Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Rhodopsin

Gene

RHO

Organism
Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi201 – 2011ZincBy similarity
Binding sitei265 – 2651Retinal chromophoreBy similarity
Metal bindingi279 – 2791ZincBy similarity

GO - Molecular functioni

GO - Biological processi

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, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin
Gene namesi
Name:RHO
OrganismiTursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus)
Taxonomic identifieri9739 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaCetaceaOdontocetiDelphinidaeTursiops

Subcellular locationi

  • Membrane; Multi-pass membrane protein

  • Note: Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to the rod outer segment (OS) photosensory cilia.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3636ExtracellularAdd
BLAST
Transmembranei37 – 6125Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini62 – 7312CytoplasmicAdd
BLAST
Transmembranei74 – 9825Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini99 – 11315ExtracellularAdd
BLAST
Transmembranei114 – 13320Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini134 – 15219CytoplasmicAdd
BLAST
Transmembranei153 – 17624Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini177 – 20226ExtracellularAdd
BLAST
Transmembranei203 – 23028Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini231 – 25222CytoplasmicAdd
BLAST
Transmembranei253 – 27624Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini277 – 2848Extracellular
Transmembranei285 – 30925Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini310 – 34839CytoplasmicAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348RhodopsinPRO_0000197726Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Glycosylationi2 – 21N-linked (GlcNAc...)By similarity
Glycosylationi15 – 151N-linked (GlcNAc...)By similarity
Disulfide bondi110 ↔ 187PROSITE-ProRule annotation
Modified residuei296 – 2961N6-(retinylidene)lysineBy similarity
Lipidationi322 – 3221S-palmitoyl cysteineBy similarity
Lipidationi323 – 3231S-palmitoyl cysteineBy similarity
Modified residuei334 – 3341PhosphoserineBy similarity
Modified residuei335 – 3351PhosphothreonineBy similarity
Modified residuei336 – 3361PhosphothreonineBy similarity
Modified residuei338 – 3381PhosphoserineBy similarity
Modified residuei340 – 3401PhosphothreonineBy similarity
Modified residuei342 – 3421PhosphothreonineBy similarity
Modified residuei343 – 3431PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.By similarity
Contains one covalently linked retinal chromophore.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Expressioni

Tissue specificityi

Rod shaped photoreceptor cells which mediates vision in dim light.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9739.ENSTTRP00000010688.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi51 – 6414

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RY1electron microscopy12.00S50-67[»]
2J28electron microscopy8.00750-67[»]
ProteinModelPortaliO62798.
SMRiO62798. Positions 1-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO62798.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni113 – 12513Retinal chromophore bindingBy similarityAdd
BLAST
Regioni207 – 2126Retinal chromophore bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi134 – 1374'Ionic lock' involved in activated form stabilization

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.
HOGENOMiHOG000253932.
HOVERGENiHBG107442.
OrthoDBiEOG72NRQJ.
TreeFamiTF324998.

Family and domain databases

Gene3Di4.10.840.10. 1 hit.
InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR000732. Rhodopsin.
IPR019477. Rhodopsin_N.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
PF10413. Rhodopsin_N. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00579. RHODOPSIN.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
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.

O62798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGTEGLNFY VPFSNKTGVV RSPFEYPQYY LAEPWQFSVL AAYMFLLIVL
60 70 80 90 100
GFPINFLTLY VTVQHKKLRT PLNYILLNLA VANLFMVFGG FTTTLYTSLH
110 120 130 140 150
AYFVFGPTGC NLEGFFATLG GEIALWSLVV LAIERYVVVC KPMSNFRFGE
160 170 180 190 200
NHAIMGLALT WIMAMACAAA PLVGWSRYIP EGMQCSCGID YYTSRQEVNN
210 220 230 240 250
ESFVIYMFVV HFTIPLVIIF FCYGQLVFTV KEAAAQQQES ATTQKAEKEV
260 270 280 290 300
TRMVIIMVVA FLICWVPYAS VAFYIFTHQG SDFGPIFMTI PSFFAKSSSI
310 320 330 340
YNPVIYIMMN KQFRNCMLTT LCCGRNPLGD DEASTTASKT ETSQVAPA
Length:348
Mass (Da):39,093
Last modified:August 1, 1998 - v1
Checksum:i32605DE5ED94723A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055456 mRNA. Translation: AAC12940.1.
RefSeqiNP_001267588.1. NM_001280659.1.

Genome annotation databases

GeneIDi101320374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055456 mRNA. Translation: AAC12940.1.
RefSeqiNP_001267588.1. NM_001280659.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RY1electron microscopy12.00S50-67[»]
2J28electron microscopy8.00750-67[»]
ProteinModelPortaliO62798.
SMRiO62798. Positions 1-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9739.ENSTTRP00000010688.

Protein family/group databases

GPCRDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101320374.

Organism-specific databases

CTDi6010.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
HOGENOMiHOG000253932.
HOVERGENiHBG107442.
OrthoDBiEOG72NRQJ.
TreeFamiTF324998.

Miscellaneous databases

EvolutionaryTraceiO62798.

Family and domain databases

Gene3Di4.10.840.10. 1 hit.
InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR000732. Rhodopsin.
IPR019477. Rhodopsin_N.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
PF10413. Rhodopsin_N. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00579. RHODOPSIN.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Mechanism of spectral tuning in the dolphin visual pigments."
    Fasick J.I., Robsinson P.R.
    Biochemistry 37:433-438(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure of the signal recognition particle interacting with the elongation-arrested ribosome."
    Halic M., Becker T., Pool M.R., Spahn C.M.T., Grassucci R.A., Frank J., Beckmann R.
    Nature 427:808-814(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF 50-67.

Entry informationi

Entry nameiOPSD_TURTR
AccessioniPrimary (citable) accession number: O62798
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.