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Q17094 (OPSD_ALLSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rhodopsin
Gene names
Name:RHO
OrganismAlloteuthis subulata (Squid) (Loligo subulata)
Taxonomic identifier54069 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaCephalopodaColeoideaNeocoleoideaDecapodiformesTeuthidaMyopsinaLoliginidaeAlloteuthis

Protein attributes

Sequence length439 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Membrane; Multi-pass membrane protein.

Post-translational modification

Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.

Sequence similarities

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

Biophysicochemical properties

Absorption:

Abs(max)=499 nm

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›439›439Rhodopsin
PRO_0000197733

Regions

Topological domain‹1 – 26›26Extracellular Potential
Transmembrane27 – 5125Helical; Name=1; Potential
Topological domain52 – 6312Cytoplasmic Potential
Transmembrane64 – 9027Helical; Name=2; Potential
Topological domain91 – 10414Extracellular Potential
Transmembrane105 – 12420Helical; Name=3; Potential
Topological domain125 – 14420Cytoplasmic Potential
Transmembrane145 – 16824Helical; Name=4; Potential
Topological domain169 – 19224Extracellular Potential
Transmembrane193 – 22028Helical; Name=5; Potential
Topological domain221 – 25434Cytoplasmic Potential
Transmembrane255 – 27824Helical; Name=6; Potential
Topological domain279 – 2879Extracellular Potential
Transmembrane288 – 31124Helical; Name=7; Potential
Topological domain312 – ›439›128Cytoplasmic Potential
Compositional bias363 – 37311Met-rich
Compositional bias374 – 43663Gln/Pro-rich

Amino acid modifications

Modified residue2981N6-(retinylidene)lysine By similarity
Lipidation3291S-palmitoyl cysteine By similarity
Lipidation3301S-palmitoyl cysteine By similarity
Glycosylation11N-linked (GlcNAc...) Probable
Disulfide bond101 ↔ 179 By similarity

Experimental info

Non-terminal residue11
Non-terminal residue4391

Sequences

Sequence LengthMass (Da)Tools
Q17094 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B8167DFD8A00390E

FASTA43949,017
        10         20         30         40         50         60 
NETWWYNPYM DIHSHWKQFD QVPAAVYYSL GIFIAICGII GCAGNGIVIY LFTKTKSLQT 

        70         80         90        100        110        120 
PANMFIINLA FSDFTFSLVN GFPMMTISCF LKHWVFGQAA CKVYGLIGGI FGLTSIMTMT 

       130        140        150        160        170        180 
MISIDRYNVI RRPMSASKKM SHRKAFIMIV FVWIWSTIWA IGPIFGWGAY QLEGVLCNCS 

       190        200        210        220        230        240 
FDYITRDAST RSNIVCMYIF AFMFPIVVIF FCYFNIVMSV SNHEKEMAAM AKRLNAKELR 

       250        260        270        280        290        300 
KAQAGASAEM KLAKISIVIV TQSLLSWSPY AIVALLAQFG PIEWVTPYAA QLPVMFAKAS 

       310        320        330        340        350        360 
AIHNPMIYSV SHPKFREAIA SNFPWILTCC QYDEKEIEDD KDAEAEIPAA EQSGGESVDA 

       370        380        390        400        410        420 
AQMKEMMAMM QKMQAQQQQQ PAYPPQGYPP QGYPPPPPQG YPPQGYPPQG YPPQGYPPPP 

       430 
QGPPPQGPPP QAAPPQGVD 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49108 Genomic DNA. Translation: CAA88923.1.
PIRS60755.

3D structure databases

ProteinModelPortalQ17094.
SMRQ17094. Positions 1-351.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

GPCRDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR006031. XYPPX.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
PF02162. XYPPX. 3 hits.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOPSD_ALLSU
AccessionPrimary (citable) accession number: Q17094
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries