ID A0A9J8BK95_CYPCA Unreviewed; 846 AA.
AC A0A9J8BK95;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE RecName: Full=Oxysterol-binding protein {ECO:0000256|RuleBase:RU003845};
OS Cyprinus carpio carpio.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000153650.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000153650.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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}.
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DR Ensembl; ENSCCRT00000106810.1; ENSCCRP00000153650.1; ENSCCRG00000030504.2.
DR GeneTree; ENSGT00940000155957; -.
DR OMA; MCANEKS; -.
DR Proteomes; UP001108240; Unplaced.
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 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:UP001108240};
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..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..275
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 96444 MW; 48E6E54937EE5E26 CRC64;
MSSEGKSSTM SQKISSPSHS NSSSSSKHDS RQDSWEIIEG LRGGLSNVQE PENQAGYMLK
KRKWPMKGWH KRFFYLDKGI LKYAKCAADV EKGKLHGCID VGLSVMAIKK KAKCIDLDAE
ENIYHLKIKS QELFDEWVSK LRHHRLYRQN EIAMFPHEKT LFHPHYPLTS SPTIPDSQSI
RKRASLAKQS SLHSPVSFTS QAKVTAWLQS SDDMDRCTKE LSVCEAQLLE LNHLLRSMEV
LHRTYSAPAI NALQASTYDS PKKEKRHPRK WRPKNCGKDN KTTLQVPSCI SAGSIRLHAS
NPNLSSVDLT NEKTYHETLD SPIDVSKLQE DFCRVANNLH STMKSALCML TTEKERLKQM
LEHDSCPAPS AQLMGLKNAL ASKQDSCDGS RPLVHQASNE SRASITESLS EFFDAQEVLL
SASSSENEPS EDDSYISDIS DNVSMENFSN EVENERLNTG CVENGGSQEQ RRCCLPSPSP
NTSNISLWNI LKNNIGKDLS KVAMPVQLNE PLNTLQRLCE ELEYSELLDK AAHTQDPFER
MVYIATFAVS GYASSYYRAG GKPFNPVLGE TYECDRPDKG FCFVAEQVSH HPPISACHAE
SKNFIFWQDV RWRNKFWGKS MEIVPVGKTH VVLPGFGDHY EWNKVTSCIH NILSGQRWIE
HYGEISIKNS NSEKCQCKVT FIKAKYWSSS MNEVEGAVTD HKGKVVHKLF GKWHEGMYYG
SPPSATCIWR MNPMPPDYEQ YYGFTKFALE LNELDPLTKA LLPPTDSRLR LDQRLLEEGN
VESAEVQKQR IEQLQRERRR VLEDNHMTHQ PRFFQKSRDD TWVSNNTYWE LRKDPGFSNF
DCPVLW
//
