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Oxysterol-binding protein-related protein 8 (ORP-8) (OSBP-related protein 8)

 OSBL8_HUMAN             Reviewed;         889 AA.
Q9BZF1; A8K1T2; E9PE66; E9PE68; Q52LQ3; Q68D75; Q8WXP8; Q9P277;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
15-DEC-2003, sequence version 3.
20-JUN-2018, entry version 157.
RecName: Full=Oxysterol-binding protein-related protein 8;
Short=ORP-8;
Short=OSBP-related protein 8;
Name=OSBPL8;
Synonyms=KIAA1451 {ECO:0000303|PubMed:10819331}, ORP8, OSBP10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=11735225; DOI=10.1006/geno.2001.6663;
Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R.;
"A family of 12 human genes containing oxysterol-binding domains.";
Genomics 78:185-196(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:143-150(2000).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterine endothelium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-578 (ISOFORM 2).
PubMed=11483621;
Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C.,
Staels B., Ikonen E., Olkkonen V.M.;
"The OSBP-related protein family in humans.";
J. Lipid Res. 42:1203-1213(2001).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
FUNCTION.
PubMed=17428193; DOI=10.1042/BJ20070176;
Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M.,
Saarinen H., Radzikowska A., Thiele C., Olkkonen V.M.;
"The mammalian oxysterol-binding protein-related proteins (ORPs) bind
25-hydroxycholesterol in an evolutionarily conserved pocket.";
Biochem. J. 405:473-480(2007).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17991739; DOI=10.1074/jbc.M705313200;
Yan D., Mayranpaa M.I., Wong J., Perttila J., Lehto M., Jauhiainen M.,
Kovanen P.T., Ehnholm C., Brown A.J., Olkkonen V.M.;
"OSBP-related protein 8 (ORP8) suppresses ABCA1 expression and
cholesterol efflux from macrophages.";
J. Biol. Chem. 283:332-340(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-314;
SER-807; SER-808; SER-810 AND SER-814, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NUP62.
PubMed=21698267; DOI=10.1371/journal.pone.0021078;
Zhou T., Li S., Zhong W., Vihervaara T., Beaslas O., Perttila J.,
Luo W., Jiang Y., Lehto M., Olkkonen V.M., Yan D.;
"OSBP-related protein 8 (ORP8) regulates plasma and liver tissue lipid
levels and interacts with the nucleoporin Nup62.";
PLoS ONE 6:E21078-E21078(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-328; SER-342;
SER-807 AND SER-808, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-65 AND SER-314,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
INTERACTION WITH SPAG5.
PubMed=24424245; DOI=10.1016/j.yexcr.2014.01.002;
Zhong W., Zhou Y., Li J., Mysore R., Luo W., Li S., Chang M.S.,
Olkkonen V.M., Yan D.;
"OSBP-related protein 8 (ORP8) interacts with Homo sapiens sperm
associated antigen 5 (SPAG5) and mediates oxysterol interference of
HepG2 cell cycle.";
Exp. Cell Res. 322:227-235(2014).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-807 AND SER-808, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), AND MUTAGENESIS OF
514-HIS-515.
PubMed=26206935; DOI=10.1126/science.aab1370;
Chung J., Torta F., Masai K., Lucast L., Czapla H., Tanner L.B.,
Narayanaswamy P., Wenk M.R., Nakatsu F., De Camilli P.;
"PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated
ER-plasma membrane contacts.";
Science 349:428-432(2015).
[25]
STRUCTURE BY NMR OF 147-265.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the pleckstrin homology domain of oxysterol-
binding protein-related protein 8 (KIAA1451 protein).";
Submitted (JUN-2004) to the PDB data bank.
-!- FUNCTION: Lipid transporter involved in lipid countertransport
between the endoplasmic reticulum and the plasma membrane:
specifically exchanges phosphatidylserine with
phosphatidylinositol 4-phosphate (PI4P), delivering
phosphatidylserine to the plasma membrane in exchange for PI4P,
which is degraded by the SAC1/SACM1L phosphatase in the
endoplasmic reticulum. Binds phosphatidylserine and PI4P in a
mutually exclusive manner (PubMed:26206935). Binds oxysterol, 25-
hydroxycholesterol and cholesterol (PubMed:17428193,
PubMed:17991739, PubMed:21698267). {ECO:0000269|PubMed:17428193,
ECO:0000269|PubMed:17991739, ECO:0000269|PubMed:21698267,
ECO:0000269|PubMed:26206935}.
-!- SUBUNIT: Interacts with SPAG5 (PubMed:24424245). Interacts with
NUP62 (PubMed:21698267). {ECO:0000269|PubMed:21698267,
ECO:0000269|PubMed:24424245}.
-!- SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:17991739, ECO:0000269|PubMed:26206935};
Single-pass membrane protein {ECO:0000269|PubMed:17991739}.
Nucleus membrane {ECO:0000269|PubMed:21698267}. Note=The presence
of the N-terminus extension contains an overall negative charge
that may explain the weak localization to the cortical endoplasmic
reticulum (Probable). {ECO:0000305|PubMed:26206935}.
-!- SUBCELLULAR LOCATION: Isoform 3: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:26206935}; Single-pass membrane protein.
Note=Localizes to the cortical endoplasmic reticulum at the
endoplasmic reticulum-plasma membrane contact sites.
{ECO:0000269|PubMed:26206935}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=ORP8L {ECO:0000303|PubMed:26206935};
IsoId=Q9BZF1-1; Sequence=Displayed;
Name=2;
IsoId=Q9BZF1-2; Sequence=VSP_009120;
Note=No experimental confirmation available.;
Name=3; Synonyms=ORP8S {ECO:0000303|PubMed:26206935};
IsoId=Q9BZF1-3; Sequence=VSP_045801;
-!- TISSUE SPECIFICITY: Widely expressed (PubMed:11735225). Expressed
at higher level in macrophages (PubMed:17991739).
{ECO:0000269|PubMed:11735225, ECO:0000269|PubMed:17991739}.
-!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG53411.1; Type=Frameshift; Positions=30; Evidence={ECO:0000305};
Sequence=BAA95975.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF392452; AAL40665.1; -; mRNA.
EMBL; AB040884; BAA95975.3; ALT_INIT; mRNA.
EMBL; AK289997; BAF82686.1; -; mRNA.
EMBL; CR749542; CAH18345.1; -; mRNA.
EMBL; AC117491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC122687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC093834; AAH93834.1; -; mRNA.
EMBL; BC101529; AAI01530.1; -; mRNA.
EMBL; BC111728; AAI11729.1; -; mRNA.
EMBL; AF323730; AAG53411.1; ALT_FRAME; mRNA.
CCDS; CCDS31862.1; -. [Q9BZF1-1]
CCDS; CCDS41814.1; -. [Q9BZF1-3]
RefSeq; NP_001003712.1; NM_001003712.1. [Q9BZF1-3]
RefSeq; NP_001306581.1; NM_001319652.1. [Q9BZF1-3]
RefSeq; NP_001306584.1; NM_001319655.1.
RefSeq; NP_065892.1; NM_020841.4. [Q9BZF1-1]
RefSeq; XP_005268678.1; XM_005268621.4. [Q9BZF1-1]
RefSeq; XP_006719287.1; XM_006719224.2. [Q9BZF1-3]
UniGene; Hs.430849; -.
PDB; 1V88; NMR; -; A=149-265.
PDB; 5U77; X-ray; 2.16 A; A=149-265.
PDB; 5U78; X-ray; 1.98 A; A/B/C/D=149-265.
PDBsum; 1V88; -.
PDBsum; 5U77; -.
PDBsum; 5U78; -.
ProteinModelPortal; Q9BZF1; -.
SMR; Q9BZF1; -.
BioGrid; 125383; 43.
DIP; DIP-56130N; -.
IntAct; Q9BZF1; 17.
STRING; 9606.ENSP00000261183; -.
SwissLipids; SLP:000001535; -.
TCDB; 2.D.1.1.2; the pi4p/ps counter transporter (p/p-ct) family.
iPTMnet; Q9BZF1; -.
PhosphoSitePlus; Q9BZF1; -.
SwissPalm; Q9BZF1; -.
BioMuta; OSBPL8; -.
DMDM; 39932732; -.
EPD; Q9BZF1; -.
MaxQB; Q9BZF1; -.
PaxDb; Q9BZF1; -.
PeptideAtlas; Q9BZF1; -.
PRIDE; Q9BZF1; -.
ProteomicsDB; 79828; -.
ProteomicsDB; 79829; -. [Q9BZF1-2]
Ensembl; ENST00000261183; ENSP00000261183; ENSG00000091039. [Q9BZF1-1]
Ensembl; ENST00000393249; ENSP00000376939; ENSG00000091039. [Q9BZF1-3]
Ensembl; ENST00000393250; ENSP00000376940; ENSG00000091039. [Q9BZF1-3]
Ensembl; ENST00000611266; ENSP00000478240; ENSG00000091039. [Q9BZF1-3]
GeneID; 114882; -.
KEGG; hsa:114882; -.
UCSC; uc001sye.2; human. [Q9BZF1-1]
CTD; 114882; -.
DisGeNET; 114882; -.
EuPathDB; HostDB:ENSG00000091039.16; -.
GeneCards; OSBPL8; -.
HGNC; HGNC:16396; OSBPL8.
HPA; HPA001309; -.
MIM; 606736; gene.
neXtProt; NX_Q9BZF1; -.
OpenTargets; ENSG00000091039; -.
PharmGKB; PA32832; -.
eggNOG; KOG2210; Eukaryota.
eggNOG; ENOG410XRW6; LUCA.
GeneTree; ENSGT00550000074515; -.
HOGENOM; HOG000233870; -.
HOVERGEN; HBG053375; -.
InParanoid; Q9BZF1; -.
KO; K22285; -.
OMA; SYYHADI; -.
OrthoDB; EOG091G0A3R; -.
PhylomeDB; Q9BZF1; -.
TreeFam; TF312807; -.
Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
ChiTaRS; OSBPL8; human.
EvolutionaryTrace; Q9BZF1; -.
GeneWiki; OSBPL8; -.
GenomeRNAi; 114882; -.
PMAP-CutDB; Q9BZF1; -.
PRO; PR:Q9BZF1; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000091039; -.
CleanEx; HS_OSBPL8; -.
ExpressionAtlas; Q9BZF1; baseline and differential.
Genevisible; Q9BZF1; HS.
GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
GO; GO:0005548; F:phospholipid transporter activity; IDA:UniProtKB.
GO; GO:0032148; P:activation of protein kinase B activity; ISS:BHF-UCL.
GO; GO:0045444; P:fat cell differentiation; IDA:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:BHF-UCL.
GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
GO; GO:0015914; P:phospholipid transport; IDA:UniProtKB.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; ISS:BHF-UCL.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:BHF-UCL.
GO; GO:0090204; P:protein localization to nuclear pore; IEA:Ensembl.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR037239; OSBP_sf.
InterPro; IPR000648; Oxysterol-bd.
InterPro; IPR018494; Oxysterol-bd_CS.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR10972; PTHR10972; 1.
Pfam; PF01237; Oxysterol_BP; 1.
Pfam; PF00169; PH; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF144000; SSF144000; 1.
PROSITE; PS01013; OSBP; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 889 Oxysterol-binding protein-related protein
8.
/FTId=PRO_0000100378.
TRANSMEM 871 888 Helical. {ECO:0000255}.
DOMAIN 148 265 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
REGION 420 425 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 420 425 Phosphatidylserine binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 482 485 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 514 515 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 485 485 Phosphatidylserine.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 540 540 Phosphatidylserine.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 706 706 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 710 710 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 714 714 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 342 342 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 807 807 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 808 808 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 810 810 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 814 814 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 1 42 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_045801.
VAR_SEQ 15 29 Missing (in isoform 2).
{ECO:0000303|PubMed:11483621}.
/FTId=VSP_009120.
MUTAGEN 514 515 HH->AA: Impaired lipid countertransport
between the endoplasmic reticulum and the
plasma membrane.
{ECO:0000269|PubMed:26206935}.
CONFLICT 347 347 M -> V (in Ref. 5; CAH18345).
{ECO:0000305}.
STRAND 151 158 {ECO:0000244|PDB:5U78}.
STRAND 160 162 {ECO:0000244|PDB:5U77}.
STRAND 165 172 {ECO:0000244|PDB:5U78}.
STRAND 175 184 {ECO:0000244|PDB:5U78}.
STRAND 187 192 {ECO:0000244|PDB:5U78}.
HELIX 193 195 {ECO:0000244|PDB:5U78}.
STRAND 197 200 {ECO:0000244|PDB:5U78}.
TURN 203 205 {ECO:0000244|PDB:1V88}.
STRAND 208 213 {ECO:0000244|PDB:5U78}.
STRAND 240 249 {ECO:0000244|PDB:5U78}.
HELIX 250 264 {ECO:0000244|PDB:5U78}.
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


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