GenomeNet

Database: UniProt
Entry: A0A3Q1MX43_BOVIN
LinkDB: A0A3Q1MX43_BOVIN
Original site: A0A3Q1MX43_BOVIN 
ID   A0A3Q1MX43_BOVIN        Unreviewed;       851 AA.
AC   A0A3Q1MX43;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 2.
DT   18-JUN-2025, entry version 29.
DE   RecName: Full=Oxysterol-binding protein {ECO:0000256|RuleBase:RU003845};
GN   Name=OSBPL3 {ECO:0000313|Ensembl:ENSBTAP00000060232.2,
GN   ECO:0000313|VGNC:VGNC:32462};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000060232.2, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000060232.2, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000060232.2,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000060232.2}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000060232.2};
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}.
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   AlphaFoldDB; A0A3Q1MX43; -.
DR   Ensembl; ENSBTAT00000085579.2; ENSBTAP00000060232.2; ENSBTAG00000019342.6.
DR   VEuPathDB; HostDB:ENSBTAG00000019342; -.
DR   VGNC; VGNC:32462; OSBPL3.
DR   GeneTree; ENSGT00940000155957; -.
DR   OrthoDB; 1854502at2759; -.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000019342; Expressed in oocyte and 100 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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:UP000009136};
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          261..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          782..809
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"
SQ   SEQUENCE   851 AA;  97271 MW;  0802A762AA7278BE CRC64;
     RMSDEKSLAV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE PPIQKGFLLK
     KRKWPLKGWH KRFFYLDRGI LKYAKNQTDI EREKLHGCID VGLSVMSVKK SSKCIDLDTE
     EHIYHLKVKS EDVFDEWVSK LRHHRMYRQN EIAMFPHEVN HFFPGSTVPD SGPGVMDTIS
     SRKRSSISKQ NSFQTGSNLS FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL
     QNMDILHRTY SAPAINAIQG GAFESPKKEK RSHRRWRSRA LGKDAKGTLQ VPKPFSGPIR
     LHSSNPNLST LDFGEEKNYS DGSETSSEFS KMQEDLCHIA HKVYFTLRSA FNTISTEREK
     LKQLMEQDVS ASPSAQVLGL KHALSSENSR DDSRALVHQL SNESRLSITD SLSEFFDAQE
     VLLSPSSSEN EISEDDSYVS DISDNFSLDN LSNDLDNERQ TLGPVIDSGG EARSKRRTCL
     PAPCPKSSNI SLWNILRNNI GKDLSKVAMP VELNEPLNTL QRLCEELEYS ELLDKAAQLP
     NALERMVYVA AFAVSAYASS YFRAGSKPFN PVLGETYECI REDKGFRFFS EQVSHHPPIS
     ACHAESANFV FWQDVRWKNK FWGKSMEIVP IGTTHVTLPA FGDHFEWNKV TSCIHNILSG
     QRWIEHYGEI VIKNLNDDSC HCKVNFIKAK YWSTNAHEIE GTVFDQSGKA VHRLFGKWHE
     SIYCGGSSSS ACIWRANPMP KGYEQYYGFT QFALELNEMD PLLKSLLPPT DTRFRPDQRF
     LEEGNLEEAE IQKQRIEQLQ RERRRVLEEN KVEHQPRFFR KSIDDSWVSN GTYLELRKDF
     GFSKLDHPVL W
//
DBGET integrated database retrieval system