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Oxysterol-binding protein-related protein 5 (ORP-5) (OSBP-related protein 5) (Oxysterol-binding protein homolog 1)

 OSBL5_MOUSE             Reviewed;         874 AA.
Q9ER64; Q8R510; Q99NF5;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
11-FEB-2002, sequence version 3.
28-MAR-2018, entry version 127.
RecName: Full=Oxysterol-binding protein-related protein 5;
Short=ORP-5;
Short=OSBP-related protein 5;
AltName: Full=Oxysterol-binding protein homolog 1 {ECO:0000303|Ref.2};
Name=Osbpl5; Synonyms=Obph1 {ECO:0000303|Ref.2}, Osbp2;
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 [GENOMIC DNA / MRNA].
STRAIN=129/Sv;
PubMed=11063728; DOI=10.1093/hmg/9.18.2691;
Engemann S., Stroedicke M., Paulsen M., Franck O., Reinhardt R.,
Lane N., Reik W., Walter J.;
"Sequence and functional comparison in the Beckwith-Wiedemann region:
implications for a novel imprinting centre and extended imprinting.";
Hum. Mol. Genet. 9:2691-2706(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Higashimoto K., Soejima H., Yatsuki H., Joh K., Wang Y., Ishino F.,
Ono R., Jinno Y., Iwasaka T., Uchiyama M., Masuko S., Xin Z., Zhu X.,
Katsuki T., Mukai T.;
"Unique imprinted status of mouse Obph1 gene and no imprimted status
of the human homologue in placenta.";
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; 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]
IMPRINTING.
PubMed=18024232; DOI=10.1016/j.modgep.2007.09.005;
Kuzmin A., Han Z., Golding M.C., Mann M.R., Latham K.E., Varmuza S.;
"The PcG gene Sfmbt2 is paternally expressed in extraembryonic
tissues.";
Gene Expr. Patterns 8:107-116(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-746 AND SER-749,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Lung;
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: 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. May cooperate with NPC1 to mediate the
exit of cholesterol from endosomes/lysosomes. Binds 25-
hydroxycholesterol and cholesterol.
{ECO:0000250|UniProtKB:Q9H0X9}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q9H0X9}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q9H0X9}. Note=Localizes to the cortical
endoplasmic reticulum at the endoplasmic reticulum-plasma membrane
contact sites. {ECO:0000250|UniProtKB:Q9H0X9}.
-!- MISCELLANEOUS: Imprinted gene expressed from the maternal allele
in blastocysts. {ECO:0000269|PubMed:18024232}.
-!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAC16404.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAC27351.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ278263; CAC16404.2; ALT_INIT; mRNA.
EMBL; AJ276505; CAC27351.1; ALT_INIT; Genomic_DNA.
EMBL; AB074008; BAB85687.1; -; mRNA.
EMBL; BC079872; AAH79872.1; -; mRNA.
CCDS; CCDS57598.1; -.
RefSeq; NP_001186156.1; NM_001199227.1.
UniGene; Mm.21199; -.
ProteinModelPortal; Q9ER64; -.
SMR; Q9ER64; -.
STRING; 10090.ENSMUSP00000020411; -.
iPTMnet; Q9ER64; -.
PhosphoSitePlus; Q9ER64; -.
EPD; Q9ER64; -.
MaxQB; Q9ER64; -.
PaxDb; Q9ER64; -.
PRIDE; Q9ER64; -.
Ensembl; ENSMUST00000119499; ENSMUSP00000113362; ENSMUSG00000037606.
GeneID; 79196; -.
KEGG; mmu:79196; -.
UCSC; uc009kpw.2; mouse.
CTD; 114879; -.
MGI; MGI:1930265; Osbpl5.
eggNOG; KOG2210; Eukaryota.
eggNOG; ENOG410XRW6; LUCA.
GeneTree; ENSGT00550000074515; -.
HOGENOM; HOG000233870; -.
HOVERGEN; HBG053375; -.
InParanoid; Q9ER64; -.
KO; K20464; -.
PhylomeDB; Q9ER64; -.
Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
ChiTaRS; Osbpl5; mouse.
PRO; PR:Q9ER64; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000037606; -.
CleanEx; MM_OSBP2; -.
CleanEx; MM_OSBPL5; -.
ExpressionAtlas; Q9ER64; baseline and differential.
Genevisible; Q9ER64; MM.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO: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:0015914; P:phospholipid transport; ISS:UniProtKB.
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;
Coiled coil; Complete proteome; Endoplasmic reticulum;
Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 874 Oxysterol-binding protein-related protein
5.
/FTId=PRO_0000100374.
TRANSMEM 855 873 Helical. {ECO:0000255}.
DOMAIN 126 243 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
REGION 383 388 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 383 388 Phosphatidylserine binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 445 448 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 477 478 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
COILED 93 123 {ECO:0000255}.
BINDING 448 448 Phosphatidylserine.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 503 503 Phosphatidylserine.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 669 669 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 673 673 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 677 677 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 746 746 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 749 749 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 37 44 ENELGPIT -> MSLVPSPQ (in Ref. 1;
CAC27351). {ECO:0000305}.
CONFLICT 312 312 D -> N (in Ref. 2; BAB85687).
{ECO:0000305}.
SEQUENCE 874 AA; 98922 MW; FBC41FA8E219F5E3 CRC64;
MKEEAFLRRR FSLCPPASTP QKTDPRKVPR NLLLGCENEL GPITPGRDME SNGPSQPRDE
EPQTPGSATK VPLAEYRLCN GSDKECTSPT TRVSKKDALK AQKENYRQEK KRATKQLFSA
LTDPSVVIMA DSLKIRGTLK SWTKLWCVLK PGVLLIYKTP KVGQWVGTVL LHCCELIERP
SKKDGFCFKL FHPLDQSVWA VKGPKGESVG SITQPLPSSY LIFRAASESD GRCWLDALEL
ALRCSSLLRL STCKQGRDGE QGSSPDASPS SLYGLPTSAT IPDQDLFPLN GSALENDAFS
DKSERENAED SDAETQDHSR KTNESGSDLL DSPGGPWRGT TYVEQVQEEL GELDETSQVE
TVSEENKSLM WVLLRQLRPG MDLSRVVLPT FVLEPRSFLG KLSDYYYHGD LLSRAAAEDD
PYCRMKLVLR WYLSGFYKKP KGIKKPYNPI LGETFRCRWL HPQTNSHTFY IAEQVSHHPP
VSAFYVSNRK DGFCMSGSIT AKSKFYGNSL SALLDGKAKL TFLNRKEEYT LTMPYAHCRG
ILYGTMTMEL GGKVNIECEK NNLQAELDFK LKPFFGSSAN INQISGKIMS GEEVLARLTG
HWDRDVFIKE ESSGGTELFW TPSEEVRRQR LKRHTVLLEE QSELESERLW QHVTRAIREG
DQHKATQEKS VLEEAQRQRA REHQQSLTPW KPQLFLLDPL TQEWRYRYED LSPWDPLKDI
AQYEQDGILH TLQRETMSGQ TTFLGSPDSR HKRPSSDRRL RKASDQPSGH SQVTESSGST
PESCPDLSDE DFVPGGESPC PRCRREVHRL KMLQEAVLSI QEAQQELHRH LSTMLSSTVR
AGQAPAPSLL QNPRSWFLLC IFLTCQLFIN YILK


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