OSBL6_HUMAN
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 03-AUG-2022, entry version 171.
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 Q9BZF3-6; O14901: KLF11; NbExp=3; IntAct=EBI-10698423, EBI-948266;
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};
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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 AlphaFoldDB; Q9BZF3; -.
DR SMR; Q9BZF3; -.
DR BioGRID; 125381; 79.
DR ELM; Q9BZF3; -.
DR IntAct; Q9BZF3; 30.
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; 134 antibodies from 23 providers.
DR DNASU; 114880; -.
DR Ensembl; ENST00000190611.9; ENSP00000190611.4; ENSG00000079156.17. [Q9BZF3-1]
DR Ensembl; ENST00000315022.2; ENSP00000318723.2; ENSG00000079156.17. [Q9BZF3-3]
DR Ensembl; ENST00000357080.8; ENSP00000349591.4; ENSG00000079156.17. [Q9BZF3-6]
DR Ensembl; ENST00000359685.7; ENSP00000352713.3; ENSG00000079156.17. [Q9BZF3-2]
DR Ensembl; ENST00000392505.6; ENSP00000376293.2; ENSG00000079156.17. [Q9BZF3-5]
DR Ensembl; ENST00000409045.7; ENSP00000387248.3; ENSG00000079156.17. [Q9BZF3-4]
DR Ensembl; ENST00000409631.5; ENSP00000386885.1; ENSG00000079156.17. [Q9BZF3-2]
DR GeneID; 114880; -.
DR KEGG; hsa:114880; -.
DR MANE-Select; ENST00000190611.9; ENSP00000190611.4; NM_032523.4; NP_115912.1.
DR UCSC; uc002ulw.4; human. [Q9BZF3-1]
DR CTD; 114880; -.
DR DisGeNET; 114880; -.
DR GeneCards; OSBPL6; -.
DR HGNC; HGNC:16388; OSBPL6.
DR HPA; ENSG00000079156; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 606734; gene.
DR neXtProt; NX_Q9BZF3; -.
DR OpenTargets; ENSG00000079156; -.
DR PharmGKB; PA32830; -.
DR VEuPathDB; HostDB:ENSG00000079156; -.
DR eggNOG; KOG1737; Eukaryota.
DR GeneTree; ENSGT00940000156791; -.
DR HOGENOM; CLU_007105_4_1_1; -.
DR InParanoid; Q9BZF3; -.
DR OMA; EGLSLWN; -.
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 SignaLink; Q9BZF3; -.
DR BioGRID-ORCS; 114880; 14 hits in 1086 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 178 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: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; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|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 REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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
