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Protein

Opsin Rh2

Gene

Rh2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.

Absorptioni

Abs(max)=420 nm1 Publication

GO - Molecular functioni

  • G-protein coupled photoreceptor activity Source: FlyBase

GO - Biological processi

  • G-protein coupled receptor signaling pathway Source: FlyBase
  • phototransduction Source: FlyBase
  • protein-chromophore linkage Source: UniProtKB-KW
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Photoreceptor protein, Receptor, Retinal protein, Transducer

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Chromophore

Enzyme and pathway databases

ReactomeiR-DME-2187335. The retinoid cycle in cones (daylight vision).
R-DME-2453902. The canonical retinoid cycle in rods (twilight vision).
R-DME-2485179. Activation of the phototransduction cascade.
R-DME-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-DME-419771. Opsins.
R-DME-5620916. VxPx cargo-targeting to cilium.

Names & Taxonomyi

Protein namesi
Recommended name:
Opsin Rh2
Alternative name(s):
Ocellar opsin
Gene namesi
Name:Rh2
ORF Names:CG16740
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003248. Rh2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5656ExtracellularAdd
BLAST
Transmembranei57 – 8125Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini82 – 9312CytoplasmicAdd
BLAST
Transmembranei94 – 11926Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini120 – 13314ExtracellularAdd
BLAST
Transmembranei134 – 15320Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini154 – 17219CytoplasmicAdd
BLAST
Transmembranei173 – 19624Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini197 – 22024ExtracellularAdd
BLAST
Transmembranei221 – 24828Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini249 – 28335CytoplasmicAdd
BLAST
Transmembranei284 – 30724Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini308 – 3147Extracellular
Transmembranei315 – 33925Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini340 – 38142CytoplasmicAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Opsin Rh2PRO_0000197625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi27 – 271N-linked (GlcNAc...)Curated
Disulfide bondi130 ↔ 207PROSITE-ProRule annotation
Modified residuei326 – 3261N6-(retinylidene)lysine

Post-translational modificationi

Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP08099.
PRIDEiP08099.

Expressioni

Tissue specificityi

Predominant opsin expressed in the dorsal ocelli.

Gene expression databases

BgeeiP08099.
ExpressionAtlasiP08099. differential.
GenevisibleiP08099. DM.

Interactioni

Protein-protein interaction databases

BioGridi67266. 3 interactions.
DIPiDIP-22447N.
IntActiP08099. 1 interaction.
MINTiMINT-844888.
STRINGi7227.FBpp0083111.

Structurei

3D structure databases

ProteinModelPortaliP08099.
SMRiP08099. Positions 41-381.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
InParanoidiP08099.
KOiK04255.
OMAiPRFQAQS.
OrthoDBiEOG790G0Q.
PhylomeDBiP08099.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR001735. Opsin_RH1/RH2.
IPR027430. Retinal_BS.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00576. OPSINRH1RH2.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERSHLPETP FDLAHSGPRF QAQSSGNGSV LDNVLPDMAH LVNPYWSRFA
60 70 80 90 100
PMDPMMSKIL GLFTLAIMII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA
110 120 130 140 150
FSDFCMMASQ SPVMIINFYY ETWVLGPLWC DIYAGCGSLF GCVSIWSMCM
160 170 180 190 200
IAFDRYNVIV KGINGTPMTI KTSIMKILFI WMMAVFWTVM PLIGWSAYVP
210 220 230 240 250
EGNLTACSID YMTRMWNPRS YLITYSLFVY YTPLFLICYS YWFIIAAVAA
260 270 280 290 300
HEKAMREQAK KMNVKSLRSS EDCDKSAEGK LAKVALTTIS LWFMAWTPYL
310 320 330 340 350
VICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRIVLKEK
360 370 380
CPMCVFGNTD EPKPDAPASD TETTSEADSK A
Length:381
Mass (Da):42,722
Last modified:August 1, 1988 - v1
Checksum:i628322D228396F9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12896 Genomic DNA. Translation: AAA28734.1.
AE014297 Genomic DNA. Translation: AAF55601.1.
PIRiA24058. OOFF2.
RefSeqiNP_524398.1. NM_079674.3.
UniGeneiDm.2404.

Genome annotation databases

EnsemblMetazoaiFBtr0083697; FBpp0083111; FBgn0003248.
GeneIDi42261.
KEGGidme:Dmel_CG16740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12896 Genomic DNA. Translation: AAA28734.1.
AE014297 Genomic DNA. Translation: AAF55601.1.
PIRiA24058. OOFF2.
RefSeqiNP_524398.1. NM_079674.3.
UniGeneiDm.2404.

3D structure databases

ProteinModelPortaliP08099.
SMRiP08099. Positions 41-381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67266. 3 interactions.
DIPiDIP-22447N.
IntActiP08099. 1 interaction.
MINTiMINT-844888.
STRINGi7227.FBpp0083111.

Protein family/group databases

GPCRDBiSearch...

Proteomic databases

PaxDbiP08099.
PRIDEiP08099.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0083697; FBpp0083111; FBgn0003248.
GeneIDi42261.
KEGGidme:Dmel_CG16740.

Organism-specific databases

CTDi42261.
FlyBaseiFBgn0003248. Rh2.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
InParanoidiP08099.
KOiK04255.
OMAiPRFQAQS.
OrthoDBiEOG790G0Q.
PhylomeDBiP08099.

Enzyme and pathway databases

ReactomeiR-DME-2187335. The retinoid cycle in cones (daylight vision).
R-DME-2453902. The canonical retinoid cycle in rods (twilight vision).
R-DME-2485179. Activation of the phototransduction cascade.
R-DME-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-DME-419771. Opsins.
R-DME-5620916. VxPx cargo-targeting to cilium.

Miscellaneous databases

ChiTaRSiRh2. fly.
GenomeRNAii42261.
PROiP08099.

Gene expression databases

BgeeiP08099.
ExpressionAtlasiP08099. differential.
GenevisibleiP08099. DM.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR001735. Opsin_RH1/RH2.
IPR027430. Retinal_BS.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00576. OPSINRH1RH2.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An opsin gene expressed in only one photoreceptor cell type of the Drosophila eye."
    Cowman A.F., Zuker C.S., Rubin G.M.
    Cell 44:705-710(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "Targeted misexpression of a Drosophila opsin gene leads to altered visual function."
    Feiler R., Harris W.A., Kirschfeld K., Wehrhahn C., Zuker C.S.
    Nature 333:737-741(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: LOCALIZATION OF OPSIN RH2, BIOPHYSICOCHEMICAL PROPERTIES.
  5. "Transcript localization of four opsin genes in the three visual organs of Drosophila; RH2 is ocellus specific."
    Pollock J.A., Benzer S.
    Nature 333:779-782(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: LOCALIZATION OF OPSIN RH2.

Entry informationi

Entry nameiOPS2_DROME
AccessioniPrimary (citable) accession number: P08099
Secondary accession number(s): Q9VE29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 6, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.