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Protein

Opsin Rh1

Gene

ninaE

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 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)=480 nm

GO - Molecular functioni

  • G-protein coupled photoreceptor activity Source: FlyBase
  • G-protein coupled receptor activity Source: FlyBase

GO - Biological processi

  • adult locomotory behavior Source: FlyBase
  • detection of UV Source: FlyBase
  • detection of visible light Source: FlyBase
  • G-protein coupled receptor signaling pathway Source: FlyBase
  • negative regulation of compound eye retinal cell programmed cell death Source: FlyBase
  • optomotor response Source: FlyBase
  • phospholipase C-activating rhodopsin mediated signaling pathway Source: FlyBase
  • photoreceptor cell morphogenesis Source: FlyBase
  • phototaxis Source: FlyBase
  • phototransduction Source: FlyBase
  • protein-chromophore linkage Source: UniProtKB-KW
  • response to light intensity Source: FlyBase
  • rhabdomere development Source: FlyBase
  • sensory perception of pain Source: FlyBase
  • thermotaxis Source: FlyBase
  • 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 Rh1
Alternative name(s):
Neither inactivation nor afterpotential E protein
Outer R1-R6 photoreceptor cells opsin
Gene namesi
Name:ninaE
Synonyms:Rh1
ORF Names:CG4550
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0002940. ninaE.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4949ExtracellularAdd
BLAST
Transmembranei50 – 7425Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini75 – 8612CytoplasmicAdd
BLAST
Transmembranei87 – 11226Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini113 – 12614ExtracellularAdd
BLAST
Transmembranei127 – 14620Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini147 – 16519CytoplasmicAdd
BLAST
Transmembranei166 – 18924Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini190 – 21324ExtracellularAdd
BLAST
Transmembranei214 – 24128Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini242 – 27635CytoplasmicAdd
BLAST
Transmembranei277 – 30024Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini301 – 3077Extracellular
Transmembranei308 – 33225Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini333 – 37341CytoplasmicAdd
BLAST

GO - Cellular componenti

  • cytoplasmic, membrane-bounded vesicle Source: FlyBase
  • inaD signaling complex Source: FlyBase
  • integral component of membrane Source: FlyBase
  • multivesicular body Source: FlyBase
  • plasma membrane Source: FlyBase
  • rhabdomere Source: FlyBase
  • rough endoplasmic reticulum Source: FlyBase
  • secondary lysosome Source: FlyBase
  • subrhabdomeral cisterna Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 373373Opsin Rh1PRO_0000197622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi20 – 201N-linked (GlcNAc...)Curated
Disulfide bondi123 ↔ 200PROSITE-ProRule annotation
Glycosylationi196 – 1961N-linked (GlcNAc...)1 Publication
Modified residuei319 – 3191N6-(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

PaxDbiP06002.
PRIDEiP06002.

Expressioni

Gene expression databases

BgeeiP06002.
GenevisibleiP06002. DM.

Interactioni

Protein-protein interaction databases

BioGridi67356. 27 interactions.
DIPiDIP-17500N.
IntActiP06002. 2 interactions.
MINTiMINT-326982.
STRINGi7227.FBpp0083266.

Structurei

3D structure databases

ProteinModelPortaliP06002.
SMRiP06002. Positions 12-369.
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.
GeneTreeiENSGT00760000118977.
InParanoidiP06002.
KOiK13802.
OMAiARRTYLI.
OrthoDBiEOG790G0Q.
PhylomeDBiP06002.

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.

P06002-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESFAVAAAQ LGPHFAPLSN GSVVDKVTPD MAHLISPYWN QFPAMDPIWA
60 70 80 90 100
KILTAYMIMI GMISWCGNGV VIYIFATTKS LRTPANLLVI NLAISDFGIM
110 120 130 140 150
ITNTPMMGIN LYFETWVLGP MMCDIYAGLG SAFGCSSIWS MCMISLDRYQ
160 170 180 190 200
VIVKGMAGRP MTIPLALGKI AYIWFMSSIW CLAPAFGWSR YVPEGNLTSC
210 220 230 240 250
GIDYLERDWN PRSYLIFYSI FVYYIPLFLI CYSYWFIIAA VSAHEKAMRE
260 270 280 290 300
QAKKMNVKSL RSSEDAEKSA EGKLAKVALV TITLWFMAWT PYLVINCMGL
310 320 330 340 350
FKFEGLTPLN TIWGACFAKS AACYNPIVYG ISHPKYRLAL KEKCPCCVFG
360 370
KVDDGKSSDA QSQATASEAE SKA
Length:373
Mass (Da):41,495
Last modified:August 13, 1987 - v1
Checksum:iFFF36C90DDD68294
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02315 Genomic DNA. Translation: AAA28733.1.
K02320
, K02316, K02317, K02318, K02319 Genomic DNA. Translation: AAA28735.1. Sequence problems.
AE014297 Genomic DNA. Translation: AAF55712.1.
BT010221 mRNA. Translation: AAQ23539.1.
BT023714 mRNA. Translation: AAY85114.1.
BT029277 mRNA. Translation: ABK30914.1.
PIRiA90864. OOFF.
RefSeqiNP_524407.1. NM_079683.3.
UniGeneiDm.6744.

Genome annotation databases

EnsemblMetazoaiFBtr0083857; FBpp0083266; FBgn0002940.
GeneIDi42367.
KEGGidme:Dmel_CG4550.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02315 Genomic DNA. Translation: AAA28733.1.
K02320
, K02316, K02317, K02318, K02319 Genomic DNA. Translation: AAA28735.1. Sequence problems.
AE014297 Genomic DNA. Translation: AAF55712.1.
BT010221 mRNA. Translation: AAQ23539.1.
BT023714 mRNA. Translation: AAY85114.1.
BT029277 mRNA. Translation: ABK30914.1.
PIRiA90864. OOFF.
RefSeqiNP_524407.1. NM_079683.3.
UniGeneiDm.6744.

3D structure databases

ProteinModelPortaliP06002.
SMRiP06002. Positions 12-369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67356. 27 interactions.
DIPiDIP-17500N.
IntActiP06002. 2 interactions.
MINTiMINT-326982.
STRINGi7227.FBpp0083266.

Protein family/group databases

GPCRDBiSearch...

Proteomic databases

PaxDbiP06002.
PRIDEiP06002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0083857; FBpp0083266; FBgn0002940.
GeneIDi42367.
KEGGidme:Dmel_CG4550.

Organism-specific databases

CTDi42367.
FlyBaseiFBgn0002940. ninaE.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118977.
InParanoidiP06002.
KOiK13802.
OMAiARRTYLI.
OrthoDBiEOG790G0Q.
PhylomeDBiP06002.

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

ChiTaRSininaE. fly.
GenomeRNAii42367.
NextBioi828455.
PROiP06002.

Gene expression databases

BgeeiP06002.
GenevisibleiP06002. 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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Isolation and structure of a rhodopsin gene from D. melanogaster."
    Zuker C.S., Cowman A.F., Rubin G.M.
    Cell 40:851-858(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  6. Cited for: NUCLEOTIDE SEQUENCE OF 26-346.
  7. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
    Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
    Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Oregon-R.
    Tissue: Head.

Entry informationi

Entry nameiOPS1_DROME
AccessioniPrimary (citable) accession number: P06002
Secondary accession number(s): A0AVV9
, Q4QPQ2, Q9TX56, Q9VDS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 11, 2016
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Each Drosophila eye is composed of 800 facets or ommatidia. Each ommatidium contains 8 photoreceptor cells (R1-R8), the R1 to R6 cells are outer cells, while R7 and R8 are inner cells.

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.