ID A0A3P9B7F4_9CICH Unreviewed; 854 AA.
AC A0A3P9B7F4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE RecName: Full=Oxysterol-binding protein {ECO:0000256|RuleBase:RU003845};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005005785.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005005785.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005005785.1}
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 AlphaFoldDB; A0A3P9B7F4; -.
DR Ensembl; ENSMZET00005006037.1; ENSMZEP00005005785.1; ENSMZEG00005004482.1.
DR GeneTree; ENSGT00940000156791; -.
DR Proteomes; UP000265160; LG16.
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 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:UP000265160};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003845}.
FT DOMAIN 71..166
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..273
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 377..404
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 26..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 97127 MW; 9C113865DCA06D6D CRC64;
MSHHQHYQQR GPHSRTMSSE ERSSTPVNKI STPVHKSTSS SSSSQRDSRQ EADSWEIIEG
LKIGQSNVQR PDKHEGFMLK KRKWPLKGWH KRFFVLDNGI LKYSKSPIDI QKGKLHGSID
VGLSVMSIKK RARRIDLDTE EHIYHLKVKS QDIFDAWVSK LRHHRLYRQN EIVRSPRDAT
MRTFPPSAAM DSPQPTPAVV NEVKTKPSSL PWQPAAPSNS STSSLPASYS NGQSKVVAWL
QESEEMDKCA EELARCQSNL TELSRLLQSL EILQRTQSAP NFTDMQVPLS ASMSPVRLHS
SNPNLCAELV DFQPPVSRLT DSVECASDYI KLQEEFCIIA QKVHSLLKSA FNTVAIEKEK
IKQILSDQEQ PDQSAQINSL RKSLSQALSQ NAELRTRLNR IHSESVLTEQ VVSVNIISTP
DEAGEQMGIP LTQQASNESR LSMSESVSEF FDAQEVLLSA SSSENEGSDD ESYVSDVSDN
ISEDNASVTD NVSRQMANGD FAGSAFRNGR RSCLSAPCPD TSNINLWNIL RNNIGKDLSK
VSMPVELNEP LNTLQRMCEE LEYSELLDKA AETEDPFERM VLVAAFAVSG YSSTYYRAGS
KPFNPLLGET YECIREDKGF CFFSEQVSHH PPVSACHCES KNFTFWQDVR WKNKFWGKSM
EILPIGSVNL MIPRFGDQYE WNKVTTCVHN ILSGRRWIEH YGEITIRNIK SSACLCKLTF
VKGNYWSSNV NEVQGFVMDQ EGKVIHRLFG KWHEGVYCGV PPSAKCIWRP GSMPTDYELY
YGFTRFAIEL NELCPELKDA LPRTDARFRP DQRYLEEGNL EMASSEKQRI EDMQRVRRKW
NDENNIKHEP RFFK
//
