ID B3LXT0_DROAN Unreviewed; 373 AA.
AC B3LXT0;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=G-protein coupled receptors family 1 profile domain-containing protein {ECO:0000259|PROSITE:PS50262};
GN Name=Dana\GF17352 {ECO:0000313|EMBL:EDV41737.1};
GN Synonyms=dana_GLEANR_18619 {ECO:0000313|EMBL:EDV41737.1};
GN ORFNames=GF17352 {ECO:0000313|EMBL:EDV41737.1};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV41737.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV41737.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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).
CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC mediate vision. They consist of an apoprotein, opsin, covalently linked
CC to cis-retinal. {ECO:0000256|ARBA:ARBA00002881}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000256|RuleBase:RU004951}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU004951}.
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DR EMBL; CH902617; EDV41737.1; -; Genomic_DNA.
DR RefSeq; XP_001953154.1; XM_001953119.2.
DR AlphaFoldDB; B3LXT0; -.
DR SMR; B3LXT0; -.
DR STRING; 7217.B3LXT0; -.
DR EnsemblMetazoa; FBtr0122052; FBpp0120544; FBgn0094370.
DR GeneID; 6500137; -.
DR KEGG; dan:6500137; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; B3LXT0; -.
DR OMA; MEQLNCG; -.
DR OrthoDB; 3432893at2759; -.
DR PhylomeDB; B3LXT0; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005769; C:early endosome; IEA:EnsemblMetazoa.
DR GO; GO:0016027; C:inaD signaling complex; IEA:EnsemblMetazoa.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:EnsemblMetazoa.
DR GO; GO:0016029; C:subrhabdomeral cisterna; IEA:EnsemblMetazoa.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IEA:EnsemblMetazoa.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:EnsemblMetazoa.
DR GO; GO:0009589; P:detection of UV; IEA:EnsemblMetazoa.
DR GO; GO:0046673; P:negative regulation of compound eye retinal cell programmed cell death; IEA:EnsemblMetazoa.
DR GO; GO:0071632; P:optomotor response; IEA:EnsemblMetazoa.
DR GO; GO:0030265; P:phospholipase C-activating rhodopsin mediated signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0042331; P:phototaxis; IEA:EnsemblMetazoa.
DR GO; GO:0009642; P:response to light intensity; IEA:EnsemblMetazoa.
DR GO; GO:0042052; P:rhabdomere development; IEA:EnsemblMetazoa.
DR GO; GO:0043052; P:thermotaxis; IEA:EnsemblMetazoa.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd15079; 7tmA_photoreceptors_insect; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001760; Opsin.
DR InterPro; IPR001735; Opsin_RH1/RH2.
DR InterPro; IPR027430; Retinal_BS.
DR PANTHER; PTHR24240; OPSIN; 1.
DR PANTHER; PTHR24240:SF85; OPSIN RH1-RELATED; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00576; OPSINRH1RH2.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|RuleBase:RU004951};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU004951};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004951};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543,
KW ECO:0000256|RuleBase:RU004951};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004951};
KW Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW Retinal protein {ECO:0000256|ARBA:ARBA00022925,
KW ECO:0000256|RuleBase:RU004951};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606,
KW ECO:0000256|RuleBase:RU004951};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU004951};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU004951};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU004951}; Vision {ECO:0000256|ARBA:ARBA00023305}.
FT TRANSMEM 48..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 88..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 125..146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 166..188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 215..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 277..295
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT DOMAIN 67..329
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 354..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 373 AA; 41479 MW; E2B6743B8E416015 CRC64;
MESFAAAATQ LGPHFAPLSN GSVVDKVTPD MAHLISPYWN QFPAMDPIWA KILTAYMIII
GMISWCGNGV VIYIFATTKS LRTPANLLVI NLAISDFGIM ITNTPMMGIN LYFETWVLGP
MMCDIYAGLG SAFGCSSIWS MCMISLDRYQ VIVKGMAGRP MTIPLALGKI AYIWFMSSIW
CLAPAFGWSR YVPEGNLTSC GIDYLERDWN PRSYLIFYSI FVYYIPLFLI CYSYWFIIAA
VSAHEKAMRE QAKKMNVKSL RSSEDAEKSA EGKLAKVALV TITLWFMAWT PYLVINCMGL
FKFEGLTPLN TIWGACFAKS AACYNPIVYG ISHPKYRLAL KEKCPCCVFG KVDDGKSSDA
QSQATASEAE SKA
//
