ID A0A7J8D7E0_ROUAE Unreviewed; 887 AA.
AC A0A7J8D7E0;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=Oxysterol-binding protein {ECO:0000256|RuleBase:RU003845};
GN ORFNames=HJG63_014752 {ECO:0000313|EMBL:KAF6419097.1};
OS Rousettus aegyptiacus (Egyptian fruit bat) (Pteropus aegyptiacus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Rousettinae; Rousettus.
OX NCBI_TaxID=9407 {ECO:0000313|EMBL:KAF6419097.1, ECO:0000313|Proteomes:UP000593571};
RN [1] {ECO:0000313|EMBL:KAF6419097.1, ECO:0000313|Proteomes:UP000593571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRouAeg1 {ECO:0000313|EMBL:KAF6419097.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6419097.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- FUNCTION: Phosphoinositide-binding protein which associates with both
CC cell and endoplasmic reticulum (ER) membranes. Can bind to the ER
CC membrane protein VAPA and recruit VAPA to plasma membrane sites, thus
CC linking these intracellular compartments. The ORP3-VAPA complex
CC stimulates RRAS signaling which in turn attenuates integrin beta-1
CC (ITGB1) activation at the cell surface. With VAPA, may regulate ER
CC morphology. Has a role in regulation of the actin cytoskeleton, cell
CC polarity and cell adhesion. Binds to phosphoinositides with preference
CC for PI(3,4)P2 and PI(3,4,5)P3. Also binds 25-hydroxycholesterol and
CC cholesterol. {ECO:0000256|ARBA:ARBA00055107}.
CC -!- SUBUNIT: Homodimer. Interacts with RRAS. Interacts (phosphorylated
CC form) with VAPA. Interacts with OSBPL6.
CC {ECO:0000256|ARBA:ARBA00064163}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell
CC projection, filopodium tip {ECO:0000256|ARBA:ARBA00004495}. Cytoplasm,
CC cytosol {ECO:0000256|ARBA:ARBA00004514}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}. Nucleus membrane
CC {ECO:0000256|ARBA:ARBA00004617}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004617}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000256|ARBA:ARBA00008842,
CC ECO:0000256|RuleBase:RU003844}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6419097.1}.
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DR EMBL; JACASE010000013; KAF6419097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8D7E0; -.
DR OrthoDB; 1854502at2759; -.
DR Proteomes; UP000593571; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0031965; C:nuclear membrane; IEA:TreeGrafter.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0015485; F:cholesterol binding; IEA:TreeGrafter.
DR GO; GO:0005319; F:lipid transporter activity; IEA:UniProtKB-ARBA.
DR CDD; cd13287; PH_ORP3_ORP6_ORP7; 1.
DR FunFam; 2.30.29.30:FF:000011; Oxysterol-binding protein; 1.
DR FunFam; 2.40.160.120:FF:000001; Oxysterol-binding protein; 1.
DR FunFam; 3.30.70.3490:FF:000004; Oxysterol-binding protein; 1.
DR Gene3D; 2.40.160.120; -; 1.
DR Gene3D; 3.30.70.3490; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR041680; PH_8.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10972:SF15; OXYSTEROL-BINDING PROTEIN-RELATED PROTEIN 3; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF15409; PH_8; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055,
KW ECO:0000256|RuleBase:RU003845};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000593571};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003845}.
FT DOMAIN 51..146
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 818..845
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..32
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..280
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 100746 MW; 28BEEB2126D2AE90 CRC64;
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTEE PSVQKGFLLK
KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID VGLSVMSVKK SSKCIDLDTE
EHIYHLKVKS EEVFEEWVSK LRHHRMYRQN EIAMFPHEVN HFFPGSSITD SAPGVLDSIS
SRKRSSISKQ NSFQTGSNLS FSCGSETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL
QSMDVLHRTY SAPAINAIQG GTFESPKKEK RSHRRWRSRA IGKDAKGTLQ VPKPFSGPQR
LHSSNPNLST LDFGEEKNYS DGSETSSEFS KMQEDLCHIA HKVYFTLRSA FNTISTEKEK
LKQLMDQDVS SSPSAQVVGL KHALSSALAQ NTDLKERLCR IHAESLLLDP PAAAKSGDSL
AEENSADNSR PLVHQLSNES RLSIADSLSE FFDAQEVLLS PSSSENEVSE DDSYVSDISD
NLSLDNLSND LDNERQTLGP VLECGGEAKC RRRTCLPAPC PNTSNISLWN ILRNNIGKDL
SKVAMPVQLN EPLNTLQRLC EELEYSELLD KAAQIPSALE RMVYVAAFAV SAYASSFFRA
GSKPFNPVLG ETYECIREDK GFRFFSEQVS HHPPISACHA ESGNFVFWQD VRWKNKFWGK
SMEIVPIGTT HVTLPAFGDH FEWNKVTSCI HNILSGQRWI EHYGEIVIRN LNDDSCYCKV
NFIKAKYWST NAREIEGTVF DRSGNAVHRL FGKWHESIYC GGSSSSACVW RANPMPKGYE
QYYGFTQFAL ELNDIDPLCV SSLPPTDTRF RPDQRFLEEG NIEEAETQKQ RIEQLQRERR
RVLEENCVEH QPRFFRKSDD DSWVSNGTYL ELRKDLGFSK LDHPVLW
//
