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

 OSBL8_MOUSE             Reviewed;         889 AA.
B9EJ86; G3X9N6; Q69ZJ4;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 1.
28-MAR-2018, entry version 79.
RecName: Full=Oxysterol-binding protein-related protein 8;
Short=ORP-8;
Short=OSBP-related protein 8;
Name=Osbpl8 {ECO:0000312|MGI:MGI:2443807};
Synonyms=Kiaa1451 {ECO:0000303|PubMed:15368895}, Orp8;
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 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 461-889.
TISSUE=Thymus;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
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).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-807; SER-808;
SER-810 AND SER-814, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[9]
DISRUPTION PHENOTYPE.
PubMed=23554939; DOI=10.1371/journal.pone.0058856;
Beaslas O., Metso J., Nissila E., Laurila P.P., Kaiharju E.,
Batchu K.C., Kaipiainen L., Mayranpaa M.I., Yan D., Gylling H.,
Jauhiainen M., Olkkonen V.M.;
"Osbpl8 deficiency in mouse causes an elevation of high-density
lipoproteins and gender-specific alterations of lipid metabolism.";
PLoS ONE 8:E58856-E58856(2013).
[10]
DISRUPTION PHENOTYPE.
PubMed=25347070; DOI=10.1371/journal.pone.0109024;
van Kampen E., Beaslas O., Hildebrand R.B., Lammers B.,
Van Berkel T.J., Olkkonen V.M., Van Eck M.;
"Orp8 deficiency in bone marrow-derived cells reduces atherosclerotic
lesion progression in LDL receptor knockout mice.";
PLoS ONE 9:E109024-E109024(2014).
-!- 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. Binds oxysterol, 25-hydroxycholesterol
and cholesterol. {ECO:0000250|UniProtKB:Q9BZF1}.
-!- SUBUNIT: Interacts with SPAG5. Interacts with NUP62.
{ECO:0000250|UniProtKB:Q9BZF1}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q9BZF1}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q9BZF1}. Nucleus membrane
{ECO:0000250|UniProtKB:Q9BZF1}. Note=The presence of the N-
terminus extension contains an overall negative charge that may
explain the weak localization to the cortical endoplasmic
reticulum. {ECO:0000250|UniProtKB:Q9BZF1}.
-!- TISSUE SPECIFICITY: Widely expressed. Most abundant in liver,
spleen, kidney, brain and adipose tissue.
{ECO:0000269|PubMed:17991739}.
-!- DISRUPTION PHENOTYPE: Mice are apparently healthy and show no
developmental defects nor gross abnormality of glucose or lipid
metabolism. However, they display a significant elevation of
plasma HDL cholesterol and phospholipid levels. They also show a
modest increase of APOA1, plus a number of mild gender- or diet-
specific lipid metabolism phenotypes (PubMed:23554939). Deletion
in bone marrow-derived cells, including macrophages, reduces
atherosclerotic lesion progression (PubMed:25347070).
{ECO:0000269|PubMed:23554939, ECO:0000269|PubMed:25347070}.
-!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EDL21722.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC121871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466539; EDL21721.1; -; Genomic_DNA.
EMBL; CH466539; EDL21722.1; ALT_SEQ; Genomic_DNA.
EMBL; BC141383; AAI41384.1; -; mRNA.
EMBL; AK173174; BAD32452.1; -; mRNA.
CCDS; CCDS36056.1; -.
RefSeq; NP_001003717.1; NM_001003717.1.
RefSeq; NP_780698.2; NM_175489.3.
RefSeq; XP_006513702.1; XM_006513639.2.
UniGene; Mm.220204; -.
ProteinModelPortal; B9EJ86; -.
SMR; B9EJ86; -.
STRING; 10090.ENSMUSP00000100911; -.
iPTMnet; B9EJ86; -.
PhosphoSitePlus; B9EJ86; -.
MaxQB; B9EJ86; -.
PaxDb; B9EJ86; -.
PeptideAtlas; B9EJ86; -.
PRIDE; B9EJ86; -.
Ensembl; ENSMUST00000105275; ENSMUSP00000100911; ENSMUSG00000020189.
GeneID; 237542; -.
KEGG; mmu:237542; -.
UCSC; uc007gzy.1; mouse.
UCSC; uc007gzz.1; mouse.
CTD; 114882; -.
MGI; MGI:2443807; Osbpl8.
eggNOG; KOG2210; Eukaryota.
eggNOG; ENOG410XRW6; LUCA.
GeneTree; ENSGT00550000074515; -.
HOGENOM; HOG000233870; -.
HOVERGEN; HBG053375; -.
KO; K22285; -.
OMA; SYYHADI; -.
OrthoDB; EOG091G0A3R; -.
PhylomeDB; B9EJ86; -.
TreeFam; TF312807; -.
Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
ChiTaRS; Osbpl8; mouse.
PRO; PR:B9EJ86; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000020189; -.
ExpressionAtlas; B9EJ86; baseline and differential.
Genevisible; B9EJ86; MM.
GO; GO:0032541; C:cortical endoplasmic reticulum; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031965; C:nuclear membrane; IMP:MGI.
GO; GO:0015485; F:cholesterol binding; ISO:MGI.
GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
GO; GO:0005548; F:phospholipid transporter activity; ISS:UniProtKB.
GO; GO:0032148; P:activation of protein kinase B activity; IMP:BHF-UCL.
GO; GO:0045444; P:fat cell differentiation; ISO:MGI.
GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI.
GO; GO:0010891; P:negative regulation of sequestering of triglyceride; ISO:MGI.
GO; GO:0015914; P:phospholipid transport; ISS:UniProtKB.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IMP:BHF-UCL.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:BHF-UCL.
GO; GO:0090204; P:protein localization to nuclear pore; IMP:MGI.
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;
Acetylation; 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_0000434121.
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:0000250|UniProtKB:Q9BZF1}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BZF1}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BZF1}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BZF1}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BZF1}.
MOD_RES 342 342 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BZF1}.
MOD_RES 807 807 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 808 808 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 810 810 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 814 814 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
SEQUENCE 889 AA; 101269 MW; 01565BEBAD48553C CRC64;
MEAALADGEP DRSSLLGDSK DVLGPSTVVA NSDEPQHLTP GKMSQRQGRD ANPTPTRDLP
QPSLSPASLH SQGFERGKED ISQNKDDSSL SMSKSKSESK LYNGSEKDSS TSSKLTKKES
LKVQKKNYRE EKKRATKELL STITDPSVIV MADWLKIRGT LKSWTKLWCV LKPGVLLIYK
TQKNGQWVGT VLLNACEIIE RPSKKDGFCF KLFHPLEQSI WAVKGPKGEA VGSITQPLPS
SYLIIRATSE SDGRCWMDAL ELALKCSSLL KRTMVREGKE HDLSISSDST HVTLYGLLRA
NNLHSGDNFQ LNDSEIERQH FKDQDLYSDK SDKENDPEHD ESDNEVLGKS EESDTDTSER
QDDSYIDPEP VEPLKETTYM EQSHEELGEA GEASQTETVS EENKSLIWTL LKQVRPGMDL
SRVVLPTFIL EPRSFLDKLS DYYYHADFLS EAALEENPYF RLKKVVKWYL SGFYKKPKGL
KKPYNPILGE TFRCLWIHPR TNSKTFYIAE QVSHHPPISA FYVSNRKDGF CLSGSILAKS
KFYGNSLSAI LEGEARLTFL NRGEDYVMTM PYAHCKGILY GTMTLELGGT VNITCQKTGY
SAILEFKLKP FLGSSDYVNQ ISGKLKLGKE VLATLEGHWD SEVFINDKKT DNSEIFWNPT
PDIKQWRLIR HTVKFEEQDD FESEKLWQRV TKAINAKDQT EATQEKYVLE EAQRQAARDR
KTKTQEWVCK LFELDPLTGE WHYKFSDTRP WDPLNDMIQF EKDGVIQTKV KHRTPMVSVP
KMKHKPTRQQ KKVVKGYSSP EPDIQDSSGS EAQSVKPSTR RKKGIDLGDI QSSIESIKQT
QEEIKRNIMA LRNHLLSSTP ATDYFLQQKD YFVIFLLILL QVIINFIFK


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