OPS1_DROPS
ID OPS1_DROPS Reviewed; 373 AA.
AC P28678; Q294T3; Q56RD3; Q8I154; Q8STC6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 4.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Opsin Rh1;
DE AltName: Full=Outer R1-R6 photoreceptor cells opsin;
GN Name=ninaE; Synonyms=Rh1; ORFNames=GA18249;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Apple Hill;
RX PubMed=1398053; DOI=10.1093/genetics/132.1.193;
RA Carulli J.P., Hartl D.L.;
RT "Variable rates of evolution among Drosophila opsin genes.";
RL Genetics 132:193-204(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tucson 14011-0121.4;
RX PubMed=12537575; DOI=10.1186/gb-2002-3-12-research0086;
RA Bergman C.M., Pfeiffer B.D., Rincon-Limas D.E., Hoskins R.A., Gnirke A.,
RA Mungall C.J., Wang A.M., Kronmiller B., Pacleb J.M., Park S., Stapleton M.,
RA Wan K.H., George R.A., de Jong P.J., Botas J., Rubin G.M., Celniker S.E.;
RT "Assessing the impact of comparative genomic sequence data on the
RT functional annotation of the Drosophila genome.";
RL Genome Biol. 3:RESEARCH0086.1-RESEARCH0086.20(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15545653; DOI=10.1534/genetics.104.033068;
RA Bartolome C., Maside X., Yi S., Grant A.L., Charlesworth B.;
RT "Patterns of selection on synonymous and nonsynonymous variants in
RT Drosophila miranda.";
RL Genetics 169:1495-1507(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-341.
RC STRAIN=Abajo36, AF2, AFC12, AFC3, AFC7, Flagstaff14, Flagstaff16,
RC Flagstaff18, Flagstaff5, Mather10, Mather17, Mather32, Mather48, Mather52,
RC MSH10, MSH21, and MSH32;
RX PubMed=11919289; DOI=10.1093/oxfordjournals.molbev.a004103;
RA Machado C.A., Kliman R.M., Markert J.A., Hey J.;
RT "Inferring the history of speciation from multilocus DNA sequence data: the
RT case of Drosophila pseudoobscura and close relatives.";
RL Mol. Biol. Evol. 19:472-488(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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=480 nm;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region.
CC -!- MISCELLANEOUS: Each Drosophila eye is composed of 800 facets or
CC ommatidia. Each ommatidium contains 8 photoreceptor cells (R1-R8), the
CC R1 to R6 cells are outer cells, while R7 and R8 are inner cells.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X65877; CAA46708.1; -; Genomic_DNA.
DR EMBL; AY190960; AAO01119.1; -; Genomic_DNA.
DR EMBL; AY754574; AAX13149.1; -; Genomic_DNA.
DR EMBL; CM000070; EAL28881.2; -; Genomic_DNA.
DR EMBL; AF450965; AAM09428.1; -; Genomic_DNA.
DR EMBL; AF450966; AAM09429.1; -; Genomic_DNA.
DR EMBL; AF450967; AAM09430.1; -; Genomic_DNA.
DR EMBL; AF450968; AAM09431.1; -; Genomic_DNA.
DR EMBL; AF450969; AAM09432.1; -; Genomic_DNA.
DR EMBL; AF450970; AAM09433.1; -; Genomic_DNA.
DR EMBL; AF450971; AAM09434.1; -; Genomic_DNA.
DR EMBL; AF450972; AAM09435.1; -; Genomic_DNA.
DR EMBL; AF450973; AAM09436.1; -; Genomic_DNA.
DR EMBL; AF450974; AAM09437.1; -; Genomic_DNA.
DR EMBL; AF450975; AAM09438.1; -; Genomic_DNA.
DR EMBL; AF450976; AAM09439.1; -; Genomic_DNA.
DR EMBL; AF450977; AAM09440.1; -; Genomic_DNA.
DR EMBL; AF450978; AAM09441.1; -; Genomic_DNA.
DR EMBL; AF450979; AAM09442.1; -; Genomic_DNA.
DR EMBL; AF450980; AAM09443.1; -; Genomic_DNA.
DR EMBL; AF450981; AAM09444.1; -; Genomic_DNA.
DR PIR; S40691; S40691.
DR RefSeq; XP_001359729.2; XM_001359692.3.
DR AlphaFoldDB; P28678; -.
DR SMR; P28678; -.
DR DIP; DIP-769N; -.
DR STRING; 7237.FBpp0284713; -.
DR EnsemblMetazoa; FBtr0286275; FBpp0284713; FBgn0012733.
DR GeneID; 4802902; -.
DR KEGG; dpo:Dpse_GA18249; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; P28678; -.
DR OMA; AHYIIGC; -.
DR ChiTaRS; ninaE; fly.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0012733; Expressed in insect adult head and 2 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IEA:UniProt.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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 Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00576; OPSINRH1RH2.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 1: Evidence at protein 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..373
FT /note="Opsin Rh1"
FT /id="PRO_0000197623"
FT TOPO_DOM 1..54
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..331
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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"
FT MOD_RES 319
FT /note="N6-(retinylidene)lysine"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 123..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 1..2
FT /note="MD -> CC (in Ref. 3; AAX13149)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="H -> Q (in Ref. 1; CAA46708)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="L -> P (in Ref. 1; CAA46708)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="N -> D (in Ref. 1; CAA46708)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="S -> T (in Ref. 1; CAA46708)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="C -> CC (in Ref. 1; CAA46708)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="N -> T (in Ref. 1; CAA46708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 41524 MW; 80E580372EC4EABB CRC64;
MDSFAAVATQ LGPHFAALSN GSVVDKVTPD MAHLISPYWN QFPAMDPIWA KILTAYMIII
GMISWCGNGV VIYIFATTKS LRTPANLLVI NLAISDFGIM ITNTPMMGIN LYFETWVLGP
MMCDIYAGLG SAFGCSSIWS MCMISLDRYQ VIVKGMAGRP MTIPLALGKI AYIWFMSSIW
CLAPVFGWSR YVPEGNLTSC GIDYLERDWN PRSYLIFYSI FVYYIPLFLI CYSYWFIIAA
VSAHEKAMRE QAKKMNVKSL RSSEDADKSA EGKLAKVALV TISLWFMAWT PYLVINCMGL
FKFEGLTPLN TIWGACFAKS AACYNPIVYG ISHPKYRLAL KEKCPCCVFG KVDDGKSSEA
QSQATNSEAE SKA