:5636-5648(2018).
RN [20] {ECO:0007744|PDB:1ZHT, ECO:0007744|PDB:1ZHW, ECO:0007744|PDB:1ZHX, ECO:0007744|PDB:1ZHY, ECO:0007744|PDB:1ZHZ, ECO:0007744|PDB:1ZI7}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-434 IN COMPLEXES WITH
RP 20-HYDROXYCHOLESTEROL; 25-HYDROXYCHOLESTEROL; 7BETA-HYDROXYCHOLESTEROL;
RP CHOLESTEROL AND ERGOSTEROL, FUNCTION, DOMAIN, AND MUTAGENESIS OF TYR-97;
RP LYS-109; LEU-111; GLU-117; 143-HIS-HIS-144; LYS-168; LYS-336 AND ARG-344.
RX PubMed=16136145; DOI=10.1038/nature03923;
RA Im Y.J., Raychaudhuri S., Prinz W.A., Hurley J.H.;
RT "Structural mechanism for sterol sensing and transport by OSBP-related
RT proteins.";
RL Nature 437:154-158(2005).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH PHOSPHATIDYLINOSITOL
RP 4-PHOSPHATE, FUNCTION, AND MUTAGENESIS OF LYS-109; ASN-112;
RP 143-HIS-HIS-144; 202-HIS--GLU-204; LYS-336; GLU-340 AND ARG-344.
RX PubMed=22162133; DOI=10.1083/jcb.201104062;
RA de Saint-Jean M., Delfosse V., Douguet D., Chicanne G., Payrastre B.,
RA Bourguet W., Antonny B., Drin G.;
RT "Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid
RT bilayers.";
RL J. Cell Biol. 195:965-978(2011).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 2-434 IN COMPLEX WITH STEROL.
RX PubMed=23756172; DOI=10.1016/j.steroids.2013.05.016;
RA Koag M.C., Cheun Y., Kou Y., Ouzon-Shubeita H., Min K., Monzingo A.F.,
RA Lee S.;
RT "Synthesis and structure of 16,22-diketocholesterol bound to oxysterol-
RT binding protein Osh4.";
RL Steroids 78:938-944(2013).
CC -!- FUNCTION: Lipid transport protein (LTP) involved in non-vesicular
CC transfer of lipids between membranes. Functions in phosphoinositide-
CC coupled directional transport of various lipids by carrying the lipid
CC molecule in a hydrophobic pocket and transfering it between membranes
CC through the cytosol. Involved in maintenance of intracellular sterol
CC distribution and homeostasis (PubMed:20008566, PubMed:15173322,
CC PubMed:16136145, PubMed:22162133). Involved in lipid countertransport
CC between the Golgi complex and membranes of the endoplasmic reticulum.
CC Specifically exchanges sterol with phosphatidylinositol 4-phosphate
CC (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is
CC delivered to the ER-localized PI4P phosphatase SAC1 for degradation.
CC Thus, by maintaining a PI4P gradient at the ER/Golgi interface, SAC1
CC may drive PS transport (PubMed:25849868, PubMed:16136145,
CC PubMed:22162133). Displays a similar affinity for PI4P and sterols
CC (PubMed:22162133). Binds sterol and PI4P in a mutually exclusive manner
CC (PubMed:22162133). Involved in ergosterol transport from the plasma
CC membrane (PM) to the ER (PubMed:16585271). Mediates sterol transport
CC from the ER to mitochondria (PubMed:29487131). Involved in the negative
CC regulation of Golgi-derived transport vesicle biogenesis
CC (PubMed:8978672). Plays a role in the positive regulation of vesicular
CC transport of ceramide from the ER to the Golgi, negatively regulating
CC COPII-mediated ER export of cargos (PubMed:24213531).
CC {ECO:0000269|PubMed:15173322, ECO:0000269|PubMed:16136145,
CC ECO:0000269|PubMed:16585271, ECO:0000269|PubMed:20008566,
CC ECO:0000269|PubMed:22162133, ECO:0000269|PubMed:24213531,
CC ECO:0000269|PubMed:25849868, ECO:0000269|PubMed:29487131,
CC ECO:0000269|PubMed:8978672}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8978672}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:11916983}.
CC -!- DOMAIN: The OSBP-related domain (ORD) mediates binding of sterols and
CC phospholipids. It displays an incomplete beta-barrel containing a
CC central hydrophobic tunnel that can accommodate a single lipid molecule
CC with a flexible lid covering the tunnel entrance. The ORD can bind two
CC membranes simultaneously. It has at least two membrane-binding
CC surfaces; one near the mouth of the lipid-binding pocket and a distal
CC site that can bind a second membrane. These structural features
CC correlate with the phosphatidylinositol 4-phosphate (PI(4)P)-coupled
CC lipid transport optimized in closely apposed membranes, such as
CC organelle contact sites. The lipid transfer cycle starts from the
CC association of the LTP with a donor membrane, which accompanies
CC conformational changes that uncover the ligand-binding pocket. The
CC tunnel opening is generally mediated by displacement of the lid
CC covering the binding pocket allowing uptake or release of a lipid
CC molecule. The LTPs extract the lipid from the membrane by providing a
CC hydrophobic environment as well as specific interaction. Dissociation
CC from the donor membrane shifts the conformation to a closed form. Then,
CC the LTPs loaded with a cargo lipid diffuse through the aqueous phase.
CC Lid opening may be induced by the interaction of a hydrophobic side of
CC the lid with the target membranes. {ECO:0000269|PubMed:16136145,
CC ECO:0000269|PubMed:20008566, ECO:0000269|PubMed:22162133}.
CC -!- DOMAIN: The ArfGAP1 lipid packing sensor (ALPS) motif is a membrane-
CC binding motif that is sensitive to curvature.
CC {ECO:0000269|PubMed:17220896}.
CC -!- MISCELLANEOUS: Present with 32200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
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DR EMBL; U03913; AAA17736.1; -; Unassigned_DNA.
DR EMBL; U43703; AAB68217.1; -; Genomic_DNA.
DR EMBL; X96770; CAA65548.1; -; Genomic_DNA.
DR EMBL; Z73501; CAA97849.1; -; Genomic_DNA.
DR EMBL; AY558047; AAS56373.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11290.1; -; Genomic_DNA.
DR PIR; S42676; S42676.
DR RefSeq; NP_015180.1; NM_001183959.1.
DR PDB; 1ZHT; X-ray; 1.90 A; A=2-434.
DR PDB; 1ZHW; X-ray; 1.70 A; A=2-434.
DR PDB; 1ZHX; X-ray; 1.50 A; A=2-434.
DR PDB; 1ZHY; X-ray; 1.60 A; A=2-434.
DR PDB; 1ZHZ; X-ray; 1.90 A; A=2-434.
DR PDB; 1ZI7; X-ray; 2.50 A; A/B/C=30-434.
DR PDB; 3SPW; X-ray; 2.60 A; A/B=1-434.
DR PDB; 4F4B; X-ray; 1.87 A; A/B=2-434.
DR PDB; 4FES; X-ray; 2.00 A; A/B=2-434.
DR PDB; 4JCH; X-ray; 1.70 A; A/B=2-434.
DR PDBsum; 1ZHT; -.
DR PDBsum; 1ZHW; -.
DR PDBsum; 1ZHX; -.
DR PDBsum; 1ZHY; -.
DR PDBsum; 1ZHZ; -.
DR PDBsum; 1ZI7; -.
DR PDBsum; 3SPW; -.
DR PDBsum; 4F4B; -.
DR PDBsum; 4FES; -.
DR PDBsum; 4JCH; -.
DR AlphaFoldDB; P35844; -.
DR SMR; P35844; -.
DR BioGRID; 36038; 296.
DR DIP; DIP-2867N; -.
DR IntAct; P35844; 13.
DR MINT; P35844; -.
DR STRING; 4932.YPL145C; -.
DR iPTMnet; P35844; -.
DR MaxQB; P35844; -.
DR PaxDb; P35844; -.
DR PRIDE; P35844; -.
DR EnsemblFungi; YPL145C_mRNA; YPL145C; YPL145C.
DR GeneID; 855958; -.
DR KEGG; sce:YPL145C; -.
DR SGD; S000006066; KES1.
DR VEuPathDB; FungiDB:YPL145C; -.
DR eggNOG; KOG2210; Eukaryota.
DR GeneTree; ENSGT00940000176691; -.
DR HOGENOM; CLU_012334_0_0_1; -.
DR InParanoid; P35844; -.
DR OMA; SSYWTEH; -.
DR BioCyc; YEAST:G3O-34042-MON; -.
DR Reactome; R-SCE-1482801; Acyl chain remodelling of PS.
DR Reactome; R-SCE-192105; Synthesis of bile acids and bile salts.
DR EvolutionaryTrace; P35844; -.
DR PRO; PR:P35844; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P35844; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:0008142; F:oxysterol binding; IMP:SGD.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:SGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IMP:SGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0120015; F:sterol transfer activity; IDA:SGD.
DR GO; GO:0015248; F:sterol transporter activity; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IGI:SGD.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; IGI:SGD.
DR GO; GO:0030011; P:maintenance of cell polarity; IGI:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IGI:SGD.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; IDA:SGD.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IGI:SGD.
DR GO; GO:0006665; P:sphingolipid metabolic process; IMP:SGD.
DR GO; GO:0015918; P:sterol transport; IDA:UniProtKB.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Golgi apparatus; Lipid transport; Lipid-binding;
KW Membrane; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..434
FT /note="Oxysterol-binding protein homolog 4"
FT /id="PRO_0000100386"
FT REGION 7..29
FT /note="ALPS motif"
FT /evidence="ECO:0000305|PubMed:17220896"
FT REGION 16..366
FT /note="OSBP-related domain (ORD)"
FT /evidence="ECO:0000305"
FT BINDING 24..29
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:22162133,
FT ECO:0007744|PDB:3SPW"
FT BINDING 96
FT /ligand="20-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:1296"
FT /evidence="ECO:0000269|PubMed:16136145,
FT ECO:0007744|PDB:1ZHW"
FT BINDING 96
FT /ligand="25-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:42977"
FT /evidence="ECO:0007744|PDB:1ZHX"
FT BINDING 96
FT /ligand="7beta-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:42989"
FT /evidence="ECO:0007744|PDB:1ZHT"
FT BINDING 96
FT /ligand="cholesterol"
FT /ligand_id="ChEBI:CHEBI:16113"
FT /evidence="ECO:0007744|PDB:1ZHY"
FT BINDING 96
FT /ligand="ergosterol"
FT /ligand_id="ChEBI:CHEBI:16933"
FT /evidence="ECO:0007744|PDB:1ZHZ"
FT BINDING 100
FT /ligand="7beta-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:42989"
FT /evidence="ECO:0007744|PDB:1ZHT"
FT BINDING 109..112
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:22162133,
FT ECO:0007744|PDB:3SPW"
FT BINDING 143..144
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:22162133,
FT ECO:0007744|PDB:3SPW"
FT BINDING 336
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:22162133,
FT ECO:0007744|PDB:3SPW"
FT BINDING 340
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:22162133,
FT ECO:0007744|PDB:3SPW"
FT BINDING 344
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:22162133,
FT ECO:0007744|PDB:3SPW"
FT MOD_RES 370
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 97
FT /note="Y->F: Abolishes both cholesterol binding and
FT biological function."
FT /evidence="ECO:0000269|PubMed:16136145"
FT MUTAGEN 109
FT /note="K->A: Strong reduction in cholesterol transport.
FT Abolishes binding to phosphatidylinositol 4-phosphate."
FT /evidence="ECO:0000269|PubMed:16136145,
FT ECO:0000269|PubMed:22162133"
FT MUTAGEN 111
FT /note="L->D: Abolishes both cholesterol binding and
FT biological function."
FT /evidence="ECO:0000269|PubMed:16136145"
FT MUTAGEN 112
FT /note="N->E: Abolishes binding to phosphatidylinositol 4-
FT phosphate."
FT /evidence="ECO:0000269|PubMed:22162133"
FT MUTAGEN 117
FT /note="E->A: Abolishes both cholesterol binding and
FT biological function."
FT /evidence="ECO:0000269|PubMed:16136145"
FT MUTAGEN 143..144
FT /note="HH->AA: Reduction in cholesterol transport.
FT Abolishes binding to phosphatidylinositol 4-phosphate."
FT /evidence="ECO:0000269|PubMed:16136145,
FT ECO:0000269|PubMed:22162133, ECO:0000269|PubMed:26206936"
FT MUTAGEN 168
FT /note="K->A: Slight reduction in cholesterol transport."
FT /evidence="ECO:0000269|PubMed:16136145"
FT MUTAGEN 168
FT /note="K->A: Strong reduction in cholesterol transport."
FT /evidence="ECO:0000269|PubMed:16136145"
FT MUTAGEN 202..204
FT /note="HIE->AIA: Strong reduction in cholesterol binding
FT without affecting phosphatidylinositol 4-phosphate
FT binding."
FT /evidence="ECO:0000269|PubMed:22162133"
FT MUTAGEN 336
FT /note="K->A: Strong reduction in cholesterol transport.
FT Abolishes binding to phosphatidylinositol 4-phosphate."
FT /evidence="ECO:0000269|PubMed:16136145,
FT ECO:0000269|PubMed:22162133"
FT MUTAGEN 340
FT /note="E->A: Abolishes binding to phosphatidylinositol 4-
FT phosphate."
FT /evidence="ECO:0000269|PubMed:22162133"
FT MUTAGEN 344
FT /note="R->A: Slight reduction in cholesterol transport.
FT Abolishes binding to phosphatidylinositol 4-phosphate."
FT /evidence="ECO:0000269|PubMed:16136145,
FT ECO:0000269|PubMed:22162133"
FT CONFLICT 355
FT /note="I -> T (in Ref. 5; AAS56373)"
FT /evidence="ECO:0000305"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:1ZHX"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1ZI7"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1ZHX"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 77..104
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1ZHX"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:1ZHX"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1ZHX"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 159..171
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1ZI7"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1ZHX"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 241..253
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:1ZHX"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 329..353
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:1ZI7"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 383..391
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:1ZHX"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:1ZHX"
FT HELIX 423..427
FT /evidence="ECO:0007829|PDB:1ZHX"
SQ SEQUENCE 434 AA; 49492 MW; 360E4A46ABE2D87B CRC64;
MSQYASSSSW TSFLKSIASF NGDLSSLSAP PFILSPISLT EFSQYWAEHP ELFLEPSFIN
DDNYKEHCLI DPEVESPELA RMLAVTKWFI STLKSQYCSR NESLGSEKKP LNPFLGELFV
GKWENKEHPE FGETVLLSEQ VSHHPPVTAF SIFNDKNKVK LQGYNQIKAS FTKSLMLTVK
QFGHTMLDIK DESYLVTPPP LHIEGILVAS PFVELEGKSY IQSSTGLLCV IEFSGRGYFS
GKKNSFKARI YKDSKDSKDK EKALYTISGQ WSGSSKIIKA NKKEESRLFY DAARIPAEHL
NVKPLEEQHP LESRKAWYDV AGAIKLGDFN LIAKTKTELE ETQRELRKEE EAKGISWQRR
WFKDFDYSVT PEEGALVPEK DDTFLKLASA LNLSTKNAPS GTLVGDKEDR KEDLSSIHWR
FQRELWDEEK EIVL
