ID A0A6I9HI52_GEOFO Unreviewed; 888 AA.
AC A0A6I9HI52;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=Oxysterol-binding protein {ECO:0000256|RuleBase:RU003845};
GN Name=OSBPL3 {ECO:0000313|RefSeq:XP_005421806.1};
OS Geospiza fortis (Medium ground-finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Thraupidae; Geospiza.
OX NCBI_TaxID=48883 {ECO:0000313|Proteomes:UP000504602, ECO:0000313|RefSeq:XP_005421806.1};
RN [1] {ECO:0000313|RefSeq:XP_005421806.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_005421806.1; XM_005421749.2.
DR AlphaFoldDB; A0A6I9HI52; -.
DR GeneID; 102033666; -.
DR KEGG; gfr:102033666; -.
DR CTD; 26031; -.
DR InParanoid; A0A6I9HI52; -.
DR OrthoDB; 1854502at2759; -.
DR Proteomes; UP000504602; 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:UP000504602};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003845}.
FT DOMAIN 50..145
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 101248 MW; 2D205D0D5331E340 CRC64;
MSEEKNFGAS QKMLSPSRST SSCSSKQGSR QDSWEIVEGL RGAMNCTQEP QKQEGCLLKK
RKWPLKGWHK RYFFLDRGIL KYSKCRADIE RGKLHGCIDV GLSVMSVKKS TKCIDLDTEE
QIYHLKVKSQ ELFDEWVAKL RHHRMYRQNE ISMFPHDANN IFFPVSTTTD SVPGFCDSAP
GRKAGSLTKQ NSTSTGGNLS FSFSSNESRI SSWLQSSEDM EKCSRDLSNC HTYLLEMNQL
LQSMDVLHRT YSAPAINAMQ VGPFESPKKE KRTHRRWRSR VVGKEAKGML QVPSVFSAPM
RLHASNPNLS TIDFVEEKNY SDGSETSSEF TKMQEDLFHV AHKVYFTLRS AFSTISTERE
KLKQMLEYDA SSSPSAQIVG LKNALTSAIA QNTDLKDRLR RIHAESKIID SASNAKSSPD
LVKENSREEG RGLVHQVSNE SRLSIADSLT EFFDAQEVLL SASSSENEVS DDDSYVSDIS
DNASEDNLSN DMENERQTLD CISESGIGCN SKRRTCLPAP CPNTSNISLW NILRNNIGKD
LSKVAMPVEL NEPLNTLQRL CEELEYSELL DTAAHTPNPF ERMVYIAAFA VSAYASSYYR
AGSKPFNPVL GETYECIRED KGFQFFAEQV SHHPPISACH AESVNFAFWQ DVRWKNKFWG
KSMEIVPVGT THVTLPAFKD HFAWNKVTSC IHNILSGQRW IEHYGEIIIK NLNDDTCHCK
LTFIKAKYWS PNAHEIEGSV VDKSGKVVHR LYGKWHESLY CGTTSSSNCI WRANPMPKDY
EQWYGFTQFA LELNELDPQT RSLLPSTDTR FRPDQRFLEE GNIEGAEMQK QRIEQLQRER
RKVLEENNLE HQPRFFRKSS DDSWVSNGTY MDLRKEPGFS KLDNPVLW
//
