OSBP1_HUMAN
ID OSBP1_HUMAN Reviewed; 807 AA.
AC P22059; Q6P524;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Oxysterol-binding protein 1 {ECO:0000305};
GN Name=OSBP {ECO:0000312|HGNC:HGNC:8503}; Synonyms=OSBP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1970801; DOI=10.1016/0888-7543(90)90519-z;
RA Levanon D., Hsieh C.L., Francke U., Dawson P.A., Ridgway N.D., Brown M.S.,
RA Goldstein J.L.;
RT "cDNA cloning of human oxysterol-binding protein and localization of the
RT gene to human chromosome 11 and mouse chromosome 19.";
RL Genomics 7:65-74(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=11278871; DOI=10.1074/jbc.m011259200;
RA Moreira E.F., Jaworski C., Li A., Rodriguez I.R.;
RT "Molecular and biochemical characterization of a novel oxysterol-binding
RT protein (OSBP2) highly expressed in retina.";
RL J. Biol. Chem. 276:18570-18578(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=15746430; DOI=10.1126/science.1107710;
RA Wang P.-Y., Weng J., Anderson R.G.W.;
RT "OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2
RT activation.";
RL Science 307:1472-1476(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351 AND
RP SER-382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP FUNCTION.
RX PubMed=17428193; DOI=10.1042/bj20070176;
RA Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M., Saarinen H.,
RA Radzikowska A., Thiele C., Olkkonen V.M.;
RT "The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-
RT hydroxycholesterol in an evolutionarily conserved pocket.";
RL Biochem. J. 405:473-480(2007).
RN [7]
RP FUNCTION.
RX PubMed=18450749; DOI=10.1074/jbc.m800918200;
RA Bowden K., Ridgway N.D.;
RT "OSBP negatively regulates ABCA1 protein stability.";
RL J. Biol. Chem. 283:18210-18217(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351;
RP SER-382 AND SER-389, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-198;
RP SER-351 AND SER-382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193 AND SER-351, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351 AND
RP SER-382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193 AND SER-351, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-351, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, FFAT MOTIF, INTERACTION WITH VAPA,
RP AND MUTAGENESIS OF ARG-108 AND 359-PHE-PHE-360.
RX PubMed=24209621; DOI=10.1016/j.cell.2013.09.056;
RA Mesmin B., Bigay J., Moser von Filseck J., Lacas-Gervais S., Drin G.,
RA Antonny B.;
RT "A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P
RT exchange by the ER-Golgi tether OSBP.";
RL Cell 155:830-843(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-238;
RP SER-240; SER-338; SER-351; THR-377; SER-379; SER-382; SER-385; SER-386 AND
RP SER-389, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351;
RP THR-377; SER-382; SER-385 AND SER-386, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP STRUCTURE BY NMR OF 346-379, AND INTERACTION WITH VAPA.
RX PubMed=20178991; DOI=10.1074/jbc.m109.082602;
RA Furuita K., Jee J., Fukada H., Mishima M., Kojima C.;
RT "Electrostatic interaction between oxysterol-binding protein and VAMP-
RT associated protein A revealed by NMR and mutagenesis studies.";
RL J. Biol. Chem. 285:12961-12970(2010).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-278.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [22]
RP SUBCELLULAR LOCATION.
RX PubMed=29514919; DOI=10.1083/jcb.201709123;
RA Sobajima T., Yoshimura S.I., Maeda T., Miyata H., Miyoshi E., Harada A.;
RT "The Rab11-binding protein RELCH/KIAA1468 controls intracellular
RT cholesterol distribution.";
RL J. Cell Biol. 217:1777-1796(2018).
CC -!- FUNCTION: Lipid transporter involved in lipid countertransport between
CC 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 degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum
CC (PubMed:24209621). Binds cholesterol and a range of oxysterols
CC including 25-hydroxycholesterol (PubMed:15746430, PubMed:17428193).
CC Cholesterol binding promotes the formation of a complex with PP2A and a
CC tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-
CC hydroxycholesterol causes its disassembly (PubMed:15746430). Regulates
CC cholesterol efflux by decreasing ABCA1 stability (PubMed:18450749).
CC {ECO:0000269|PubMed:15746430, ECO:0000269|PubMed:17428193,
CC ECO:0000269|PubMed:18450749, ECO:0000269|PubMed:24209621}.
CC -!- SUBUNIT: Homodimer or homotrimer. Interacts (via FFAT motif) with VAPA
CC (PubMed:24209621, PubMed:20178991). Interacts (via C-terminus) with
CC RELCH (via the third HEAT repeat) (By similarity). Found in a complex
CC composed of RELCH, OSBP1 and RAB11A (By similarity).
CC {ECO:0000250|UniProtKB:Q3B7Z2, ECO:0000269|PubMed:20178991,
CC ECO:0000269|PubMed:24209621}.
CC -!- INTERACTION:
CC P22059; Q92685: ALG3; NbExp=2; IntAct=EBI-2681902, EBI-2848814;
CC P22059; O75344: FKBP6; NbExp=3; IntAct=EBI-2681902, EBI-744771;
CC P22059; Q9P0L0: VAPA; NbExp=4; IntAct=EBI-2681902, EBI-1059156;
CC P22059; A0A0H3NDL6: sseL; Xeno; NbExp=3; IntAct=EBI-2681902, EBI-10726249;
CC P22059; Q8ZNG2: sseL; Xeno; NbExp=4; IntAct=EBI-2681902, EBI-10690213;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24209621,
CC ECO:0000269|PubMed:29514919}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:24209621}. Golgi apparatus membrane; Peripheral
CC membrane protein {ECO:0000269|PubMed:24209621}. Endoplasmic reticulum
CC membrane; Peripheral membrane protein {ECO:0000269|PubMed:24209621}.
CC Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:29514919}.
CC Note=Predominantly cytosolic. {ECO:0000269|PubMed:24209621}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11278871}.
CC -!- DOMAIN: The FFAT motif is required for interaction with VATA and proper
CC localization of the protein. {ECO:0000269|PubMed:24209621}.
CC -!- DOMAIN: The PH and the Ala/Gly-rich domains control cholesterol binding
CC without affecting 25-hydroxycholesterol binding.
CC {ECO:0000250|UniProtKB:P16258}.
CC -!- DOMAIN: The second coiled-coil domain is required for interaction with
CC the tyrosine phosphatase. {ECO:0000250|UniProtKB:P16258}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63121.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; M86917; AAA59973.1; -; mRNA.
DR EMBL; AF185696; AAG17011.1; -; mRNA.
DR EMBL; AF185705; AAG28373.1; -; Genomic_DNA.
DR EMBL; AF185697; AAG28373.1; JOINED; Genomic_DNA.
DR EMBL; AF185698; AAG28373.1; JOINED; Genomic_DNA.
DR EMBL; AF185699; AAG28373.1; JOINED; Genomic_DNA.
DR EMBL; AF185700; AAG28373.1; JOINED; Genomic_DNA.
DR EMBL; AF185701; AAG28373.1; JOINED; Genomic_DNA.
DR EMBL; AF185702; AAG28373.1; JOINED; Genomic_DNA.
DR EMBL; AF185703; AAG28373.1; JOINED; Genomic_DNA.
DR EMBL; AF185704; AAG28373.1; JOINED; Genomic_DNA.
DR EMBL; BC011581; AAH11581.1; -; mRNA.
DR EMBL; BC063121; AAH63121.1; ALT_SEQ; mRNA.
DR CCDS; CCDS7974.1; -.
DR PIR; A34581; A34581.
DR RefSeq; NP_002547.1; NM_002556.2.
DR PDB; 2RR3; NMR; -; B=346-379.
DR PDBsum; 2RR3; -.
DR AlphaFoldDB; P22059; -.
DR BMRB; P22059; -.
DR SMR; P22059; -.
DR BioGRID; 111048; 97.
DR ComplexPortal; CPX-489; VAPA-OSBP complex.
DR CORUM; P22059; -.
DR ELM; P22059; -.
DR IntAct; P22059; 25.
DR MINT; P22059; -.
DR STRING; 9606.ENSP00000263847; -.
DR ChEMBL; CHEMBL4523203; -.
DR SwissLipids; SLP:000000490; -.
DR GlyGen; P22059; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P22059; -.
DR MetOSite; P22059; -.
DR PhosphoSitePlus; P22059; -.
DR SwissPalm; P22059; -.
DR BioMuta; OSBP; -.
DR DMDM; 129308; -.
DR EPD; P22059; -.
DR jPOST; P22059; -.
DR MassIVE; P22059; -.
DR MaxQB; P22059; -.
DR PaxDb; P22059; -.
DR PeptideAtlas; P22059; -.
DR PRIDE; P22059; -.
DR ProteomicsDB; 53954; -.
DR Antibodypedia; 27760; 278 antibodies from 32 providers.
DR DNASU; 5007; -.
DR Ensembl; ENST00000263847.6; ENSP00000263847.1; ENSG00000110048.12.
DR GeneID; 5007; -.
DR KEGG; hsa:5007; -.
DR MANE-Select; ENST00000263847.6; ENSP00000263847.1; NM_002556.3; NP_002547.1.
DR UCSC; uc001noc.1; human.
DR CTD; 5007; -.
DR DisGeNET; 5007; -.
DR GeneCards; OSBP; -.
DR HGNC; HGNC:8503; OSBP.
DR HPA; ENSG00000110048; Low tissue specificity.
DR MIM; 167040; gene.
DR neXtProt; NX_P22059; -.
DR OpenTargets; ENSG00000110048; -.
DR PharmGKB; PA32822; -.
DR VEuPathDB; HostDB:ENSG00000110048; -.
DR eggNOG; KOG1737; Eukaryota.
DR GeneTree; ENSGT00940000156164; -.
DR HOGENOM; CLU_007105_5_0_1; -.
DR InParanoid; P22059; -.
DR OMA; EFEMANS; -.
DR OrthoDB; 542090at2759; -.
DR PhylomeDB; P22059; -.
DR TreeFam; TF320922; -.
DR PathwayCommons; P22059; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
DR SignaLink; P22059; -.
DR SIGNOR; P22059; -.
DR BioGRID-ORCS; 5007; 343 hits in 1081 CRISPR screens.
DR ChiTaRS; OSBP; human.
DR EvolutionaryTrace; P22059; -.
DR GeneWiki; OSBP; -.
DR GenomeRNAi; 5007; -.
DR Pharos; P22059; Tbio.
DR PRO; PR:P22059; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P22059; protein.
DR Bgee; ENSG00000110048; Expressed in type B pancreatic cell and 213 other tissues.
DR ExpressionAtlas; P22059; baseline and differential.
DR Genevisible; P22059; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0008142; F:oxysterol binding; TAS:ProtInc.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0120015; F:sterol transfer activity; IDA:GO_Central.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
DR GO; GO:0035627; P:ceramide transport; IMP:ComplexPortal.
DR GO; GO:0032367; P:intracellular cholesterol transport; IMP:UniProtKB.
DR GO; GO:0015914; P:phospholipid transport; IDA:ComplexPortal.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:1904411; P:positive regulation of secretory granule organization; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IMP:ComplexPortal.
DR GO; GO:0015918; P:sterol transport; IDA:UniProtKB.
DR DisProt; DP01491; -.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm; Endoplasmic reticulum;
KW Golgi apparatus; Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..807
FT /note="Oxysterol-binding protein 1"
FT /id="PRO_0000100364"
FT DOMAIN 88..181
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 61..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 291..326
FT /evidence="ECO:0000255"
FT COILED 730..760
FT /evidence="ECO:0000255"
FT MOTIF 358..364
FT /note="FFAT"
FT /evidence="ECO:0000269|PubMed:24209621"
FT COMPBIAS 718..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117..122
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 314
FT /ligand="20-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:1296"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 314
FT /ligand="25-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:42977"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 314
FT /ligand="7beta-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:42989"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 314
FT /ligand="cholesterol"
FT /ligand_id="ChEBI:CHEBI:16113"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 314
FT /ligand="ergosterol"
FT /ligand_id="ChEBI:CHEBI:16933"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 493..496
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 522..523
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 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3B7Z2"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 278
FT /note="D -> A (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036099"
FT MUTAGEN 108
FT /note="R->L: Impaired lipid exchange activity. Induces a
FT shift in subcellular location to the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:24209621"
FT MUTAGEN 359..360
FT /note="FF->AA: Impaired lipid exchange activity. Abolishes
FT interaction with VAPA."
FT /evidence="ECO:0000269|PubMed:24209621"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:2RR3"
SQ SEQUENCE 807 AA; 89421 MW; 2590A47BCB54FDFB CRC64;
MAATELRGVV GPGPAAIAAL GGGGAGPPVV GGGGGRGDAG PGSGAASGTV VAAAAGGPGP
GAGGVAAAGP APAPPTGGSG GSGAGGSGSA REGWLFKWTN YIKGYQRRWF VLSNGLLSYY
RSKAEMRHTC RGTINLATAN ITVEDSCNFI ISNGGAQTYH LKASSEVERQ RWVTALELAK
AKAVKMLAES DESGDEESVS QTDKTELQNT LRTLSSKVED LSTCNDLIAK HGTALQRSLS
ELESLKLPAE SNEKIKQVNE RATLFRITSN AMINACRDFL MLAQTHSKKW QKSLQYERDQ
RIRLEETLEQ LAKQHNHLER AFRGATVLPA NTPGNVGSGK DQCCSGKGDM SDEDDENEFF
DAPEIITMPE NLGHKRTGSN ISGASSDISL DEQYKHQLEE TKKEKRTRIP YKPNYSLNLW
SIMKNCIGKE LSKIPMPVNF NEPLSMLQRL TEDLEYHELL DRAAKCENSL EQLCYVAAFT
VSSYSTTVFR TSKPFNPLLG ETFELDRLEE NGYRSLCEQV SHHPPAAAHH AESKNGWTLR
QEIKITSKFR GKYLSIMPLG TIHCIFHATG HHYTWKKVTT TVHNIIVGKL WIDQSGEIDI
VNHKTGDKCN LKFVPYSYFS RDVARKVTGE VTDPSGKVHF ALLGTWDEKM ECFKVQPVIG
ENGGDARQRG HEAEESRVML WKRNPLPKNA ENMYYFSELA LTLNAWESGT APTDSRLRPD
QRLMENGRWD EANAEKQRLE EKQRLSRKKR EAEAMKATED GTPYDPYKAL WFERKKDPVT
KELTHIYRGE YWECKEKQDW SSCPDIF
