OSBL8_HUMAN
ID OSBL8_HUMAN Reviewed; 889 AA.
AC Q9BZF1; A8K1T2; E9PE66; E9PE68; Q52LQ3; Q68D75; Q8WXP8; Q9P277;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Oxysterol-binding protein-related protein 8;
DE Short=ORP-8;
DE Short=OSBP-related protein 8;
GN Name=OSBPL8; Synonyms=KIAA1451 {ECO:0000303|PubMed:10819331}, ORP8, OSBP10;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
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].
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-578 (ISOFORM 2).
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 [9]
RP 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 [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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17991739; DOI=10.1074/jbc.m705313200;
RA Yan D., Mayranpaa M.I., Wong J., Perttila J., Lehto M., Jauhiainen M.,
RA Kovanen P.T., Ehnholm C., Brown A.J., Olkkonen V.M.;
RT "OSBP-related protein 8 (ORP8) suppresses ABCA1 expression and cholesterol
RT efflux from macrophages.";
RL J. Biol. Chem. 283:332-340(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-314; SER-807;
RP SER-808; SER-810 AND SER-814, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP 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 [16]
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 [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NUP62.
RX PubMed=21698267; DOI=10.1371/journal.pone.0021078;
RA Zhou T., Li S., Zhong W., Vihervaara T., Beaslas O., Perttila J., Luo W.,
RA Jiang Y., Lehto M., Olkkonen V.M., Yan D.;
RT "OSBP-related protein 8 (ORP8) regulates plasma and liver tissue lipid
RT levels and interacts with the nucleoporin Nup62.";
RL PLoS ONE 6:E21078-E21078(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-328; SER-342; SER-807
RP AND SER-808, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-65 AND SER-314, AND
RP 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 [21]
RP INTERACTION WITH SPAG5.
RX PubMed=24424245; DOI=10.1016/j.yexcr.2014.01.002;
RA Zhong W., Zhou Y., Li J., Mysore R., Luo W., Li S., Chang M.S.,
RA Olkkonen V.M., Yan D.;
RT "OSBP-related protein 8 (ORP8) interacts with Homo sapiens sperm associated
RT antigen 5 (SPAG5) and mediates oxysterol interference of HepG2 cell
RT cycle.";
RL Exp. Cell Res. 322:227-235(2014).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-807 AND SER-808, AND
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 [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [24]
RP FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), AND MUTAGENESIS OF
RP 514-HIS-515.
RX PubMed=26206935; DOI=10.1126/science.aab1370;
RA Chung J., Torta F., Masai K., Lucast L., Czapla H., Tanner L.B.,
RA Narayanaswamy P., Wenk M.R., Nakatsu F., De Camilli P.;
RT "PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-
RT plasma membrane contacts.";
RL Science 349:428-432(2015).
RN [25]
RP STRUCTURE BY NMR OF 147-265.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the pleckstrin homology domain of oxysterol-binding
RT protein-related protein 8 (KIAA1451 protein).";
RL Submitted (JUN-2004) to the PDB data bank.
CC -!- FUNCTION: Lipid transporter involved in lipid countertransport between
CC the endoplasmic reticulum and the plasma membrane: specifically
CC exchanges phosphatidylserine with phosphatidylinositol 4-phosphate
CC (PI4P), delivering phosphatidylserine to the plasma membrane in
CC exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in
CC the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a
CC mutually exclusive manner (PubMed:26206935). Binds oxysterol, 25-
CC hydroxycholesterol and cholesterol (PubMed:17428193, PubMed:17991739,
CC PubMed:21698267). {ECO:0000269|PubMed:17428193,
CC ECO:0000269|PubMed:17991739, ECO:0000269|PubMed:21698267,
CC ECO:0000269|PubMed:26206935}.
CC -!- SUBUNIT: Interacts with SPAG5 (PubMed:24424245). Interacts with NUP62
CC (PubMed:21698267). {ECO:0000269|PubMed:21698267,
CC ECO:0000269|PubMed:24424245}.
CC -!- INTERACTION:
CC Q9BZF1; Q96R06: SPAG5; NbExp=6; IntAct=EBI-2684038, EBI-413317;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17991739, ECO:0000269|PubMed:26206935}; Single-pass
CC membrane protein {ECO:0000269|PubMed:17991739}. Nucleus membrane
CC {ECO:0000269|PubMed:21698267}. Note=The presence of the N-terminus
CC extension contains an overall negative charge that may explain the weak
CC localization to the cortical endoplasmic reticulum (Probable).
CC {ECO:0000305|PubMed:26206935}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:26206935}; Single-pass membrane protein.
CC Note=Localizes to the cortical endoplasmic reticulum at the endoplasmic
CC reticulum-plasma membrane contact sites. {ECO:0000269|PubMed:26206935}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=ORP8L {ECO:0000303|PubMed:26206935};
CC IsoId=Q9BZF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZF1-2; Sequence=VSP_009120;
CC Name=3; Synonyms=ORP8S {ECO:0000303|PubMed:26206935};
CC IsoId=Q9BZF1-3; Sequence=VSP_045801;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:11735225). Expressed at
CC higher level in macrophages (PubMed:17991739).
CC {ECO:0000269|PubMed:11735225, ECO:0000269|PubMed:17991739}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG53411.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA95975.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF392452; AAL40665.1; -; mRNA.
DR EMBL; AB040884; BAA95975.3; ALT_INIT; mRNA.
DR EMBL; AK289997; BAF82686.1; -; mRNA.
DR EMBL; CR749542; CAH18345.1; -; mRNA.
DR EMBL; AC117491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093834; AAH93834.1; -; mRNA.
DR EMBL; BC101529; AAI01530.1; -; mRNA.
DR EMBL; BC111728; AAI11729.1; -; mRNA.
DR EMBL; AF323730; AAG53411.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31862.1; -. [Q9BZF1-1]
DR CCDS; CCDS41814.1; -. [Q9BZF1-3]
DR RefSeq; NP_001003712.1; NM_001003712.1. [Q9BZF1-3]
DR RefSeq; NP_001306581.1; NM_001319652.1. [Q9BZF1-3]
DR RefSeq; NP_001306584.1; NM_001319655.1.
DR RefSeq; NP_065892.1; NM_020841.4. [Q9BZF1-1]
DR RefSeq; XP_005268678.1; XM_005268621.4. [Q9BZF1-1]
DR RefSeq; XP_006719287.1; XM_006719224.2. [Q9BZF1-3]
DR PDB; 1V88; NMR; -; A=149-265.
DR PDB; 5U77; X-ray; 2.16 A; A=149-265.
DR PDB; 5U78; X-ray; 1.98 A; A/B/C/D=149-265.
DR PDBsum; 1V88; -.
DR PDBsum; 5U77; -.
DR PDBsum; 5U78; -.
DR AlphaFoldDB; Q9BZF1; -.
DR BMRB; Q9BZF1; -.
DR SMR; Q9BZF1; -.
DR BioGRID; 125383; 231.
DR DIP; DIP-56130N; -.
DR IntAct; Q9BZF1; 56.
DR MINT; Q9BZF1; -.
DR STRING; 9606.ENSP00000261183; -.
DR SwissLipids; SLP:000001535; -.
DR TCDB; 2.D.1.1.2; the pi4p/ps counter transporter (p/p-ct) family.
DR GlyGen; Q9BZF1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BZF1; -.
DR PhosphoSitePlus; Q9BZF1; -.
DR SwissPalm; Q9BZF1; -.
DR BioMuta; OSBPL8; -.
DR DMDM; 39932732; -.
DR EPD; Q9BZF1; -.
DR jPOST; Q9BZF1; -.
DR MassIVE; Q9BZF1; -.
DR MaxQB; Q9BZF1; -.
DR PaxDb; Q9BZF1; -.
DR PeptideAtlas; Q9BZF1; -.
DR PRIDE; Q9BZF1; -.
DR ProteomicsDB; 19821; -.
DR ProteomicsDB; 79828; -. [Q9BZF1-1]
DR ProteomicsDB; 79829; -. [Q9BZF1-2]
DR Antibodypedia; 680; 97 antibodies from 18 providers.
DR DNASU; 114882; -.
DR Ensembl; ENST00000261183.8; ENSP00000261183.3; ENSG00000091039.17. [Q9BZF1-1]
DR Ensembl; ENST00000393249.6; ENSP00000376939.2; ENSG00000091039.17. [Q9BZF1-3]
DR Ensembl; ENST00000393250.8; ENSP00000376940.4; ENSG00000091039.17. [Q9BZF1-3]
DR Ensembl; ENST00000611266.4; ENSP00000478240.1; ENSG00000091039.17. [Q9BZF1-3]
DR GeneID; 114882; -.
DR KEGG; hsa:114882; -.
DR MANE-Select; ENST00000261183.8; ENSP00000261183.3; NM_020841.5; NP_065892.1.
DR UCSC; uc001sye.2; human. [Q9BZF1-1]
DR CTD; 114882; -.
DR DisGeNET; 114882; -.
DR GeneCards; OSBPL8; -.
DR HGNC; HGNC:16396; OSBPL8.
DR HPA; ENSG00000091039; Low tissue specificity.
DR MIM; 606736; gene.
DR neXtProt; NX_Q9BZF1; -.
DR OpenTargets; ENSG00000091039; -.
DR PharmGKB; PA32832; -.
DR VEuPathDB; HostDB:ENSG00000091039; -.
DR eggNOG; KOG2210; Eukaryota.
DR GeneTree; ENSGT00940000156622; -.
DR InParanoid; Q9BZF1; -.
DR OMA; ESDCEKH; -.
DR OrthoDB; 949920at2759; -.
DR PhylomeDB; Q9BZF1; -.
DR TreeFam; TF312807; -.
DR PathwayCommons; Q9BZF1; -.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR SignaLink; Q9BZF1; -.
DR BioGRID-ORCS; 114882; 17 hits in 1075 CRISPR screens.
DR ChiTaRS; OSBPL8; human.
DR EvolutionaryTrace; Q9BZF1; -.
DR GeneWiki; OSBPL8; -.
DR GenomeRNAi; 114882; -.
DR Pharos; Q9BZF1; Tbio.
DR PRO; PR:Q9BZF1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BZF1; protein.
DR Bgee; ENSG00000091039; Expressed in lower lobe of lung and 212 other tissues.
DR ExpressionAtlas; Q9BZF1; baseline and differential.
DR Genevisible; Q9BZF1; HS.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0140343; F:phosphatidylserine transfer activity; IDA:GO_Central.
DR GO; GO:0005548; F:phospholipid transporter activity; TAS:Reactome.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISS:BHF-UCL.
DR GO; GO:0045444; P:fat cell differentiation; IDA:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:BHF-UCL.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0015914; P:phospholipid transport; IDA:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; ISS:BHF-UCL.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:BHF-UCL.
DR GO; GO:0090204; P:protein localization to nuclear pore; IEA:Ensembl.
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; Alternative splicing; Endoplasmic reticulum;
KW Lipid transport; Lipid-binding; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..889
FT /note="Oxysterol-binding protein-related protein 8"
FT /id="PRO_0000100378"
FT TRANSMEM 871..888
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 148..265
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..791
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 420..425
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 420..425
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 482..485
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 485
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 514..515
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 540
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 706
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 710
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 714
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 MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_045801"
FT VAR_SEQ 15..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11483621"
FT /id="VSP_009120"
FT MUTAGEN 514..515
FT /note="HH->AA: Impaired lipid countertransport between the
FT endoplasmic reticulum and the plasma membrane."
FT /evidence="ECO:0000269|PubMed:26206935"
FT CONFLICT 347
FT /note="M -> V (in Ref. 5; CAH18345)"
FT /evidence="ECO:0000305"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:5U78"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5U77"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:5U78"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:5U78"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:5U78"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:5U78"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:5U78"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:1V88"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:5U78"
FT STRAND 240..249
FT /evidence="ECO:0007829|PDB:5U78"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:5U78"
SQ SEQUENCE 889 AA; 101196 MW; 79DB8055BD15FE95 CRC64;
MEGGLADGEP DRTSLLGDSK DVLGPSTVVA NSDESQLLTP GKMSQRQGKE AYPTPTKDLH
QPSLSPASPH SQGFERGKED ISQNKDESSL SMSKSKSESK LYNGSEKDSS TSSKLTKKES
LKVQKKNYRE EKKRATKELL STITDPSVIV MADWLKIRGT LKSWTKLWCV LKPGVLLIYK
TQKNGQWVGT VLLNACEIIE RPSKKDGFCF KLFHPLEQSI WAVKGPKGEA VGSITQPLPS
SYLIIRATSE SDGRCWMDAL ELALKCSSLL KRTMIREGKE HDLSVSSDST HVTFYGLLRA
NNLHSGDNFQ LNDSEIERQH FKDQDMYSDK SDKENDQEHD ESDNEVMGKS EESDTDTSER
QDDSYIEPEP VEPLKETTYT EQSHEELGEA GEASQTETVS EENKSLIWTL LKQVRPGMDL
SKVVLPTFIL EPRSFLDKLS DYYYHADFLS EAALEENPYF RLKKVVKWYL SGFYKKPKGL
KKPYNPILGE TFRCLWIHPR TNSKTFYIAE QVSHHPPISA FYVSNRKDGF CLSGSILAKS
KFYGNSLSAI LEGEARLTFL NRGEDYVMTM PYAHCKGILY GTMTLELGGT VNITCQKTGY
SAILEFKLKP FLGSSDCVNQ ISGKLKLGKE VLATLEGHWD SEVFITDKKT DNSEVFWNPT
PDIKQWRLIR HTVKFEEQGD FESEKLWQRV TRAINAKDQT EATQEKYVLE EAQRQAARDR
KTKNEEWSCK LFELDPLTGE WHYKFADTRP WDPLNDMIQF EKDGVIQTKV KHRTPMVSVP
KMKHKPTRQQ KKVAKGYSSP EPDIQDSSGS EAQSVKPSTR RKKGIELGDI QSSIESIKQT
QEEIKRNIMA LRNHLVSSTP ATDYFLQQKD YFIIFLLILL QVIINFMFK
