HES1_YEAST
ID HES1_YEAST Reviewed; 434 AA.
AC P35843; D6W2U0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Oxysterol-binding protein homolog 5 {ECO:0000303|PubMed:11238399};
DE AltName: Full=Homologous to KES1 protein 1 {ECO:0000303|PubMed:8017104};
DE Short=Protein HES1 {ECO:0000303|PubMed:8017104};
DE AltName: Full=Oxysterol-binding protein-related protein 5;
DE Short=ORP 5;
DE Short=OSBP-related protein 5;
GN Name=HES1 {ECO:0000303|PubMed:8017104};
GN Synonyms=OSH5 {ECO:0000303|PubMed:11238399}; OrderedLocusNames=YOR237W;
GN ORFNames=O5234;
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 96604 / S288c / FY1679;
RX PubMed=8972580;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1575::aid-yea45>3.0.co;2-e;
RA Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.;
RT "Sequence and analysis of a 26.9 kb fragment from chromosome XV of the
RT yeast Saccharomyces cerevisiae.";
RL Yeast 12:1575-1586(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=16408938; DOI=10.1021/ac051388p;
RA Wiltschi B., Schober M., Kohlwein S.D., Oesterhelt D., Sinner E.K.;
RT "Sterol binding assay using surface plasmon fluorescence spectroscopy.";
RL Anal. Chem. 78:547-555(2006).
RN [9]
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 [10]
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 [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=26928762; DOI=10.1038/nmeth.3795;
RA Yofe I., Weill U., Meurer M., Chuartzman S., Zalckvar E., Goldman O.,
RA Ben-Dor S., Schuetze C., Wiedemann N., Knop M., Khmelinskii A.,
RA Schuldiner M.;
RT "One library to make them all: streamlining the creation of yeast libraries
RT via a SWAp-Tag strategy.";
RL Nat. Methods 13:371-378(2016).
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. Plays a role in ergosterol synthesis
CC (PubMed:15173322, PubMed:11238399, PubMed:16408938, PubMed:20008566).
CC Binds and transports sterol (PubMed:20008566). May be involved in
CC ergosterol transport from the plasma membrane (PM) to the ER
CC (PubMed:16585271). {ECO:0000269|PubMed:11238399,
CC ECO:0000269|PubMed:15173322, ECO:0000269|PubMed:16408938,
CC ECO:0000269|PubMed:16585271, ECO:0000269|PubMed:20008566}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:26928762}.
CC Bud neck {ECO:0000269|PubMed:26928762}.
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:0000305|PubMed:20008566}.
CC -!- MISCELLANEOUS: Present with 1690 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
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DR EMBL; U03914; AAA17737.1; -; Unassigned_DNA.
DR EMBL; Z75145; CAA99458.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11006.1; -; Genomic_DNA.
DR PIR; S42677; S42677.
DR RefSeq; NP_014880.3; NM_001183656.3.
DR AlphaFoldDB; P35843; -.
DR SMR; P35843; -.
DR BioGRID; 34629; 46.
DR STRING; 4932.YOR237W; -.
DR PaxDb; P35843; -.
DR PRIDE; P35843; -.
DR EnsemblFungi; YOR237W_mRNA; YOR237W; YOR237W.
DR GeneID; 854412; -.
DR KEGG; sce:YOR237W; -.
DR SGD; S000005763; HES1.
DR VEuPathDB; FungiDB:YOR237W; -.
DR eggNOG; KOG2210; Eukaryota.
DR GeneTree; ENSGT00940000176691; -.
DR HOGENOM; CLU_012334_0_0_1; -.
DR InParanoid; P35843; -.
DR OMA; ECVYSTA; -.
DR BioCyc; YEAST:G3O-33733-MON; -.
DR Reactome; R-SCE-1482801; Acyl chain remodelling of PS.
DR PRO; PR:P35843; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P35843; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA: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; IDA:SGD.
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; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IGI: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:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0015918; P:sterol transport; IDA:SGD.
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 Lipid biosynthesis; Lipid metabolism; Membrane; Phosphoprotein;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Vacuole.
FT CHAIN 1..434
FT /note="Oxysterol-binding protein homolog 5"
FT /id="PRO_0000100385"
FT REGION 18..371
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:0000250|UniProtKB:P35844"
FT BINDING 96
FT /ligand="20-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:1296"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 96
FT /ligand="25-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:42977"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 96
FT /ligand="7beta-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:42989"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 96
FT /ligand="cholesterol"
FT /ligand_id="ChEBI:CHEBI:16113"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 96
FT /ligand="ergosterol"
FT /ligand_id="ChEBI:CHEBI:16933"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 100
FT /ligand="7beta-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:42989"
FT /evidence="ECO:0000250|UniProtKB:P35844"
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:0000250|UniProtKB:P35844"
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:0000250|UniProtKB:P35844"
FT BINDING 335
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:0000250|UniProtKB:P35844"
FT BINDING 339
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:0000250|UniProtKB:P35844"
FT BINDING 343
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:0000250|UniProtKB:P35844"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35844"
SQ SEQUENCE 434 AA; 49505 MW; 8D7D71C860A91097 CRC64;
MSQHASSSSW TSFLKSISSF NGDLSSLSAP PFILSPTSLT EFSQYWAEHP ALFLEPSLID
GENYKDHCPF DPNVESKEVA QMLAVVRWFI STLRSQYCSR SESMGSEKKP LNPFLGEVFV
GKWKNDEHPE FGETVLLSEQ VSHHPPMTAF SIFNEKNDVS VQGYNQIKTG FTKTLTLTVK
PYGHVILKIK DETYLITTPP LHIEGILVAS PFVELGGRSF IQSSNGMLCV IEFSGRGYFT
GKKNSFKARI YRSPQEHSHK ENALYLISGQ WSGVSTIIKK DSQVSHQFYD SSETPTEHLL
VKPIEEQHPL ESRRAWKDVA EAIRQGNISM IKKTKEELEN KQRALREQER VKGVEWQRRW
FKQVDYMNEN TSNDVEKASE DDAFRKLASK LQLSVKNVPS GTLIGGKDDK KDVSTALHWR
FDKNLWMREN EITI
