OSBL5_MOUSE
ID OSBL5_MOUSE Reviewed; 874 AA.
AC Q9ER64; Q8R510; Q99NF5;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Oxysterol-binding protein-related protein 5;
DE Short=ORP-5;
DE Short=OSBP-related protein 5;
DE AltName: Full=Oxysterol-binding protein homolog 1 {ECO:0000303|Ref.2};
GN Name=Osbpl5; Synonyms=Obph1 {ECO:0000303|Ref.2}, Osbp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv;
RX PubMed=11063728; DOI=10.1093/hmg/9.18.2691;
RA Engemann S., Stroedicke M., Paulsen M., Franck O., Reinhardt R., Lane N.,
RA Reik W., Walter J.;
RT "Sequence and functional comparison in the Beckwith-Wiedemann region:
RT implications for a novel imprinting centre and extended imprinting.";
RL Hum. Mol. Genet. 9:2691-2706(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Higashimoto K., Soejima H., Yatsuki H., Joh K., Wang Y., Ishino F., Ono R.,
RA Jinno Y., Iwasaka T., Uchiyama M., Masuko S., Xin Z., Zhu X., Katsuki T.,
RA Mukai T.;
RT "Unique imprinted status of mouse Obph1 gene and no imprimted status of the
RT human homologue in placenta.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IMPRINTING.
RX PubMed=18024232; DOI=10.1016/j.modgep.2007.09.005;
RA Kuzmin A., Han Z., Golding M.C., Mann M.R., Latham K.E., Varmuza S.;
RT "The PcG gene Sfmbt2 is paternally expressed in extraembryonic tissues.";
RL Gene Expr. Patterns 8:107-116(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-746 AND SER-749, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Lipid transporter involved in lipid countertransport between
CC the endoplasmic reticulum and the plasma membrane: specifically
CC exchanges phosphatidylserine with phosphatidylinositol 4-phosphate
CC (PI4P), delivering phosphatidylserine to the plasma membrane in
CC exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in
CC the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a
CC mutually exclusive manner. May cooperate with NPC1 to mediate the exit
CC of cholesterol from endosomes/lysosomes. Binds 25-hydroxycholesterol
CC and cholesterol. {ECO:0000250|UniProtKB:Q9H0X9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9H0X9}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9H0X9}. Note=Localizes to endoplasmic
CC reticulum-plasma membrane contact sites (EPCS). Localizes to the
CC cortical endoplasmic reticulum at the EPCS.
CC {ECO:0000250|UniProtKB:Q9H0X9}.
CC -!- MISCELLANEOUS: Imprinted gene expressed from the maternal allele in
CC blastocysts. {ECO:0000269|PubMed:18024232}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC16404.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC27351.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ278263; CAC16404.2; ALT_INIT; mRNA.
DR EMBL; AJ276505; CAC27351.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB074008; BAB85687.1; -; mRNA.
DR EMBL; BC079872; AAH79872.1; -; mRNA.
DR CCDS; CCDS57598.1; -.
DR RefSeq; NP_001186156.1; NM_001199227.1.
DR AlphaFoldDB; Q9ER64; -.
DR SMR; Q9ER64; -.
DR BioGRID; 219738; 1.
DR STRING; 10090.ENSMUSP00000020411; -.
DR iPTMnet; Q9ER64; -.
DR PhosphoSitePlus; Q9ER64; -.
DR EPD; Q9ER64; -.
DR MaxQB; Q9ER64; -.
DR PaxDb; Q9ER64; -.
DR PRIDE; Q9ER64; -.
DR ProteomicsDB; 293526; -.
DR Antibodypedia; 23281; 85 antibodies from 24 providers.
DR DNASU; 79196; -.
DR Ensembl; ENSMUST00000119499; ENSMUSP00000113362; ENSMUSG00000037606.
DR GeneID; 79196; -.
DR KEGG; mmu:79196; -.
DR UCSC; uc009kpw.2; mouse.
DR CTD; 114879; -.
DR MGI; MGI:1930265; Osbpl5.
DR VEuPathDB; HostDB:ENSMUSG00000037606; -.
DR eggNOG; KOG2210; Eukaryota.
DR GeneTree; ENSGT00940000159535; -.
DR HOGENOM; CLU_012334_2_1_1; -.
DR InParanoid; Q9ER64; -.
DR OMA; NHHMEND; -.
DR PhylomeDB; Q9ER64; -.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR BioGRID-ORCS; 79196; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Osbpl5; mouse.
DR PRO; PR:Q9ER64; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9ER64; protein.
DR Bgee; ENSMUSG00000037606; Expressed in ileal epithelium and 211 other tissues.
DR ExpressionAtlas; Q9ER64; baseline and differential.
DR Genevisible; Q9ER64; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; ISO:MGI.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0140343; F:phosphatidylserine transfer activity; ISS:UniProtKB.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; Lipid transport; Lipid-binding;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..874
FT /note="Oxysterol-binding protein-related protein 5"
FT /id="PRO_0000100374"
FT TRANSMEM 855..873
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 126..243
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 93..123
FT /evidence="ECO:0000255"
FT COMPBIAS 299..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 383..388
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 383..388
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 445..448
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 448
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 477..478
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 503
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 669
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 673
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 677
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 37..44
FT /note="ENELGPIT -> MSLVPSPQ (in Ref. 1; CAC27351)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="D -> N (in Ref. 2; BAB85687)"
FT /evidence="ECO:0000305"
SQ 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
