ID   A0A9J8BW86_CYPCA        Unreviewed;       894 AA.
AC   A0A9J8BW86;
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:ENSCCRP00000162169.1, ECO:0000313|Proteomes:UP001108240};
RN   [1] {ECO:0000313|Ensembl:ENSCCRP00000162169.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Endoplasmic
CC       reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
CC   -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000256|ARBA:ARBA00008842,
CC       ECO:0000256|RuleBase:RU003844}.
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DR   Ensembl; ENSCCRT00000173313.1; ENSCCRP00000162169.1; ENSCCRG00000060246.1.
DR   GeneTree; ENSGT00940000156791; -.
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:000002; 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:SF76; OXYSTEROL-BINDING PROTEIN-RELATED PROTEIN 6; 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   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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP001108240};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003845}.
FT   DOMAIN          41..136
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          148..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          820..848
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        159..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   894 AA;  102056 MW;  29A0163136F6A00B CRC64;
     LDKYSREYSC LSEHKQNSCY ETDSWEIIEG LRIGQTHIQR PEKHEGFMLK KRKWPLKGWH
     KRFFVLDNGI LKYSKSPVDT QKGKLHGSID VGLSVMSIKK RARRIDLDTE EHIYHLKVKS
     PDVFDIWVFK LRHHRLFRQN EIVRSPRDAT LRTFPPSASA ESPQNTSSSQ GKPSGLPWQL
     PPSCSNGQSK VAAWLQESEE MDKCAEDLAY CQSSLLELSQ LLQSLEILQR TQSAPNFTDM
     QSNCVNLTKK EKRVSRRWRT KSVSKDAKFK LQRISPAQGA MNTVPLSASM SQVCLHASNP
     NLCVELADFQ TPVTRLTDSI DSASDYIKLQ EDFCIVAQKV HSLLKSAFNT VAIEKEKIKQ
     VLLEQEQTGQ SHQIITLRRS LSQVSSALSQ NAELKTRLNR IHSESVLSDQ VVSVNIISSP
     DEAGDPLHVG IPLSQQVSNE SRLSMSESVS EFFDAQEVLL SASSSENEAS DDESYISDVS
     DNISEDNASV TDNVSRQMPN GDLASGAFRN GRRTCLPAPA PDTSNINLWN ILKNNIGKDL
     SKVSMPVELN EPLNTLQHMC EELEYTELLD KAAQTDDPYE RMAIVAAFAV SGYSSTYYRA
     GSKPFNPLLG ETYECIREDK GFCFFSEQVS HHPPISACHC ESQNFTFWQG KTDTTPIFNS
     QRLFIPHSSV CLCVRLYGDS SHWNSECHVT ACIHNILSGR RWIEHYGEVT IRNTRNTTCI
     CKLTFVKGNY WSSNVNEVQG SVMDQEGKVI HRLFGKWHEG LYCGVPPSAK CIWRPGSMPT
     DYELYYGFSR FAIELNELCP ELKELLPPTD ARFRPDQRYL EEGNVQMAAA EKQRIEEQQR
     NRRKWLEENN IRHQPRFFKK VMDSHQRERW VSNNTYWELR KDPGFLKLEN PELW
//