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Protein

Rhodopsin

Gene

rho

Organism
Scyliorhinus canicula (Small-spotted catshark) (Squalus canicula)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Visual pigments such as rhodopsin and porphyropsin are light-absorbing molecules that mediate vision. Rhodopsin consists of an apoprotein, opsin, covalently linked to 11-cis-retinal. This receptor is coupled to the activation of phospholipase C. Porphyropsin consists of opsin covalently linked to 11-cis 3,4-didehydroretinal.

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

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin
Gene namesi
Name:rho
OrganismiScyliorhinus canicula (Small-spotted catshark) (Squalus canicula)
Taxonomic identifieri7830 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiGaleomorphiiGaleoideaCarcharhiniformesScyliorhinidaeScyliorhinus

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 36ExtracellularAdd BLAST36
Transmembranei37 – 61Helical; Name=1Sequence analysisAdd BLAST25
Topological domaini62 – 73CytoplasmicAdd BLAST12
Transmembranei74 – 98Helical; Name=2Sequence analysisAdd BLAST25
Topological domaini99 – 113ExtracellularAdd BLAST15
Transmembranei114 – 133Helical; Name=3Sequence analysisAdd BLAST20
Topological domaini134 – 152CytoplasmicAdd BLAST19
Transmembranei153 – 176Helical; Name=4Sequence analysisAdd BLAST24
Topological domaini177 – 202ExtracellularAdd BLAST26
Transmembranei203 – 230Helical; Name=5Sequence analysisAdd BLAST28
Topological domaini231 – 252CytoplasmicAdd BLAST22
Transmembranei253 – 276Helical; Name=6Sequence analysisAdd BLAST24
Topological domaini277 – 284Extracellular8
Transmembranei285 – 309Helical; Name=7Sequence analysisAdd BLAST25
Topological domaini310 – 354CytoplasmicAdd BLAST45

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001977181 – 354RhodopsinAdd BLAST354

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi2N-linked (GlcNAc...)Sequence analysis1
Glycosylationi15N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi110 ↔ 187PROSITE-ProRule annotation
Glycosylationi200N-linked (GlcNAc...)Sequence analysis1
Modified residuei296N6-(retinylidene)lysineBy similarity1
Lipidationi322S-palmitoyl cysteineBy similarity1

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, Lipoprotein, Palmitate, Phosphoprotein

Expressioni

Tissue specificityi

Rod shaped photoreceptor cells which mediates vision in dim light.

Structurei

3D structure databases

ProteinModelPortaliO93459.
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

HOVERGENiHBG107442.

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.
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.

O93459-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGTEGENFY IPMSNKTGVV RSPFDYPQYY LAEPWKFSVL AAYMFFLIIA
60 70 80 90 100
GFPVNFLTLY VTIQHKKLRQ PLNYILLNLA VADLFMIFGG FPSTMITSMN
110 120 130 140 150
GYFVFGPSGC NFEGFFATLG GEIGLWSLVV LAIERYVVVC KPMSNFRFGS
160 170 180 190 200
QHAFMGVGLT WIMAMACAFP PLVGWSRYIP EGMQCSCGID YYTLKPEVNN
210 220 230 240 250
ESFVIYMFVV HFSIPLTIIF FCYGRLVCTV KEAAAQQQES ETTQRAEREV
260 270 280 290 300
TRMVIIMVIA FLICWLPYAS VAFFIFCNQG SEFGPIFMTI PAFFAKAASL
310 320 330 340 350
YNPLIYILMN KQFRNCMITT ICCGKNPFEE EESTSASASK TEASSVSSSQ

VAPA
Length:354
Mass (Da):39,761
Last modified:November 1, 1998 - v1
Checksum:iC2AE5F63CED4AC70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17585 mRNA. Translation: CAA76797.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17585 mRNA. Translation: CAA76797.1.

3D structure databases

ProteinModelPortaliO93459.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

GPCRDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG107442.

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.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiOPSD_SCYCA
AccessioniPrimary (citable) accession number: O93459
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: October 5, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. 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.