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Protein

Rhodopsin

Gene

RHO

Organism
Alloteuthis subulata (Squid) (Loligo subulata)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Absorptioni

Abs(max)=499 nm

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: UniProtKB-KW
  2. photoreceptor activity Source: UniProtKB-KW

GO - Biological processi

  1. phototransduction Source: UniProtKB-KW
  2. protein-chromophore linkage Source: UniProtKB-KW
  3. visual perception Source: UniProtKB-KW
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
OrganismiAlloteuthis subulata (Squid) (Loligo subulata)
Taxonomic identifieri54069 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaCephalopodaColeoideaNeocoleoideaDecapodiformesTeuthidaMyopsinaLoliginidaeAlloteuthis

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini‹1 – 26›26ExtracellularSequence AnalysisAdd
BLAST
Transmembranei27 – 5125Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini52 – 6312CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei64 – 9027Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini91 – 10414ExtracellularSequence AnalysisAdd
BLAST
Transmembranei105 – 12420Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini125 – 14420CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei145 – 16824Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini169 – 19224ExtracellularSequence AnalysisAdd
BLAST
Transmembranei193 – 22028Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini221 – 25434CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei255 – 27824Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini279 – 2879ExtracellularSequence Analysis
Transmembranei288 – 31124Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini312 – ›439›128CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›439›439RhodopsinPRO_0000197733Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi1 – 11N-linked (GlcNAc...)Curated
Disulfide bondi101 ↔ 179PROSITE-ProRule annotation
Modified residuei298 – 2981N6-(retinylidene)lysineBy similarity
Lipidationi329 – 3291S-palmitoyl cysteineBy similarity
Lipidationi330 – 3301S-palmitoyl cysteineBy similarity

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

Structurei

3D structure databases

ProteinModelPortaliQ17094.
SMRiQ17094. Positions 1-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi363 – 37311Met-richAdd
BLAST
Compositional biasi374 – 43663Gln/Pro-richAdd
BLAST

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. 3 hits.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
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: Fragment.

Q17094-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NETWWYNPYM DIHSHWKQFD QVPAAVYYSL GIFIAICGII GCAGNGIVIY
60 70 80 90 100
LFTKTKSLQT PANMFIINLA FSDFTFSLVN GFPMMTISCF LKHWVFGQAA
110 120 130 140 150
CKVYGLIGGI FGLTSIMTMT MISIDRYNVI RRPMSASKKM SHRKAFIMIV
160 170 180 190 200
FVWIWSTIWA IGPIFGWGAY QLEGVLCNCS FDYITRDAST RSNIVCMYIF
210 220 230 240 250
AFMFPIVVIF FCYFNIVMSV SNHEKEMAAM AKRLNAKELR KAQAGASAEM
260 270 280 290 300
KLAKISIVIV TQSLLSWSPY AIVALLAQFG PIEWVTPYAA QLPVMFAKAS
310 320 330 340 350
AIHNPMIYSV SHPKFREAIA SNFPWILTCC QYDEKEIEDD KDAEAEIPAA
360 370 380 390 400
EQSGGESVDA AQMKEMMAMM QKMQAQQQQQ PAYPPQGYPP QGYPPPPPQG
410 420 430
YPPQGYPPQG YPPQGYPPPP QGPPPQGPPP QAAPPQGVD
Length:439
Mass (Da):49,017
Last modified:November 1, 1996 - v1
Checksum:iB8167DFD8A00390E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei439 – 4391

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49108 Genomic DNA. Translation: CAA88923.1.
PIRiS60755.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49108 Genomic DNA. Translation: CAA88923.1.
PIRiS60755.

3D structure databases

ProteinModelPortaliQ17094.
SMRiQ17094. Positions 1-351.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

GPCRDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. 3 hits.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
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. "The molecular basis of a spectral shift in the rhodopsins of two species of squid from different photic environments."
    Morris A., Bowmaker J.K., Hunt D.M.
    Proc. R. Soc. B 254:233-240(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Epidermis.

Entry informationi

Entry nameiOPSD_ALLSU
AccessioniPrimary (citable) accession number: Q17094
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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

External Data

Dasty 3

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 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.