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Protein

Rhodopsin

Gene

RHO

Organism
Todarodes pacificus (Japanese flying squid) (Ommastrephes pacificus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Photoreceptor required for image-forming vision at low light intensity (Probable). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Signaling mediates the activation of phospholipase C (Probable). Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity).By similarityCurated

GO - Molecular functioni

  • G-protein coupled receptor activity Source: UniProtKB-KW
  • photoreceptor activity Source: UniProtKB-KW
  • retinal binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionG-protein coupled receptor, Photoreceptor protein, Receptor, Retinal protein, Transducer
Biological processSensory transduction, Vision
LigandChromophore

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin
Gene namesi
Name:RHO
OrganismiTodarodes pacificus (Japanese flying squid) (Ommastrephes pacificus)
Taxonomic identifieri6637 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaCephalopodaColeoideaNeocoleoideaDecapodiformesTeuthidaOegopsinaOmmastrephidaeTodarodes

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 33Extracellular4 PublicationsAdd BLAST32
Transmembranei34 – 58Helical; Name=14 PublicationsAdd BLAST25
Topological domaini59 – 70Cytoplasmic4 PublicationsAdd BLAST12
Transmembranei71 – 97Helical; Name=24 PublicationsAdd BLAST27
Topological domaini98 – 109Extracellular4 PublicationsAdd BLAST12
Transmembranei110 – 131Helical; Name=34 PublicationsAdd BLAST22
Topological domaini132 – 151Cytoplasmic4 PublicationsAdd BLAST20
Transmembranei152 – 172Helical; Name=44 PublicationsAdd BLAST21
Topological domaini173 – 199Extracellular4 PublicationsAdd BLAST27
Transmembranei200 – 224Helical; Name=54 PublicationsAdd BLAST25
Topological domaini225 – 261Cytoplasmic4 PublicationsAdd BLAST37
Transmembranei262 – 283Helical; Name=64 PublicationsAdd BLAST22
Topological domaini284 – 293Extracellular4 Publications10
Transmembranei294 – 315Helical; Name=74 PublicationsAdd BLAST22
Topological domaini316 – 448Cytoplasmic4 PublicationsAdd BLAST133

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001977482 – 448RhodopsinAdd BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi8N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi108 ↔ 186PROSITE-ProRule annotationCombined sources4 Publications
Modified residuei305N6-(retinylidene)lysineCombined sources5 Publications1
Lipidationi336S-palmitoyl cysteineCombined sources1 Publication1
Lipidationi337S-palmitoyl cysteineCombined sources2 Publications1

Post-translational modificationi

Contains one covalently linked retinal chromophore. Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal (PubMed:3191148, PubMed:17554166, PubMed:18463093, PubMed:18480818, PubMed:21906602). After hydrolysis of the Schiff base and release of the covalently bound all-trans-retinal, active rhodopsin is regenerated by binding of a fresh molecule of 11-cis-retinal (By similarity).By similarity5 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

PTM databases

GlyConnecti524
UniCarbKBiP31356

Expressioni

Tissue specificityi

Retina, rhabdomere membrane (at protein level).3 Publications

Interactioni

Protein-protein interaction databases

DIPiDIP-60624N

Structurei

Secondary structure

1448
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 17Combined sources3
Helixi21 – 24Combined sources4
Helixi31 – 61Combined sources31
Helixi63 – 65Combined sources3
Helixi70 – 87Combined sources18
Helixi91 – 97Combined sources7
Helixi104 – 136Combined sources33
Turni141 – 143Combined sources3
Helixi149 – 167Combined sources19
Helixi169 – 172Combined sources4
Beta strandi177 – 179Combined sources3
Beta strandi183 – 188Combined sources6
Helixi195 – 207Combined sources13
Helixi210 – 224Combined sources15
Helixi227 – 238Combined sources12
Turni239 – 241Combined sources3
Helixi246 – 286Combined sources41
Helixi289 – 291Combined sources3
Helixi294 – 306Combined sources13
Helixi307 – 309Combined sources3
Helixi311 – 318Combined sources8
Helixi320 – 329Combined sources10
Helixi331 – 334Combined sources4
Helixi341 – 344Combined sources4
Helixi345 – 351Combined sources7
Helixi355 – 357Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z73X-ray2.50A/B1-448[»]
2ZIYX-ray3.70A2-373[»]
3AYMX-ray2.80A/B1-448[»]
3AYNX-ray2.70A/B1-448[»]
4WW3X-ray2.80A/B9-358[»]
ProteinModelPortaliP31356
SMRiP31356
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31356

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi371 – 381Met-richAdd BLAST11
Compositional biasi382 – 448Gln/Pro-richAdd BLAST67

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

InterProiView protein in InterPro
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
IPR001760 Opsin
IPR027430 Retinal_BS
IPR006031 XYPPX
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PF02162 XYPPX, 5 hits
PRINTSiPR00237 GPCRRHODOPSN
PR00238 OPSIN
SMARTiView protein in SMART
SM01381 7TM_GPCR_Srsx, 1 hit
PROSITEiView protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit
PS00238 OPSIN, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31356-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRDLRDNET WWYNPSIVVH PHWREFDQVP DAVYYSLGIF IGICGIIGCG
60 70 80 90 100
GNGIVIYLFT KTKSLQTPAN MFIINLAFSD FTFSLVNGFP LMTISCFLKK
110 120 130 140 150
WIFGFAACKV YGFIGGIFGF MSIMTMAMIS IDRYNVIGRP MAASKKMSHR
160 170 180 190 200
RAFIMIIFVW LWSVLWAIGP IFGWGAYTLE GVLCNCSFDY ISRDSTTRSN
210 220 230 240 250
ILCMFILGFF GPILIIFFCY FNIVMSVSNH EKEMAAMAKR LNAKELRKAQ
260 270 280 290 300
AGANAEMRLA KISIVIVSQF LLSWSPYAVV ALLAQFGPLE WVTPYAAQLP
310 320 330 340 350
VMFAKASAIH NPMIYSVSHP KFREAISQTF PWVLTCCQFD DKETEDDKDA
360 370 380 390 400
ETEIPAGESS DAAPSADAAQ MKEMMAMMQK MQQQQAAYPP QGYAPPPQGY
410 420 430 440
PPQGYPPQGY PPQGYPPQGY PPPPQGAPPQ GAPPAAPPQG VDNQAYQA
Length:448
Mass (Da):49,836
Last modified:January 23, 2007 - v2
Checksum:iB48D56A1D057492A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70498 mRNA Translation: CAA49906.1
PIRiS29483

Similar proteinsi

Entry informationi

Entry nameiOPSD_TODPA
AccessioniPrimary (citable) accession number: P31356
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 92 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
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Main funding by: National Institutes of Health