OPS5_DROME
ID OPS5_DROME Reviewed; 382 AA.
AC P91657; P91671; Q9VKD1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Opsin Rh5;
GN Name=Rh5; ORFNames=CG5279;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S; TISSUE=Retina;
RX PubMed=8982159; DOI=10.1016/s0896-6273(00)80243-3;
RA Chou W.-H., Hall K.J., Wilson D.B., Wideman C.L., Townson S.M.,
RA Chadwell L.V., Britt S.G.;
RT "Identification of a novel Drosophila opsin reveals specific patterning of
RT the R7 and R8 photoreceptor cells.";
RL Neuron 17:1101-1115(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9165115; DOI=10.1242/dev.124.9.1665;
RA Papatsenko D., Sheng G., Desplan C.;
RT "A new rhodopsin in R8 photoreceptors of Drosophila: evidence for
RT coordinate expression with Rh3 in R7 cells.";
RL Development 124:1665-1673(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the retina. Each
CC Drosophila eye is composed of 800 facets or ommatidia. Each ommatidium
CC contains 8 photoreceptor cells (R1-R8), the R1 to R6 cells are outer
CC cells, while R7 and R8 are inner cells. Rh5 is expressed only in the R8
CC cells of ommatidia in which Rh3 is expressed in the overlying R7 cells.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U67905; AAC47426.1; -; Genomic_DNA.
DR EMBL; U80667; AAB38966.1; -; mRNA.
DR EMBL; AE014134; AAF53145.1; -; Genomic_DNA.
DR EMBL; AY069237; AAL39382.1; -; mRNA.
DR RefSeq; NP_001285859.1; NM_001298930.1.
DR RefSeq; NP_477096.1; NM_057748.5.
DR AlphaFoldDB; P91657; -.
DR SMR; P91657; -.
DR BioGRID; 60667; 4.
DR STRING; 7227.FBpp0079875; -.
DR GlyGen; P91657; 1 site.
DR PaxDb; P91657; -.
DR DNASU; 34615; -.
DR EnsemblMetazoa; FBtr0080291; FBpp0079875; FBgn0014019.
DR EnsemblMetazoa; FBtr0342591; FBpp0309539; FBgn0014019.
DR GeneID; 34615; -.
DR KEGG; dme:Dmel_CG5279; -.
DR CTD; 34615; -.
DR FlyBase; FBgn0014019; Rh5.
DR VEuPathDB; VectorBase:FBgn0014019; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; P91657; -.
DR OMA; VRTHEQM; -.
DR OrthoDB; 723541at2759; -.
DR PhylomeDB; P91657; -.
DR BioGRID-ORCS; 34615; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34615; -.
DR PRO; PR:P91657; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0014019; Expressed in head capsule and 9 other tissues.
DR ExpressionAtlas; P91657; baseline and differential.
DR Genevisible; P91657; DM.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IGI:FlyBase.
DR GO; GO:0016038; P:absorption of visible light; IMP:FlyBase.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IGI:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007602; P:phototransduction; IGI:FlyBase.
DR GO; GO:0009416; P:response to light stimulus; IDA:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR GO; GO:0043052; P:thermotaxis; IMP:FlyBase.
DR GO; GO:0009588; P:UV-A, blue light phototransduction; NAS:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000856; Opsin_RH3/RH4.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00577; OPSINRH3RH4.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 2: Evidence at transcript level;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..382
FT /note="Opsin Rh5"
FT /id="PRO_0000197633"
FT TOPO_DOM 1..49
FT /note="Extracellular"
FT TRANSMEM 50..76
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..88
FT /note="Cytoplasmic"
FT TRANSMEM 89..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..127
FT /note="Extracellular"
FT TRANSMEM 128..147
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..165
FT /note="Cytoplasmic"
FT TRANSMEM 166..190
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..214
FT /note="Extracellular"
FT TRANSMEM 215..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..278
FT /note="Cytoplasmic"
FT TRANSMEM 279..302
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..310
FT /note="Extracellular"
FT TRANSMEM 311..335
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..382
FT /note="Cytoplasmic"
FT REGION 357..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 21..22
FT /note="SV -> RL (in Ref. 2; AAB38966)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="Y -> N (in Ref. 2; AAB38966)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="F -> S (in Ref. 2; AAB38966)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="F -> W (in Ref. 2; AAB38966)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="G -> D (in Ref. 2; AAB38966)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="A -> P (in Ref. 2; AAB38966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 42705 MW; 722B4B40015345FE CRC64;
MHINGPSGPQ AYVNDSLGDG SVFPMGHGYP AEYQHMVHAH WRGFREAPIY YHAGFYIAFI
VLMLSSIFGN GLVIWIFSTS KSLRTPSNLL ILNLAIFDLF MCTNMPHYLI NATVGYIVGG
DLGCDIYALN GGISGMGASI TNAFIAFDRY KTISNPIDGR LSYGQIVLLI LFTWLWATPF
SVLPLFQIWG RYQPEGFLTT CSFDYLTNTD ENRLFVRTIF VWSYVIPMTM ILVSYYKLFT
HVRVHEKMLA EQAKKMNVKS LSANANADNM SVELRIAKAA LIIYMLFILA WTPYSVVALI
GCFGEQQLIT PFVSMLPCLA CKSVSCLDPW VYATSHPKYR LELERRLPWL GIREKHATSG
TSGGQESVAS VSGDTLALSV QN