OSH7_YEAST
ID OSH7_YEAST Reviewed; 437 AA.
AC P38755; D3DKR7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Oxysterol-binding protein homolog 7 {ECO:0000303|PubMed:11238399};
DE AltName: Full=Oxysterol-binding protein-related protein 7;
DE Short=ORP 7;
DE Short=OSBP-related protein 7;
GN Name=OSH7 {ECO:0000303|PubMed:11238399}; OrderedLocusNames=YHR001W;
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 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 [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH VPS4.
RX PubMed=16096648; DOI=10.1038/sj.emboj.7600764;
RA Wang P., Zhang Y., Li H., Chieu H.K., Munn A.L., Yang H.;
RT "AAA ATPases regulate membrane association of yeast oxysterol binding
RT proteins and sterol metabolism.";
RL EMBO J. 24:2989-2999(2005).
RN [8]
RP SUBCELLULAR LOCATION.
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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-276, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=23934110; DOI=10.1038/nature12430;
RA Maeda K., Anand K., Chiapparino A., Kumar A., Poletto M., Kaksonen M.,
RA Gavin A.C.;
RT "Interactome map uncovers phosphatidylserine transport by oxysterol-binding
RT proteins.";
RL Nature 501:257-261(2013).
RN [11]
RP FUNCTION.
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).
CC -!- FUNCTION: ipid 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:15173322). Involved in lipid
CC countertransport between the endoplasmic reticulum and the plasma
CC membrane. Specifically exchanges phosphatidylserine with
CC phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine
CC to the PM in exchange for PI4P, which is delivered to the ER-localized
CC PI4P phosphatase SAC1 for degradation. Thus, by maintaining a PI4P
CC gradient at the ER/PM interface, SAC1 drives PS transport
CC (PubMed:23934110, PubMed:26206936). Binds phosphatidylserine and PI4P
CC in a mutually exclusive manner (PubMed:26206936).
CC {ECO:0000269|PubMed:15173322, ECO:0000269|PubMed:23934110,
CC ECO:0000269|PubMed:26206936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000269|PubMed:23934110};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664;
CC Evidence={ECO:0000269|PubMed:23934110};
CC -!- SUBUNIT: Interacts with the AAA ATPase VPS4; regulates OSH7 membrane
CC association. VPS4 is required for membrane dissociation of OSH7.
CC {ECO:0000269|PubMed:16096648}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16096648}. Cell
CC membrane {ECO:0000269|PubMed:20008566}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20008566, ECO:0000269|PubMed:23934110}.
CC Note=Localizes to the cortical endoplasmic reticulum at the endoplasmic
CC reticulum-plasma membrane contact sites. {ECO:0000269|PubMed:20008566,
CC ECO:0000269|PubMed:23934110}.
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 2350 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; U10555; AAB68425.1; -; Genomic_DNA.
DR EMBL; AY692903; AAT92922.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06687.1; -; Genomic_DNA.
DR PIR; S46796; S46796.
DR RefSeq; NP_011863.1; NM_001179131.1.
DR AlphaFoldDB; P38755; -.
DR SMR; P38755; -.
DR BioGRID; 36425; 120.
DR DIP; DIP-6363N; -.
DR IntAct; P38755; 19.
DR MINT; P38755; -.
DR STRING; 4932.YHR001W; -.
DR TCDB; 2.D.1.1.4; the pi4p/ps counter transporter (p/p-ct) family.
DR iPTMnet; P38755; -.
DR MaxQB; P38755; -.
DR PaxDb; P38755; -.
DR PRIDE; P38755; -.
DR EnsemblFungi; YHR001W_mRNA; YHR001W; YHR001W.
DR GeneID; 856389; -.
DR KEGG; sce:YHR001W; -.
DR SGD; S000001043; OSH7.
DR VEuPathDB; FungiDB:YHR001W; -.
DR eggNOG; KOG2210; Eukaryota.
DR GeneTree; ENSGT00940000154690; -.
DR HOGENOM; CLU_012334_4_2_1; -.
DR InParanoid; P38755; -.
DR OMA; DVHTHKK; -.
DR BioCyc; YEAST:YHR001W-MON; -.
DR Reactome; R-SCE-1482801; Acyl chain remodelling of PS.
DR PRO; PR:P38755; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38755; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0005548; F:phospholipid transporter activity; 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; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IGI:SGD.
DR GO; GO:0006887; P:exocytosis; IGI:SGD.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
DR GO; GO:0030011; P:maintenance of cell polarity; IGI:SGD.
DR GO; GO:0015914; P:phospholipid transport; IDA:UniProtKB.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IGI:SGD.
DR GO; GO:0016125; P:sterol metabolic process; IGI:SGD.
DR GO; GO:0015918; P:sterol transport; IGI: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 Cell membrane; Cytoplasm; Endoplasmic reticulum; Isopeptide bond;
KW Lipid transport; Lipid-binding; Membrane; Reference proteome; Transport;
KW Ubl conjugation.
FT CHAIN 1..437
FT /note="Oxysterol-binding protein homolog 7"
FT /id="PRO_0000100391"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..393
FT /note="OSBP-related domain (ORD)"
FT /evidence="ECO:0000305"
FT BINDING 64..69
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:Q02201"
FT BINDING 64..69
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 126..129
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:Q02201"
FT BINDING 129
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 157..158
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:Q02201"
FT BINDING 183
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 351
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:Q02201"
FT BINDING 355
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:Q02201"
FT BINDING 359
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:Q02201"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 437 AA; 49805 MW; 1C972ED6517D529B CRC64;
MALNKLKNIP SLTNSSHSSI NGIASNAANS KPSGADTDDI DENDESGQSI LLNIISQLKP
GCDLSRITLP TFILEKKSML ERITNQLQFP DVLLEAHSNK DGLQRFVKVV AWYLAGWHIG
PRAVKKPLNP ILGEHFTAYW DLPNKQQAFY IAEQTSHHPP ESAYFYMIPE SNIRVDGVVV
PKSKFLGNSS AAMMEGLTVL QFLDIKDANG KPEKYTLSQP NVYARGILFG KMRIELGDHM
VIMGPKYQVD IEFKTKGFIS GTYDAIEGTI KDYDGKEYYQ ISGKWNDIMY IKDLREKSSK
KTVLFDTHQH FPLAPKVRPL EEQGEYESRR LWKKVTDALA VRDHEVATEE KFQIENRQRE
LAKKRAEDGV EFHSKLFRRA EPGEDLDYYI YKHIPEGTDK HEEQIRSILE TAPILPGQTF
TEKFSIPAYK KHGIQKN
