OPS1_DROME
ID OPS1_DROME Reviewed; 373 AA.
AC P06002; A0AVV9; Q4QPQ2; Q9TX56; Q9VDS8;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Opsin Rh1;
DE AltName: Full=Neither inactivation nor afterpotential E protein;
DE AltName: Full=Outer R1-R6 photoreceptor cells opsin;
GN Name=ninaE; Synonyms=Rh1; ORFNames=CG4550;
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].
RX PubMed=2985266; DOI=10.1016/0092-8674(85)90343-5;
RA O'Tousa J.E., Baehr W., Martin R.L., Hirsh J., Pak W.L., Applebury M.L.;
RT "The Drosophila ninaE gene encodes an opsin.";
RL Cell 40:839-850(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2580638; DOI=10.1016/0092-8674(85)90344-7;
RA Zuker C.S., Cowman A.F., Rubin G.M.;
RT "Isolation and structure of a rhodopsin gene from D. melanogaster.";
RL Cell 40:851-858(1985).
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;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kapadia B., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE OF 26-346.
RX PubMed=8006992; DOI=10.1007/bf00176087;
RA Carulli J.P., Chen D.M., Stark W.S., Hartl D.L.;
RT "Phylogeny and physiology of Drosophila opsins.";
RL J. Mol. Evol. 38:250-262(1994).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=23226104; DOI=10.1371/journal.pbio.1001438;
RA Xiong B., Bayat V., Jaiswal M., Zhang K., Sandoval H., Charng W.L., Li T.,
RA David G., Duraine L., Lin Y.Q., Neely G.G., Yamamoto S., Bellen H.J.;
RT "Crag is a GEF for Rab11 required for rhodopsin trafficking and maintenance
RT of adult photoreceptor cells.";
RL PLoS Biol. 10:E1001438-E1001438(2012).
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. Cell
CC projection, cilium, photoreceptor outer segment
CC {ECO:0000269|PubMed:23226104}. Note=Upon white light stimulation, is
CC internalized into the rhabdomere membranes.
CC {ECO:0000269|PubMed:23226104}.
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}.
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DR EMBL; K02315; AAA28733.1; -; Genomic_DNA.
DR EMBL; K02320; AAA28735.1; ALT_SEQ; Genomic_DNA.
DR EMBL; K02316; AAA28735.1; JOINED; Genomic_DNA.
DR EMBL; K02317; AAA28735.1; JOINED; Genomic_DNA.
DR EMBL; K02318; AAA28735.1; JOINED; Genomic_DNA.
DR EMBL; K02319; AAA28735.1; JOINED; Genomic_DNA.
DR EMBL; AE014297; AAF55712.1; -; Genomic_DNA.
DR EMBL; BT010221; AAQ23539.1; -; mRNA.
DR EMBL; BT023714; AAY85114.1; -; mRNA.
DR EMBL; BT029277; ABK30914.1; -; mRNA.
DR PIR; A90864; OOFF.
DR RefSeq; NP_524407.1; NM_079683.3.
DR AlphaFoldDB; P06002; -.
DR SMR; P06002; -.
DR BioGRID; 67356; 77.
DR DIP; DIP-17500N; -.
DR IntAct; P06002; 5.
DR MINT; P06002; -.
DR STRING; 7227.FBpp0083266; -.
DR GlyGen; P06002; 2 sites.
DR iPTMnet; P06002; -.
DR PaxDb; P06002; -.
DR PRIDE; P06002; -.
DR EnsemblMetazoa; FBtr0083857; FBpp0083266; FBgn0002940.
DR GeneID; 42367; -.
DR KEGG; dme:Dmel_CG4550; -.
DR CTD; 42367; -.
DR FlyBase; FBgn0002940; ninaE.
DR VEuPathDB; VectorBase:FBgn0002940; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234631; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; P06002; -.
DR OMA; AHYIIGC; -.
DR OrthoDB; 911005at2759; -.
DR PhylomeDB; P06002; -.
DR SignaLink; P06002; -.
DR BioGRID-ORCS; 42367; 0 hits in 3 CRISPR screens.
DR ChiTaRS; ninaE; fly.
DR GenomeRNAi; 42367; -.
DR PRO; PR:P06002; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002940; Expressed in head capsule and 18 other tissues.
DR Genevisible; P06002; DM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
DR GO; GO:0005769; C:early endosome; IDA:FlyBase.
DR GO; GO:0016027; C:inaD signaling complex; IPI:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0016029; C:subrhabdomeral cisterna; IDA:FlyBase.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IMP:FlyBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0071482; P:cellular response to light stimulus; IMP:FlyBase.
DR GO; GO:0009589; P:detection of UV; IMP:FlyBase.
DR GO; GO:0009584; P:detection of visible light; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0046673; P:negative regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:0071632; P:optomotor response; IMP:FlyBase.
DR GO; GO:0030265; P:phospholipase C-activating rhodopsin mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:FlyBase.
DR GO; GO:0042331; P:phototaxis; IMP:FlyBase.
DR GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR GO; GO:0009642; P:response to light intensity; IMP:FlyBase.
DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR GO; GO:0043052; P:thermotaxis; IMP:FlyBase.
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 Cell projection; Chromophore; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; 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_0000197622"
FT TOPO_DOM 1..49
FT /note="Extracellular"
FT TRANSMEM 50..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..86
FT /note="Cytoplasmic"
FT TRANSMEM 87..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..126
FT /note="Extracellular"
FT TRANSMEM 127..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..165
FT /note="Cytoplasmic"
FT TRANSMEM 166..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..213
FT /note="Extracellular"
FT TRANSMEM 214..241
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..276
FT /note="Cytoplasmic"
FT TRANSMEM 277..300
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..307
FT /note="Extracellular"
FT TRANSMEM 308..332
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..373
FT /note="Cytoplasmic"
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:0000305"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT DISULFID 123..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 373 AA; 41495 MW; FFF36C90DDD68294 CRC64;
MESFAVAAAQ LGPHFAPLSN GSVVDKVTPD MAHLISPYWN QFPAMDPIWA KILTAYMIMI
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
