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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

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
OrganismiAlloteuthis subulata (Squid) (Loligo subulata)
Taxonomic identifieri54069 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaCephalopodaColeoideaNeocoleoideaDecapodiformesTeuthidaMyopsinaLoliginidaeAlloteuthis

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini‹1 – 26ExtracellularSequence analysisAdd BLAST›26
Transmembranei27 – 51Helical; Name=1Sequence analysisAdd BLAST25
Topological domaini52 – 63CytoplasmicSequence analysisAdd BLAST12
Transmembranei64 – 90Helical; Name=2Sequence analysisAdd BLAST27
Topological domaini91 – 104ExtracellularSequence analysisAdd BLAST14
Transmembranei105 – 124Helical; Name=3Sequence analysisAdd BLAST20
Topological domaini125 – 144CytoplasmicSequence analysisAdd BLAST20
Transmembranei145 – 168Helical; Name=4Sequence analysisAdd BLAST24
Topological domaini169 – 192ExtracellularSequence analysisAdd BLAST24
Transmembranei193 – 220Helical; Name=5Sequence analysisAdd BLAST28
Topological domaini221 – 254CytoplasmicSequence analysisAdd BLAST34
Transmembranei255 – 278Helical; Name=6Sequence analysisAdd BLAST24
Topological domaini279 – 287ExtracellularSequence analysis9
Transmembranei288 – 311Helical; Name=7Sequence analysisAdd BLAST24
Topological domaini312 – ›439CytoplasmicSequence analysisAdd BLAST›128

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000197733‹1 – ›439RhodopsinAdd BLAST›439

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi1N-linked (GlcNAc...)Curated1
Disulfide bondi101 ↔ 179PROSITE-ProRule annotation
Modified residuei298N6-(retinylidene)lysineBy similarity1
Lipidationi329S-palmitoyl cysteineBy similarity1
Lipidationi330S-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

Structurei

3D structure databases

ProteinModelPortaliQ17094.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi363 – 373Met-richAdd BLAST11
Compositional biasi374 – 436Gln/Pro-richAdd BLAST63

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.
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: 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)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei4391

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.
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.
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_ALLSU
AccessioniPrimary (citable) accession number: Q17094
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 79 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

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.