ID B3P6V1_DROER Unreviewed; 783 AA.
AC B3P6V1;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Oxysterol-binding protein {ECO:0000256|RuleBase:RU003845};
GN Name=Dere\Osbp {ECO:0000313|EMBL:EDV53771.1};
GN ORFNames=Dere_GG12301 {ECO:0000313|EMBL:EDV53771.1};
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000313|EMBL:EDV53771.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53771.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [2] {ECO:0000313|EMBL:EDV53771.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53771.1};
RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT "Assembly reconciliation.";
RL Bioinformatics 24:42-45(2008).
RN [3] {ECO:0000313|EMBL:EDV53771.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53771.1};
RG FlyBase;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the OSBP family.
CC {ECO:0000256|RuleBase:RU003844}.
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DR EMBL; CH954182; EDV53771.1; -; Genomic_DNA.
DR RefSeq; XP_001981901.1; XM_001981865.2.
DR AlphaFoldDB; B3P6V1; -.
DR EnsemblMetazoa; FBtr0132355; FBpp0130847; FBgn0084403.
DR GeneID; 6554142; -.
DR KEGG; der:6554142; -.
DR eggNOG; KOG1737; Eukaryota.
DR HOGENOM; CLU_007105_5_1_1; -.
DR OMA; LPEMKGW; -.
DR OrthoDB; 960at2759; -.
DR PhylomeDB; B3P6V1; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblMetazoa.
DR GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblMetazoa.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007030; P:Golgi organization; IEA:EnsemblMetazoa.
DR GO; GO:0006886; P:intracellular protein transport; IEA:EnsemblMetazoa.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0007291; P:sperm individualization; IEA:EnsemblMetazoa.
DR CDD; cd13284; PH_OSBP_ORP4; 1.
DR Gene3D; 2.40.160.120; -; 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; IPR001849; PH_domain.
DR PANTHER; PTHR10972:SF205; OXYSTEROL-BINDING PROTEIN; 1.
DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055,
KW ECO:0000256|RuleBase:RU003845};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003845}.
FT DOMAIN 14..107
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 281..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 218..248
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 291..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 89226 MW; FC67B46ADCB4F14B CRC64;
MTDAAGNALA EKGLPEMKGW LLKWTNYIKG YQRRWFVLSK GVLSYYRNQS EINHTCRGTI
SLHGALIHTV DSCTFVISNG GTQTFHIKAG TEVERQSWVT ALELAKAKAI RAIECEEEEE
TETAHVVPSQ EISSVVRDLT DRLENMRTCY DLITKHGAAL QRALNDLETN EEESLASRTK
IVNERATLFR ITSNAMINAG NDYLHTAEVQ GHKWSKMLHH EREQRQRLEE IIEQMAKQQS
QMEQAAVLVR QNKPVPSSSG AGTAGSLVTS DEEMEFFDAE EHGYSGSGRS PESPDRERGT
FILKMNKRRS SSEDQVEGHL EGSSSESDEQ KRTVQTVQQV CLVSAPRVAS GGQGDDDDVD
KALPAKQSTD SIYGRNWNPE LIKKRRDRVP DKPNHPISLW GIMKNCIGKD LSKIPMPINF
NEPLSMLQRL VEDYEYTEIL DYAATCQDEC EQLAYIAAFT VSAYATTTNR TGKPFNPLLG
ETYECDRMDD YGWRCLAEQV SHHPPVAALH CESKNWTCWQ EFSMTSKFRG KYVQVNPLGG
VYVQFPNSGR RYSWRKVTTT VNNIIVGKLW VDQHGEMEIL GSQAAQGHKC ILNFIPYSYF
SRDVQRSVKG VVMNKDNEVK WVVRGTWDMK IEIAPVLSTS GSASSPTYTT GEFKLAWRRR
PAPPDSDKFY NFTILACQLN EEEEGVAPTD SRLRPDQRLM EQGDWDESNK EKLRLEEKQR
TERRRRENEA EEAAAEGRPY PAYEPMWFKR EKEEGSEEYV HVFKNTYWEA KAAQKFEGCP
NIY
//
