LipidDB ID

LipidDB-9913-01015

Entry Name

UniProt Accession

P02699;

Theoretical PI

5.87

Molecular Weight

39007.7

Genbank Protein ID

AAA30674.1; AAA30674.1; AAA30674.1; AAA30674.1; AAA30674.1; AAA30675.1;

Genbank Nucleotide ID

K00506; K00502; K00503; K00504; K00505; M21606;

Protein Name

Rhodopsin

Protein Synonyms/Alias

Gene Name

RHO

Gene Synonyms/Alias

Created Date

21-JUL-1986

Organism

Bos taurus (Bovine)

NCBI Taxa ID

9913

Reference

[1] Mielke T, Alexiev U, Gläsel M, Otto H, Heyn MP. Light-induced changes in thestructure and accessibility of the cytoplasmic loops of rhodopsin in theactivated MII state. Biochemistry. 2002 Jun 25;41(25):7875-84.[PMID:12069576]
[2] Papac DI, Thornburg KR, Büllesbach EE, Crouch RK, Knapp DR. Palmitylation of aG-protein coupled receptor. Direct analysis by tandem mass spectrometry. J BiolChem. 1992 Aug 25;267(24):16889-94.[PMID:1512231]

Functional Description

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).

Sequence Annotation

Topological domain: 1 36 Extracellular.
Transmembrane: 37 63 Helical; Name=1.
Topological domain: 64 73 Cytoplasmic.
Transmembrane: 74 96 Helical; Name=2.
Topological domain: 97 110 Extracellular.
Transmembrane: 111 133 Helical; Name=3.
Topological domain: 134 152 Cytoplasmic.
Transmembrane: 153 173 Helical; Name=4.
Topological domain: 174 202 Extracellular.
Transmembrane: 203 224 Helical; Name=5.
Topological domain: 225 249 Cytoplasmic.
Transmembrane: 250 274 Helical; Name=6.
Topological domain: 275 286 Extracellular.
Transmembrane: 287 308 Helical; Name=7.
Topological domain: 309 348 Cytoplasmic.
Region: 113 125 Retinal chromophore binding.
Region: 207 212 Retinal chromophore binding.
Motif: 134 137 'Ionic lock' involved in activated formstabilization.
Metal binding site: 201 201 Zinc.
Metal binding site: 279 279 Zinc.
Binding site: 265 265 Retinal chromophore.
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 296 296 N6-(retinylidene)lysine.
Modified residue: 334 334 Phosphoserine.
Modified residue: 335 335 Phosphothreonine.
Modified residue: 336 336 Phosphothreonine.
Modified residue: 338 338 Phosphoserine.
Modified residue: 340 340 Phosphothreonine.
Modified residue: 342 342 Phosphothreonine.
Modified residue: 343 343 Phosphoserine; by RK and GRK7.

Protein Length

348 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005911; C:cell-cell junction; IEA:Ensembl
GO:0005794; C:Golgi apparatus; IEA:Ensembl
GO:0005887; C:integral component of plasma membrane; IDA:AgBase
GO:0097381; C:photoreceptor disc membrane; TAS:Reactome
GO:0060342; C:photoreceptor inner segment membrane; ISS:UniProtKB
GO:0042622; C:photoreceptor outer segment membrane; ISS:UniProtKB
GO:0005886; C:plasma membrane; ISS:UniProtKB
GO:0008020; F:G-protein coupled photoreceptor activity; IDA:AgBase
GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0071482; P:cellular response to light stimulus; IEA:Ensembl
GO:0007603; P:phototransduction, visible light; IDA:AgBase
GO:0043547; P:positive regulation of GTPase activity; TAS:GOC
GO:0006468; P:protein phosphorylation; IEA:Ensembl
GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW
GO:0060041; P:retina development in camera-type eye; IEA:Ensembl
GO:0007601; P:visual perception; IEA:UniProtKB-KW

Interpro

InterPro; IPR000276; GPCR_Rhodpsn
InterPro; IPR017452; GPCR_Rhodpsn_7TM
InterPro; IPR001760; Opsin
InterPro; IPR027430; Retinal_BS
InterPro; IPR000732; Rhodopsin
InterPro; IPR019477; Rhodopsin_N

Pfam

Pfam; PF00001; 7tm_1;
Pfam; PF10413; Rhodopsin_N;

SMART

PROSITE

PROSITE; PS00237; G_PROTEIN_RECEP_F1_1;
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2;
PROSITE; PS00238; OPSIN;

PRINTS

PRINTS; PR00237; GPCRRHODOPSN;
PRINTS; PR00238; OPSIN;
PRINTS; PR00579; RHODOPSIN;