OSB10_MOUSE
ID OSB10_MOUSE Reviewed; 766 AA.
AC S4R1M9; Q8R2T7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Oxysterol-binding protein-related protein 10;
DE Short=ORP-10;
DE Short=OSBP-related protein 10;
GN Name=Osbpl10 {ECO:0000312|MGI:MGI:1921736}; Synonyms=Orp10;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-766.
RC STRAIN=129;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-66, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Pancreas;
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: Probable lipid transporter involved in lipid countertransport
CC between the endoplasmic reticulum and the plasma membrane. Its ability
CC to bind phosphatidylserine, suggests that it specifically exchanges
CC phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P),
CC delivering phosphatidylserine to the plasma membrane in exchange for
CC PI4P. Plays a role in negative regulation of lipid biosynthesis.
CC Negatively regulates APOB secretion from hepatocytes. Binds cholesterol
CC and acidic phospholipids. Also binds 25-hydroxycholesterol. Binds
CC phosphatidylserine. {ECO:0000250|UniProtKB:Q9BXB5}.
CC -!- SUBUNIT: Interacts with OSBPL9. Interacts with DIAPH1.
CC {ECO:0000250|UniProtKB:Q9BXB5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9BXB5}. Note=Associates with microtubules.
CC {ECO:0000250|UniProtKB:Q9BXB5}.
CC -!- DOMAIN: The C-terminal region binds cholesterol, 25-hydroxysterol and
CC acidic phospholipids and is required for localization to microtubules.
CC {ECO:0000250|UniProtKB:Q9BXB5}.
CC -!- DOMAIN: The PH domain selectively interacts with phosphatidylinositol-
CC 4-phosphate. {ECO:0000250|UniProtKB:Q9BXB5}.
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DR EMBL; AC157586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027256; AAH27256.1; -; mRNA.
DR CCDS; CCDS40796.2; -.
DR RefSeq; NP_683761.1; NM_148958.2.
DR RefSeq; XP_006512433.1; XM_006512370.2.
DR AlphaFoldDB; S4R1M9; -.
DR SMR; S4R1M9; -.
DR STRING; 10090.ENSMUSP00000138287; -.
DR iPTMnet; S4R1M9; -.
DR PhosphoSitePlus; S4R1M9; -.
DR SwissPalm; S4R1M9; -.
DR MaxQB; S4R1M9; -.
DR PaxDb; S4R1M9; -.
DR PeptideAtlas; S4R1M9; -.
DR PRIDE; S4R1M9; -.
DR ProteomicsDB; 293524; -.
DR Antibodypedia; 1161; 171 antibodies from 30 providers.
DR DNASU; 74486; -.
DR Ensembl; ENSMUST00000183104; ENSMUSP00000138287; ENSMUSG00000040875.
DR GeneID; 74486; -.
DR KEGG; mmu:74486; -.
DR UCSC; uc009ryl.1; mouse.
DR CTD; 114884; -.
DR MGI; MGI:1921736; Osbpl10.
DR VEuPathDB; HostDB:ENSMUSG00000040875; -.
DR eggNOG; KOG2210; Eukaryota.
DR GeneTree; ENSGT00940000157880; -.
DR OMA; MHQVGQH; -.
DR OrthoDB; 949920at2759; -.
DR PhylomeDB; S4R1M9; -.
DR TreeFam; TF312807; -.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR BioGRID-ORCS; 74486; 2 hits in 61 CRISPR screens.
DR ChiTaRS; Osbpl10; mouse.
DR PRO; PR:S4R1M9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; S4R1M9; protein.
DR Bgee; ENSMUSG00000040875; Expressed in lumbar dorsal root ganglion and 202 other tissues.
DR ExpressionAtlas; S4R1M9; baseline and differential.
DR Genevisible; S4R1M9; MM.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; ISO:MGI.
DR GO; GO:0001786; F:phosphatidylserine binding; 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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; 2.
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; Cytoplasm; Cytoskeleton; Lipid biosynthesis; Lipid metabolism;
KW Lipid transport; Lipid-binding; Methylation; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..766
FT /note="Oxysterol-binding protein-related protein 10"
FT /id="PRO_0000434122"
FT DOMAIN 76..173
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..386
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 415..420
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 415..420
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 479..482
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 482
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 537..538
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 563
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 723
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 727
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 731
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 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXB5"
FT MOD_RES 40
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXB5"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXB5"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXB5"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXB5"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXB5"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXB5"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXB5"
SQ SEQUENCE 766 AA; 83856 MW; 5B15709A774E5BBE CRC64;
MERAAQSTDG GGGGGSNSSS RSSSRATSAG SSPSCSLAGR GVASRSGAAG LGGGGSRSSP
GSVAASPSGG GGRRREPALE GVLSKYTNLL QGWQSRYFVL DFEAGLLQYF VNEQSKHQKP
RGVLSLSGAI VSLSDEAPHM LVVYSANGEM YKLRAADSKE KQLWVTQLRA CAKYHMEMSS
KTTPGSRSRS LTLLPHGTPS SASPCSQRHL STGAPGVVSV TRHKSPAAAR RAKSQYSGQL
HEVREMMNQV EGQQKNLVHA IESLPGSGPL TALDQDLLLL KATSAATLSC LGECLSLLQQ
SVRQAAPPSH KPGASETILG WHGPTSHSTD QLKNGTLGSL PSASANITWA ILPNSAEEEH
NSQPEPEPDS GPELVLSEEE QSDNEDKGEV EPGAMEDQRS VILHLISQLK LGMDLTKVVL
PTFILEKRSL LEMYADFMAH PDLLLAITAG ATPEERVISF VEYYLTAFHE GRKGTLAKKP
YNPIIGETFH CSWEVPKDRV KSKWTSPHPP ISAHEHPMAD DPSKSYKLRF VAEQVSHHPP
ISCFYCECKE KRLCVNTHVW TKSKFMGMSV GVSMIGEGVL RLLDHGEEYV FTLPSAYARS
ILTVPWVELG GKVNISCAKT GYSATVTFHT KPFYGGKVHR VTAEVKHNPT NTIVCKAHGE
WNGTLEFTYS NGETKVIDTT TLPVYPKKLR PLEKQGPMES RNLWQEVTHY LRLGDIDAAT
EQKRRLEERQ RVEERKRETL RTPWRPKYFI PEGDGWVYFN PLWKTH
