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

 OSBL3_MOUSE             Reviewed;         855 AA.
Q9DBS9; E9QNI5;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
28-MAR-2018, entry version 119.
RecName: Full=Oxysterol-binding protein-related protein 3;
Short=ORP-3;
Short=OSBP-related protein 3;
Name=Osbpl3; Synonyms=Orp3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
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).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-272, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Phosphoinositide-binding protein which associates with
both cell and endoplasmic reticulum (ER) membranes. Can bind to
the ER membrane protein VAPA and recruit VAPA to plasma membrane
sites, thus linking these intracellular compartments. The ORP3-
VAPA complex stimulates RRAS signaling which in turn attenuates
integrin beta-1 (ITGB1) activation at the cell surface. With VAPA,
may regulate ER morphology. Has a role in regulation of the actin
cytoskeleton, cell polarity and cell adhesion. Binds to
phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3.
Also binds 25-hydroxycholesterol and cholesterol.
{ECO:0000250|UniProtKB:Q9H4L5}.
-!- SUBUNIT: Homodimer. Interacts with RRAS. Interacts (phosphorylated
form) with VAPA. {ECO:0000250|UniProtKB:Q9H4L5}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q9H4L5}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q9H4L5}. Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q9H4L5}. Cell membrane
{ECO:0000250|UniProtKB:Q9H4L5}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q9H4L5}. Cell projection, filopodium tip
{ECO:0000250|UniProtKB:Q9H4L5}. Nucleus membrane
{ECO:0000250|UniProtKB:Q9H4L5}; Peripheral membrane protein
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in spinal ganglia. Expressed in a
subset of small lymphocytes (at protein level).
{ECO:0000269|PubMed:14593528}.
-!- DEVELOPMENTAL STAGE: Expressed at higher levels in some regions of
the developing central and peripheral nervous system, including
hippocampal neuroepithelium, rhinencephalon, intermediate
thalamus. {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:0000250|UniProtKB:Q9H4L5}.
-!- 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. {ECO:0000250|UniProtKB:Q9H4L5}.
-!- PTM: Phosphorylation is enhanced in vitro by phorbol-12-myristate-
13-acetate (PMA), forskolin and calcium ionophore A23187.
Phosphorylation seems to be stimulated in conditions of low cell-
cell (or cell-matrix) adhesion. {ECO:0000250|UniProtKB:Q9H4L5}.
-!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK004768; BAB23547.1; -; mRNA.
EMBL; AC008160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS39489.1; -.
RefSeq; NP_001157117.1; NM_001163645.1.
RefSeq; NP_082157.2; NM_027881.3.
RefSeq; XP_006506696.1; XM_006506633.3.
UniGene; Mm.44153; -.
ProteinModelPortal; Q9DBS9; -.
SMR; Q9DBS9; -.
BioGrid; 214879; 2.
IntAct; Q9DBS9; 1.
STRING; 10090.ENSMUSP00000110112; -.
iPTMnet; Q9DBS9; -.
PhosphoSitePlus; Q9DBS9; -.
EPD; Q9DBS9; -.
MaxQB; Q9DBS9; -.
PaxDb; Q9DBS9; -.
PRIDE; Q9DBS9; -.
Ensembl; ENSMUST00000114468; ENSMUSP00000110112; ENSMUSG00000029822.
GeneID; 71720; -.
KEGG; mmu:71720; -.
UCSC; uc009bwy.2; mouse.
CTD; 26031; -.
MGI; MGI:1918970; Osbpl3.
eggNOG; KOG1737; Eukaryota.
eggNOG; ENOG410XP9E; LUCA.
GeneTree; ENSGT00760000119155; -.
HOGENOM; HOG000231072; -.
HOVERGEN; HBG058934; -.
InParanoid; Q9DBS9; -.
KO; K20463; -.
TreeFam; TF320922; -.
Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
PRO; PR:Q9DBS9; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000029822; -.
CleanEx; MM_OSBPL3; -.
ExpressionAtlas; Q9DBS9; baseline and differential.
Genevisible; Q9DBS9; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0032433; C:filopodium tip; IEA:UniProtKB-SubCell.
GO; GO:0031965; C:nuclear membrane; ISO:MGI.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0015485; F:cholesterol binding; ISO:MGI.
GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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; 2.
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;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
Nucleus; Phosphoprotein; Reference proteome; Transport.
CHAIN 1 855 Oxysterol-binding protein-related protein
3.
/FTId=PRO_0000100372.
DOMAIN 50 145 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
MOTIF 161 167 FFAT 1. {ECO:0000250|UniProtKB:Q9H4L5}.
MOTIF 450 454 FFAT 2. {ECO:0000250|UniProtKB:Q9H4L5}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4L5}.
MOD_RES 33 33 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4L5}.
MOD_RES 250 250 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4L5}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4L5}.
MOD_RES 288 288 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4L5}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4L5}.
MOD_RES 340 340 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4L5}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4L5}.
MOD_RES 405 405 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4L5}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4L5}.
CONFLICT 789 789 N -> D (in Ref. 1; BAB23547).
{ECO:0000305}.
SEQUENCE 855 AA; 96966 MW; D9551D3265278DF8 CRC64;
MSDEKNLGVS QKLVSPSRST SSCSSKQGSR QDSWEVVEGL RGEMTYTQEP PVQKGFLLKK
RKWPLKGWHK RFFCLEKGIL KYAKSQADIE REKLHGCIDV GLSVMSVKKS SKCIDLDTEE
HIYHLKVKSE ELFDEWVSKL RHHRMYRQNE IAMFPRDVNH FFSGSSVTDS APGVFESVSS
RKRSSLSKQN SFPPGSNLSF SCGGDTRVPF WLQSSEDMEK CSKDMAHCHA YLLEMSQLLE
SMDVLHRTYS APAINAIQVP KPFSGPVRLH SSNPNLSTLD FGEEKSYSDG SEASSEFSKM
QEDLCHVAHK VYFALRSAFN SISVEREKLK QLMELDTSPS PSAQVVGLKH ALSSALAQNT
DLKERLRRIH AESLLLDPPA VPKPGDNLAE ENSRDEGRAL VHQLSNESRL SITDSLSEFF
DAQEVLLSPS SSENEISDDD SYVSDISDNL SLDNLSNDLD NERQTLGPVL ESSGEARSKR
RTSLPAPGPN TSSVSLWSIL RNNIGKDLSK VAMPVELNEP LNTLQRLCEE LEYSELLDKA
SRIPSPLERM VYVAAFAISA YASSYFRAGS KPFNPVLGET YECIRQDKGF QFFAEQVSHH
PPISACHAES GNFVFWQDVR WKNKFWGKSM EIVPIGTTHV TLPAFGDHFE WNKVTSCIHN
ILSGQRWIEH YGEIDIKNLN DDSCHCKVNF IKAKYWSTNA HEIEGTVFDR SGKAVHRLFG
KWHESIYCGG ASSSTCVWRA NPMPKGYEQY YGFTQFALEL NEMDPLSRSL LPPTDTRFRP
DQRLLEEGNI EEAEVQKQRI EKLQRERRRV LEENGVEHQP RFFRKSSDDA WVSNGTYLEL
RKDLGFSKLD HPVLW


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