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Oxysterol-binding protein-related protein 3 (ORP-3) (OSBP-related protein 3)

 OSBL3_HUMAN             Reviewed;         887 AA.
Q9H4L5; A4D167; A4D168; A4D169; A4D170; A4D171; A4D172; B8ZZ79;
B8ZZP0; O14591; O43357; O43358; Q8N702; Q8N703; Q8N704; Q8NFH0;
Q8NFH1; Q8NI12; Q8NI13; Q9BZF4; Q9UED6;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 144.
RecName: Full=Oxysterol-binding protein-related protein 3;
Short=ORP-3;
Short=OSBP-related protein 3;
Name=OSBPL3; Synonyms=KIAA0704, ORP3, OSBP3;
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 1A).
PubMed=11568019; DOI=10.1182/blood.V98.7.2279;
Gregorio-King C.C., Collier G.R., McMillan J.S., Waugh C.M.,
McLeod J.L., Collier F.M., Kirkland M.A.;
"ORP-3, a human oxysterol-binding protein gene differentially
expressed in hematopoietic cells.";
Blood 98:2279-2281(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 1C; 1D; 2A; 2B; 2C AND
2D), AND TISSUE SPECIFICITY.
PubMed=12590732; DOI=10.1089/104454903321112442;
Collier F.M., Gregorio-King C.C., Apostolopoulos J., Walder K.,
Kirkland M.A.;
"ORP3 splice variants and their expression in human tissues and
hematopoietic cells.";
DNA Cell Biol. 22:1-9(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[5]
SEQUENCE REVISION.
Ohara O., Suyama M., Nagase T., Ishikawa K.;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
TISSUE=Uterus;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-245 (ISOFORM 1A).
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).
[11]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=14593528; DOI=10.1007/s00441-003-0817-y;
Lehto M., Tienari J., Lehtonen S., Lehtonen E., Olkkonen V.M.;
"Subfamily III of mammalian oxysterol-binding protein (OSBP)
homologues: the expression and intracellular localization of ORP3,
ORP6, and ORP7.";
Cell Tissue Res. 315:39-57(2004).
[12]
FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH
DOMAIN, FFAT MOTIF, AND MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72;
GLY-97 AND 451-PHE--ASP-453.
PubMed=16143324; DOI=10.1016/j.yexcr.2005.08.003;
Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K.,
Olkkonen V.M.;
"Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum
and plasma membrane is controlled by multiple determinants.";
Exp. Cell Res. 310:445-462(2005).
[13]
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).
[14]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRAS, DOMAIN PH, AND
AND PHOSPHORYLATION.
PubMed=18270267; DOI=10.1242/jcs.016964;
Lehto M., Maeyraenpaeae M.I., Pellinen T., Ihalmo P., Lehtonen S.,
Kovanen P.T., Groop P.H., Ivaska J., Olkkonen V.M.;
"The R-Ras interaction partner ORP3 regulates cell adhesion.";
J. Cell Sci. 121:695-705(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND SER-437, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-251; SER-304;
SER-372 AND SER-410, 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).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-410 AND SER-437,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-372 AND
SER-410, 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).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-200; SER-251;
SER-265; SER-304; SER-309; SER-320; SER-372; SER-410; SER-425; SER-437
AND SER-440, 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).
[24]
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).
[25]
FUNCTION, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, DOMAIN FFAT
MOTIF, PHOSPHORYLATION AT SER-251; SER-265; SER-304; SER-320; SER-323;
SER-371; SER-372; SER-410 AND SER-437, IDENTIFICATION BY MASS
SPECTROMETRY, AND MUTAGENESIS OF 162-PHE--THR-167 AND
451-PHE--ASP-453.
PubMed=25447204; DOI=10.1016/j.yexcr.2014.10.019;
Weber-Boyvat M., Kentala H., Lilja J., Vihervaara T., Hanninen R.,
Zhou Y., Peranen J., Nyman T.A., Ivaska J., Olkkonen V.M.;
"OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A
regulates R-Ras activity.";
Exp. Cell Res. 331:278-291(2015).
-!- FUNCTION: Phosphoinositide-binding protein which associates with
both cell and endoplasmic reticulum (ER) membranes
(PubMed:16143324). Can bind to the ER membrane protein VAPA and
recruit VAPA to plasma membrane sites, thus linking these
intracellular compartments (PubMed:25447204). The ORP3-VAPA
complex stimulates RRAS signaling which in turn attenuates
integrin beta-1 (ITGB1) activation at the cell surface
(PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER
morphology (PubMed:16143324). Has a role in regulation of the
actin cytoskeleton, cell polarity and cell adhesion
(PubMed:18270267). Binds to phosphoinositides with preference for
PI(3,4)P2 and PI(3,4,5)P3 (PubMed:16143324). Also binds 25-
hydroxycholesterol and cholesterol (PubMed:17428193).
{ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:17428193,
ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:25447204}.
-!- SUBUNIT: Homodimer (PubMed:16143324). Interacts with RRAS
(PubMed:18270267). Interacts (phosphorylated form) with VAPA
(PubMed:16143324, PubMed:25447204). {ECO:0000269|PubMed:16143324,
ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:25447204}.
-!- INTERACTION:
Q8TBB1:LNX1; NbExp=4; IntAct=EBI-1051317, EBI-739832;
Q9Q2G4:ORF (xeno); NbExp=5; IntAct=EBI-1051317, EBI-6248094;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:16143324}; Peripheral membrane protein
{ECO:0000269|PubMed:16143324}. Cytoplasm, cytosol
{ECO:0000269|PubMed:16143324}. Cell membrane
{ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:16143324,
ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:25447204};
Peripheral membrane protein {ECO:0000269|PubMed:14593528,
ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:18270267,
ECO:0000269|PubMed:25447204}. Cell projection, filopodium tip
{ECO:0000269|PubMed:18270267}. Nucleus membrane
{ECO:0000269|PubMed:16143324}; Peripheral membrane protein
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1a;
IsoId=Q9H4L5-1; Sequence=Displayed;
Name=1b;
IsoId=Q9H4L5-2; Sequence=VSP_008219;
Name=1c;
IsoId=Q9H4L5-3; Sequence=VSP_008220;
Name=1d;
IsoId=Q9H4L5-4; Sequence=VSP_008219, VSP_008220;
Name=2a;
IsoId=Q9H4L5-5; Sequence=VSP_008221, VSP_008222;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=2b;
IsoId=Q9H4L5-6; Sequence=VSP_008219, VSP_008221, VSP_008222;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=2c;
IsoId=Q9H4L5-7; Sequence=VSP_008220, VSP_008221, VSP_008222;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=2d;
IsoId=Q9H4L5-8; Sequence=VSP_008219, VSP_008220, VSP_008221,
VSP_008222;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Expressed in a subset of small lymphocytes (at
protein level). Expressed at high concentration in kidney, lymph
node and thymus. Expressed at moderate concentration in stomach,
jejunum, ileum, appendix, spleen, leukocytes, trachea, lung and
thyroid gland. Expressed at low concentration in whole brain,
esophagus, duodenum, ileocecum, colon, skeletal muscle, bone
marrow, placenta and mammary gland (PubMed:14593528). Isoform 1a,
isoform 1b, isoform 1c and isoform 1d are highly expressed in
brain, bone marrow, colon, kidney, lung, skeletal muscle, spleen,
thymus and thyroid. Not expressed in heart and liver. Isoform 2a,
isoform 2b, isoform 2c and isoform 2d are expressed in brain, bone
marrow, kidney, skeletal muscle, spleen, thymus and thyroid. Not
expressed in heart, liver and lung (PubMed:12590732).
{ECO:0000269|PubMed:12590732, ECO:0000269|PubMed:14593528}.
-!- DEVELOPMENTAL STAGE: Expressed in several fetal tissues including
kidney, thymus, spleen and lung. {ECO:0000269|PubMed:14593528}.
-!- DOMAIN: The FFAT 2 motif is required for interaction with VAPA and
regulation of the endoplasmic reticulum targeting of ORP3. The
FFAT 1 motif may contribute to VAPA binding.
{ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:25447204}.
-!- DOMAIN: The PH domain binds phosphoinositides, with a preference
for PI(3,4)P2 and PI(3,4,5)P3. The PH domain mediates targeting to
the plasma membrane (PubMed:18270267).
{ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:18270267}.
-!- PTM: Phosphorylation is enhanced in vitro by phorbol-12-myristate-
13-acetate (PMA), forskolin and calcium ionophore A23187
(PubMed:25447204). Phosphorylation seems to be stimulated in
conditions of low cell-cell (or cell-matrix) adhesion
(PubMed:18270267). {ECO:0000269|PubMed:18270267,
ECO:0000269|PubMed:25447204}.
-!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA31679.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AY008372; AAG23400.1; -; mRNA.
EMBL; AF392444; AAL40657.1; -; mRNA.
EMBL; AF491781; AAM27386.1; -; mRNA.
EMBL; AF491782; AAM27387.1; -; mRNA.
EMBL; AF491783; AAM27388.1; -; mRNA.
EMBL; AF491784; AAM27389.1; -; mRNA.
EMBL; AF491785; AAM27390.1; -; mRNA.
EMBL; AF491786; AAM27391.1; -; mRNA.
EMBL; AF515639; AAM74165.1; -; mRNA.
EMBL; AF515640; AAM74166.1; -; mRNA.
EMBL; AB014604; BAA31679.2; ALT_INIT; mRNA.
EMBL; AC003093; AAB83939.1; -; Genomic_DNA.
EMBL; AC004008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004016; AAC26986.2; -; Genomic_DNA.
EMBL; AC004239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236948; EAL24240.1; -; Genomic_DNA.
EMBL; CH236948; EAL24241.1; -; Genomic_DNA.
EMBL; CH236948; EAL24242.1; -; Genomic_DNA.
EMBL; CH236948; EAL24243.1; -; Genomic_DNA.
EMBL; CH236948; EAL24244.1; -; Genomic_DNA.
EMBL; CH236948; EAL24245.1; -; Genomic_DNA.
EMBL; CH471073; EAW93816.1; -; Genomic_DNA.
EMBL; CH471073; EAW93817.1; -; Genomic_DNA.
EMBL; CH471073; EAW93818.1; -; Genomic_DNA.
EMBL; CH471073; EAW93819.1; -; Genomic_DNA.
EMBL; CH471073; EAW93820.1; -; Genomic_DNA.
EMBL; CH471073; EAW93821.1; -; Genomic_DNA.
EMBL; BC017731; AAH17731.1; -; mRNA.
EMBL; AF323727; AAG53408.1; -; mRNA.
CCDS; CCDS47564.1; -. [Q9H4L5-4]
CCDS; CCDS5390.1; -. [Q9H4L5-1]
CCDS; CCDS5391.1; -. [Q9H4L5-2]
CCDS; CCDS5392.1; -. [Q9H4L5-3]
RefSeq; NP_056365.1; NM_015550.3. [Q9H4L5-1]
RefSeq; NP_663160.1; NM_145320.2. [Q9H4L5-2]
RefSeq; NP_663161.1; NM_145321.2. [Q9H4L5-3]
RefSeq; NP_663162.1; NM_145322.2. [Q9H4L5-4]
RefSeq; XP_005249755.1; XM_005249698.3. [Q9H4L5-1]
RefSeq; XP_006715744.1; XM_006715681.3. [Q9H4L5-2]
RefSeq; XP_006715745.1; XM_006715682.3. [Q9H4L5-3]
RefSeq; XP_006715746.1; XM_006715683.3. [Q9H4L5-4]
RefSeq; XP_011513560.1; XM_011515258.2. [Q9H4L5-1]
UniGene; Hs.520259; -.
ProteinModelPortal; Q9H4L5; -.
SMR; Q9H4L5; -.
BioGrid; 117497; 40.
ELM; Q9H4L5; -.
IntAct; Q9H4L5; 36.
MINT; Q9H4L5; -.
STRING; 9606.ENSP00000315410; -.
iPTMnet; Q9H4L5; -.
PhosphoSitePlus; Q9H4L5; -.
BioMuta; OSBPL3; -.
DMDM; 20139176; -.
EPD; Q9H4L5; -.
MaxQB; Q9H4L5; -.
PaxDb; Q9H4L5; -.
PeptideAtlas; Q9H4L5; -.
PRIDE; Q9H4L5; -.
Ensembl; ENST00000313367; ENSP00000315410; ENSG00000070882. [Q9H4L5-1]
Ensembl; ENST00000396429; ENSP00000379706; ENSG00000070882. [Q9H4L5-3]
Ensembl; ENST00000396431; ENSP00000379708; ENSG00000070882. [Q9H4L5-2]
Ensembl; ENST00000409069; ENSP00000386953; ENSG00000070882. [Q9H4L5-4]
Ensembl; ENST00000409452; ENSP00000386801; ENSG00000070882. [Q9H4L5-5]
Ensembl; ENST00000409555; ENSP00000386990; ENSG00000070882. [Q9H4L5-8]
Ensembl; ENST00000409759; ENSP00000386325; ENSG00000070882. [Q9H4L5-7]
Ensembl; ENST00000409863; ENSP00000386429; ENSG00000070882. [Q9H4L5-6]
GeneID; 26031; -.
KEGG; hsa:26031; -.
UCSC; uc003sxf.5; human. [Q9H4L5-1]
CTD; 26031; -.
DisGeNET; 26031; -.
EuPathDB; HostDB:ENSG00000070882.12; -.
GeneCards; OSBPL3; -.
HGNC; HGNC:16370; OSBPL3.
HPA; HPA000691; -.
HPA; HPA048401; -.
MIM; 606732; gene.
neXtProt; NX_Q9H4L5; -.
OpenTargets; ENSG00000070882; -.
PharmGKB; PA32828; -.
eggNOG; KOG1737; Eukaryota.
eggNOG; ENOG410XP9E; LUCA.
GeneTree; ENSGT00760000119155; -.
HOVERGEN; HBG058934; -.
InParanoid; Q9H4L5; -.
KO; K20463; -.
OMA; TCVWRAN; -.
OrthoDB; EOG091G0DJB; -.
PhylomeDB; Q9H4L5; -.
TreeFam; TF320922; -.
Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
ChiTaRS; OSBPL3; human.
GeneWiki; OSBPL3; -.
GenomeRNAi; 26031; -.
PRO; PR:Q9H4L5; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000070882; -.
ExpressionAtlas; Q9H4L5; baseline and differential.
Genevisible; Q9H4L5; HS.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0032433; C:filopodium tip; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:BHF-UCL.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
GO; GO:0015248; F:sterol transporter activity; TAS:Reactome.
GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
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.
SMART; SM00233; PH; 1.
SUPFAM; SSF144000; SSF144000; 1.
PROSITE; PS01013; OSBP; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Lipid transport;
Lipid-binding; Membrane; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transport.
CHAIN 1 887 Oxysterol-binding protein-related protein
3.
/FTId=PRO_0000100371.
DOMAIN 51 146 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
MOTIF 161 167 FFAT 1. {ECO:0000269|PubMed:25447204}.
MOTIF 450 454 FFAT 2. {ECO:0000269|PubMed:25447204}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 251 251 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:25447204}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:25447204}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:25447204}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000269|PubMed:25447204}.
MOD_RES 371 371 Phosphoserine.
{ECO:0000269|PubMed:25447204}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:25447204}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:25447204}.
MOD_RES 425 425 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:25447204}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 259 289 Missing (in isoform 1b, isoform 1d,
isoform 2b and isoform 2d).
{ECO:0000303|PubMed:12590732}.
/FTId=VSP_008219.
VAR_SEQ 387 422 Missing (in isoform 1c, isoform 1d,
isoform 2c and isoform 2d).
{ECO:0000303|PubMed:12590732}.
/FTId=VSP_008220.
VAR_SEQ 584 631 YVAAFAISAYASSYYRAGSKPFNPVLGETYECIREDKGFQF
FSEQVSH -> RSQPSLATVQPRSPSHEAIHGAHQRDSPCS
LRFHFDCSVNRFITQSCLASSAWLFPVTL (in isoform
2a, isoform 2b, isoform 2c and isoform
2d). {ECO:0000303|PubMed:12590732}.
/FTId=VSP_008221.
VAR_SEQ 632 887 Missing (in isoform 2a, isoform 2b,
isoform 2c and isoform 2d).
{ECO:0000303|PubMed:12590732}.
/FTId=VSP_008222.
VARIANT 354 354 M -> V (in dbSNP:rs11768296).
/FTId=VAR_053548.
MUTAGEN 60 60 K->I: Abolishes plasma membrane targeting
and nuclear localization.
{ECO:0000269|PubMed:16143324}.
MUTAGEN 61 61 K->A: Abolishes plasma membrane targeting
and nuclear localization.
{ECO:0000269|PubMed:16143324}.
MUTAGEN 71 71 K->A: Abolishes plasma membrane targeting
and nuclear localization.
{ECO:0000269|PubMed:16143324}.
MUTAGEN 72 72 R->I: Abolishes plasma membrane targeting
and nuclear localization.
{ECO:0000269|PubMed:16143324}.
MUTAGEN 97 97 G->E: Decreases plasma membrane targeting
and nuclear localization.
{ECO:0000269|PubMed:16143324}.
MUTAGEN 162 167 FFSGST->AAAAAA: No effect on interaction
with VAPA. {ECO:0000269|PubMed:25447204}.
MUTAGEN 451 453 FFD->VVV: Reduces VAPA binding. Abolishes
association with endoplasmic reticulum.
{ECO:0000269|PubMed:16143324,
ECO:0000269|PubMed:25447204}.
SEQUENCE 887 AA; 101224 MW; 12E16912BD3F2E99 CRC64;
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE PPVQKGFLLK
KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID VGLSVMSVKK SSKCIDLDTE
EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN EIAMFPHEVN HFFSGSTITD SSSGVFDSIS
SRKRSSISKQ NLFQTGSNVS FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL
QSMDVLHRTY SAPAINAIQG GSFESPKKEK RSHRRWRSRA IGKDAKGTLQ VPKPFSGPVR
LHSSNPNLST LDFGEEKNYS DGSETSSEFS KMQEDLCHIA HKVYFTLRSA FNIMSAEREK
LKQLMEQDAS SSPSAQVIGL KNALSSALAQ NTDLKERLRR IHAESLLLDS PAVAKSGDNL
AEENSRDENR ALVHQLSNES RLSITDSLSE FFDAQEVLLS PSSSENEISD DDSYVSDISD
NLSLDNLSND LDNERQTLGP VLDSGREAKS RRRTCLPAPC PSSSNISLWN ILRNNIGKDL
SKVAMPVELN EPLNTLQRLC EELEYSELLD KAAQIPSPLE RMVYVAAFAI SAYASSYYRA
GSKPFNPVLG ETYECIREDK GFQFFSEQVS HHPPISACHA ESRNFVFWQD VRWKNKFWGK
SMEIVPIGTT HVTLPVFGDH FEWNKVTSCI HNILSGQRWI EHYGEIVIKN LHDDSCYCKV
NFIKAKYWST NAHEIEGTVF DRSGKAVHRL FGKWHESIYC GGGSSSACVW RANPMPKGYE
QYYSFTQFAL ELNEMDPSSK SLLPPTDTRF RPDQRFLEEG NLEEAEIQKQ RIEQLQRERR
RVLEENHVEH QPRFFRKSDD DSWVSNGTYL ELRKDLGFSK LDHPVLW


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