ID OSBL6_HUMAN Reviewed; 934 AA. AC Q9BZF3; B4DTW1; C4AMC0; C4AME4; D3DPF6; D3DPF7; Q4ZG68; Q53T68; Q59H61; AC Q7Z4Q1; Q86V84; Q8N9T0; Q96SR1; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 12-AUG-2020, entry version 163. DE RecName: Full=Oxysterol-binding protein-related protein 6; DE Short=ORP-6; DE Short=OSBP-related protein 6; GN Name=OSBPL6; Synonyms=ORP6; 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] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=11483621; RA Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C., Staels B., RA Ikonen E., Olkkonen V.M.; RT "The OSBP-related protein family in humans."; RL J. Lipid Res. 42:1203-1213(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11735225; DOI=10.1006/geno.2001.6663; RA Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R.; RT "A family of 12 human genes containing oxysterol-binding domains."; RL Genomics 78:185-196(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Guo J.H., Zan Q., Yu L.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 195-934 (ISOFORM 1). RC TISSUE=Placenta, Teratocarcinoma, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). RC TISSUE=Lung; 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 [9] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=14593528; DOI=10.1007/s00441-003-0817-y; RA Lehto M., Tienari J., Lehtonen S., Lehtonen E., Olkkonen V.M.; RT "Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: RT the expression and intracellular localization of ORP3, ORP6, and ORP7."; RL Cell Tissue Res. 315:39-57(2004). RN [10] 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [13] 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 [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-190 AND SER-290, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [16] RP IDENTIFICATION BY MASS 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 [17] RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=26941018; DOI=10.1161/atvbaha.116.307282; RA Ouimet M., Hennessy E.J., van Solingen C., Koelwyn G.J., Hussein M.A., RA Ramkhelawon B., Rayner K.J., Temel R.E., Perisic L., Hedin U., RA Maegdefessel L., Garabedian M.J., Holdt L.M., Teupser D., Moore K.J.; RT "miRNA Targeting of Oxysterol-Binding Protein-Like 6 Regulates Cholesterol RT Trafficking and Efflux."; RL Arterioscler. Thromb. Vasc. Biol. 36:942-951(2016). RN [18] RP SUBCELLULAR LOCATION. RX PubMed=30028970; DOI=10.1016/j.yexcr.2018.07.025; RA Mochizuki S., Miki H., Zhou R., Kido Y., Nishimura W., Kikuchi M., Noda Y.; RT "Oxysterol-binding protein-related protein (ORP) 6 localizes to the ER and RT ER-plasma membrane contact sites and is involved in the turnover of PI4P in RT cerebellar granule neurons."; RL Exp. Cell Res. 370:601-612(2018). CC -!- FUNCTION: Regulates cellular transport and efflux of cholesterol CC (PubMed:26941018). Plays a role in phosphatidylinositol-4-phophate CC (PI4P) turnover at the neuronal membrane (By similarity). Binds via its CC PH domain PI4P, phosphatidylinositol-4,5-diphosphate, CC phosphatidylinositol-3,4,5-triphosphate, and phosphatidic acid (By CC similarity). Weakly binds 25-hydroxycholesterol (PubMed:17428193). CC {ECO:0000250|UniProtKB:Q8BXR9, ECO:0000269|PubMed:17428193, CC ECO:0000269|PubMed:26941018}. CC -!- SUBUNIT: Homodimer (By similarity). Interacts with OSBPL3 (By CC similarity). {ECO:0000250|UniProtKB:Q8BXR9}. CC -!- INTERACTION: CC Q9BZF3; Q9Q2G4: ORF; Xeno; NbExp=3; IntAct=EBI-2372709, EBI-6248094; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14593528, CC ECO:0000269|PubMed:30028970}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:26941018, CC ECO:0000269|PubMed:30028970}; Peripheral membrane protein CC {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:14593528}. Cell CC membrane {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:30028970}; CC Peripheral membrane protein {ECO:0000305}. Endosome membrane CC {ECO:0000269|PubMed:26941018}; Peripheral membrane protein CC {ECO:0000305}. Note=Co-localizes with OSBPL3 at contact sites between CC the plasma membrane and the endoplasmic reticulum. CC {ECO:0000250|UniProtKB:Q8BXR9}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q9BZF3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BZF3-2; Sequence=VSP_010013; CC Name=3; CC IsoId=Q9BZF3-3; Sequence=VSP_036559, VSP_036561; CC Name=4; CC IsoId=Q9BZF3-4; Sequence=VSP_036560; CC Name=5; CC IsoId=Q9BZF3-5; Sequence=VSP_036561; CC Name=6; CC IsoId=Q9BZF3-6; Sequence=VSP_036560, VSP_010013, VSP_054430, CC VSP_054431; CC -!- TISSUE SPECIFICITY: Expressed in brain and striated muscle (at protein CC level) (PubMed:14593528). Widely expressed (PubMed:11735225). Expressed CC in skeletal muscle (PubMed:14593528). CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain and lung. CC {ECO:0000269|PubMed:14593528}. CC -!- INDUCTION: By acetylated low-density lipoprotein. CC {ECO:0000269|PubMed:26941018}. CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB55223.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAD92135.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF323728; AAG53409.1; -; mRNA. DR EMBL; AF392448; AAL40661.1; -; mRNA. DR EMBL; AF462443; AAP97711.1; -; mRNA. DR EMBL; AK027600; BAB55223.1; ALT_INIT; mRNA. DR EMBL; AK093902; BAC04248.1; -; mRNA. DR EMBL; AK300389; BAG62123.1; -; mRNA. DR EMBL; AB208898; BAD92135.1; ALT_INIT; mRNA. DR EMBL; AC009948; AAX88881.1; -; Genomic_DNA. DR EMBL; AC011743; AAY15090.1; -; Genomic_DNA. DR EMBL; AC011238; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471058; EAX11040.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11041.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11042.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11043.1; -; Genomic_DNA. DR EMBL; BC052259; AAH52259.1; -; mRNA. DR CCDS; CCDS2277.1; -. [Q9BZF3-1] DR CCDS; CCDS2278.1; -. [Q9BZF3-3] DR CCDS; CCDS56150.1; -. [Q9BZF3-5] DR CCDS; CCDS56151.1; -. [Q9BZF3-2] DR CCDS; CCDS56152.1; -. [Q9BZF3-4] DR RefSeq; NP_001188409.1; NM_001201480.1. [Q9BZF3-5] DR RefSeq; NP_001188410.1; NM_001201481.1. [Q9BZF3-4] DR RefSeq; NP_001188411.1; NM_001201482.1. [Q9BZF3-2] DR RefSeq; NP_115912.1; NM_032523.3. [Q9BZF3-1] DR RefSeq; NP_665682.1; NM_145739.2. [Q9BZF3-3] DR RefSeq; XP_016858755.1; XM_017003266.1. [Q9BZF3-5] DR RefSeq; XP_016858756.1; XM_017003267.1. [Q9BZF3-5] DR RefSeq; XP_016858759.1; XM_017003270.1. [Q9BZF3-4] DR RefSeq; XP_016858760.1; XM_017003271.1. [Q9BZF3-2] DR SMR; Q9BZF3; -. DR BioGRID; 125381; 53. DR ELM; Q9BZF3; -. DR IntAct; Q9BZF3; 27. DR MINT; Q9BZF3; -. DR STRING; 9606.ENSP00000376293; -. DR iPTMnet; Q9BZF3; -. DR PhosphoSitePlus; Q9BZF3; -. DR BioMuta; OSBPL6; -. DR DMDM; 20139133; -. DR EPD; Q9BZF3; -. DR jPOST; Q9BZF3; -. DR MassIVE; Q9BZF3; -. DR MaxQB; Q9BZF3; -. DR PaxDb; Q9BZF3; -. DR PeptideAtlas; Q9BZF3; -. DR PRIDE; Q9BZF3; -. DR ProteomicsDB; 69974; -. DR ProteomicsDB; 79831; -. [Q9BZF3-1] DR ProteomicsDB; 79832; -. [Q9BZF3-2] DR ProteomicsDB; 79833; -. [Q9BZF3-3] DR ProteomicsDB; 79834; -. [Q9BZF3-4] DR ProteomicsDB; 79835; -. [Q9BZF3-5] DR Antibodypedia; 33930; 124 antibodies. DR Ensembl; ENST00000190611; ENSP00000190611; ENSG00000079156. [Q9BZF3-1] DR Ensembl; ENST00000315022; ENSP00000318723; ENSG00000079156. [Q9BZF3-3] DR Ensembl; ENST00000357080; ENSP00000349591; ENSG00000079156. [Q9BZF3-6] DR Ensembl; ENST00000359685; ENSP00000352713; ENSG00000079156. [Q9BZF3-2] DR Ensembl; ENST00000392505; ENSP00000376293; ENSG00000079156. [Q9BZF3-5] DR Ensembl; ENST00000409045; ENSP00000387248; ENSG00000079156. [Q9BZF3-4] DR Ensembl; ENST00000409631; ENSP00000386885; ENSG00000079156. [Q9BZF3-2] DR GeneID; 114880; -. DR KEGG; hsa:114880; -. DR UCSC; uc002ulw.4; human. [Q9BZF3-1] DR CTD; 114880; -. DR DisGeNET; 114880; -. DR EuPathDB; HostDB:ENSG00000079156.16; -. DR GeneCards; OSBPL6; -. DR HGNC; HGNC:16388; OSBPL6. DR HPA; ENSG00000079156; Tissue enhanced (skeletal). DR MIM; 606734; gene. DR neXtProt; NX_Q9BZF3; -. DR OpenTargets; ENSG00000079156; -. DR PharmGKB; PA32830; -. DR eggNOG; KOG1737; Eukaryota. DR GeneTree; ENSGT00940000156791; -. DR HOGENOM; CLU_007105_4_1_1; -. DR InParanoid; Q9BZF3; -. DR KO; K20463; -. DR OMA; SESIICE; -. DR OrthoDB; 542090at2759; -. DR PhylomeDB; Q9BZF3; -. DR TreeFam; TF320922; -. DR PathwayCommons; Q9BZF3; -. DR Reactome; R-HSA-192105; Synthesis of bile acids and bile salts. DR BioGRID-ORCS; 114880; 4 hits in 878 CRISPR screens. DR ChiTaRS; OSBPL6; human. DR GenomeRNAi; 114880; -. DR Pharos; Q9BZF3; Tbio. DR PRO; PR:Q9BZF3; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9BZF3; protein. DR Bgee; ENSG00000079156; Expressed in bronchial epithelial cell and 199 other tissues. DR Genevisible; Q9BZF3; HS. DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL. DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0031965; C:nuclear membrane; IDA:BHF-UCL. DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central. DR GO; GO:0008289; F:lipid binding; IBA:GO_Central. DR GO; GO:0032934; F:sterol binding; IBA: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:0032374; P:regulation of cholesterol transport; IMP:UniProtKB. 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; IPR041680; PH_8. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR10972; PTHR10972; 1. DR Pfam; PF01237; Oxysterol_BP; 1. DR Pfam; PF15409; PH_8; 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 Acetylation; Alternative splicing; Cell membrane; Cytoplasm; KW Endoplasmic reticulum; Endosome; Lipid transport; Lipid-binding; Membrane; KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000244|PubMed:19369195" FT CHAIN 2..934 FT /note="Oxysterol-binding protein-related protein 6" FT /id="PRO_0000100375" FT DOMAIN 86..181 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000244|PubMed:19369195" FT MOD_RES 35 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 290 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT VAR_SEQ 1..34 FT /note="MSSDEKGISPAHKTSTPTHRSASSSTSSQRDSRQ -> MHQLSLIRGNRGR FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_036559" FT VAR_SEQ 298..328 FT /note="Missing (in isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_036560" FT VAR_SEQ 329 FT /note="Q -> QEGPPAKGQFSTTRRRQRLAAAVATT (in isoform 3 and FT isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.5" FT /id="VSP_036561" FT VAR_SEQ 431..466 FT /note="Missing (in isoform 2 and isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_010013" FT VAR_SEQ 541..575 FT /note="ILNGELTGGAFRNGRRACLPAPCPDTSNINLWNIL -> SMHHLSFQVVLST FT CQIATRRLNEQAFPLPRHPHPC (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054430" FT VAR_SEQ 576..934 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054431" FT VARIANT 53 FT /note="R -> Q (in dbSNP:rs35032920)" FT /id="VAR_057663" FT VARIANT 58 FT /note="P -> L (in dbSNP:rs34874235)" FT /id="VAR_053550" FT CONFLICT 319 FT /note="S -> G (in Ref. 4; BAB55223)" FT /evidence="ECO:0000305" FT CONFLICT 350 FT /note="A -> V (in Ref. 4; BAG62123)" FT /evidence="ECO:0000305" FT CONFLICT 487 FT /note="S -> P (in Ref. 4; BAC04248)" FT /evidence="ECO:0000305" FT CONFLICT 714 FT /note="N -> S (in Ref. 4; BAB55223)" FT /evidence="ECO:0000305" SQ SEQUENCE 934 AA; 106306 MW; D20F90EA34C81497 CRC64; MSSDEKGISP AHKTSTPTHR SASSSTSSQR DSRQSIHILE RTASSSTEPS VSRQLLEPEP VPLSKEADSW EIIEGLKIGQ TNVQKPDKHE GFMLKKRKWP LKGWHKRFFV LDNGMLKYSK APLDIQKGKV HGSIDVGLSV MSIKKKARRI DLDTEEHIYH LKVKSQDWFD AWVSKLRHHR LYRQNEIVRS PRDASFHIFP STSTAESSPA ANVSVMDGKM QPNSFPWQSP LPCSNSLPAT CTTGQSKVAA WLQDSEEMDR CAEDLAHCQS NLVELSKLLQ NLEILQRTQS APNFTDMQAN CVDISKKDKR VTRRWRTKSV SKDTKIQLQV PFSATMSPVR LHSSNPNLCA DIEFQTPPSH LTDPLESSTD YTKLQEEFCL IAQKVHSLLK SAFNSIAIEK EKLKQMVSEQ DHSKGHSTQM ARLRQSLSQA LNQNAELRSR LNRIHSESII CDQVVSVNII PSPDEAGEQI HVSLPLSQQV ANESRLSMSE SVSEFFDAQE VLLSASSSEN EASDDESYIS DVSDNISEDN TSVADNISRQ ILNGELTGGA FRNGRRACLP APCPDTSNIN LWNILRNNIG KDLSKVSMPV ELNEPLNTLQ HLCEEMEYSE LLDKASETDD PYERMVLVAA FAVSGYCSTY FRAGSKPFNP VLGETYECIR EDKGFRFFSE QVSHHPPISA CHCESKNFVF WQDIRWKNKF WGKSMEILPV GTLNVMLPKY GDYYVWNKVT TCIHNILSGR RWIEHYGEVT IRNTKSSVCI CKLTFVKVNY WNSNMNEVQG VVIDQEGKAV YRLFGKWHEG LYCGVAPSAK CIWRPGSMPT NYELYYGFTR FAIELNELDP VLKDLLPPTD ARFRPDQRFL EEGNLEAAAS EKQRVEELQR SRRRYMEENN LEHIPKFFKK VIDANQREAW VSNDTYWELR KDPGFSKVDS PVLW //