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Protein

Rhodopsin

Gene

RHO

Organism
Todarodes pacificus (Japanese flying squid) (Ommastrephes pacificus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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
OrganismiTodarodes pacificus (Japanese flying squid) (Ommastrephes pacificus)
Taxonomic identifieri6637 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaCephalopodaColeoideaNeocoleoideaDecapodiformesTeuthidaOegopsinaOmmastrephidaeTodarodes

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 33ExtracellularSequence analysisAdd BLAST32
Transmembranei34 – 58Helical; Name=1Sequence analysisAdd BLAST25
Topological domaini59 – 70CytoplasmicSequence analysisAdd BLAST12
Transmembranei71 – 97Helical; Name=2Sequence analysisAdd BLAST27
Topological domaini98 – 111ExtracellularSequence analysisAdd BLAST14
Transmembranei112 – 131Helical; Name=3Sequence analysisAdd BLAST20
Topological domaini132 – 151CytoplasmicSequence analysisAdd BLAST20
Transmembranei152 – 175Helical; Name=4Sequence analysisAdd BLAST24
Topological domaini176 – 199ExtracellularSequence analysisAdd BLAST24
Transmembranei200 – 227Helical; Name=5Sequence analysisAdd BLAST28
Topological domaini228 – 261CytoplasmicSequence analysisAdd BLAST34
Transmembranei262 – 285Helical; Name=6Sequence analysisAdd BLAST24
Topological domaini286 – 293ExtracellularSequence analysis8
Transmembranei294 – 318Helical; Name=7Sequence analysisAdd BLAST25
Topological domaini319 – 448CytoplasmicSequence analysisAdd BLAST130

GO - Cellular componenti

Complete GO annotation...

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...)1
Disulfide bondi108 ↔ 186PROSITE-ProRule annotation
Modified residuei305N6-(retinylidene)lysine1
Lipidationi336S-palmitoyl cysteineBy similarity1
Lipidationi337S-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

PTM databases

UniCarbKBiP31356.

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

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR006031. XYPPX.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
PF02162. XYPPX. 5 hits.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
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.

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.

Cross-referencesi

Sequence databases

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

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...

Protein-protein interaction databases

DIPiDIP-60624N.

Protein family/group databases

GPCRDBiSearch...

PTM databases

UniCarbKBiP31356.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP31356.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR006031. XYPPX.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
PF02162. XYPPX. 5 hits.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
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...

Entry informationi

Entry nameiOPSD_TODPA
AccessioniPrimary (citable) accession number: P31356
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.