Q17094 (OPSD_ALLSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 69.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Rhodopsin | ||
| Gene names |
| ||
| Organism | Alloteuthis subulata (Squid) (Loligo subulata) | ||
| Taxonomic identifier | 54069 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Lophotrochozoa › Mollusca › Cephalopoda › Coleoidea › Neocoleoidea › Decapodiformes › Teuthida › Myopsina › Loliginidae › Alloteuthis![]() |
Protein attributes
| Sequence length | 439 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence 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 | |
| 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 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Sensory transduction Vision |
| Cellular component | Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | Chromophore |
| Molecular function | G-protein coupled receptor Photoreceptor protein Receptor Retinal protein Transducer |
| PTM | Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein |
| Gene Ontology (GO) | |
| Biological_process | phototransduction Inferred from electronic annotation. Source: UniProtKB-KW protein-chromophore linkageInferred from electronic annotation. Source: UniProtKB-KW visual perceptionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | G-protein coupled receptor activity Inferred from electronic annotation. Source: UniProtKB-KW photoreceptor activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›439 | ›439 | Rhodopsin | PRO_0000197733 | |||||||
Regions | |||||||||||
| Topological domain | ‹1 – 26 | ›26 | Extracellular Potential | ||||||||
| Transmembrane | 27 – 51 | 25 | Helical; Name=1; Potential | ||||||||
| Topological domain | 52 – 63 | 12 | Cytoplasmic Potential | ||||||||
| Transmembrane | 64 – 90 | 27 | Helical; Name=2; Potential | ||||||||
| Topological domain | 91 – 104 | 14 | Extracellular Potential | ||||||||
| Transmembrane | 105 – 124 | 20 | Helical; Name=3; Potential | ||||||||
| Topological domain | 125 – 144 | 20 | Cytoplasmic Potential | ||||||||
| Transmembrane | 145 – 168 | 24 | Helical; Name=4; Potential | ||||||||
| Topological domain | 169 – 192 | 24 | Extracellular Potential | ||||||||
| Transmembrane | 193 – 220 | 28 | Helical; Name=5; Potential | ||||||||
| Topological domain | 221 – 254 | 34 | Cytoplasmic Potential | ||||||||
| Transmembrane | 255 – 278 | 24 | Helical; Name=6; Potential | ||||||||
| Topological domain | 279 – 287 | 9 | Extracellular Potential | ||||||||
| Transmembrane | 288 – 311 | 24 | Helical; Name=7; Potential | ||||||||
| Topological domain | 312 – ›439 | ›128 | Cytoplasmic Potential | ||||||||
| Compositional bias | 363 – 373 | 11 | Met-rich | ||||||||
| Compositional bias | 374 – 436 | 63 | Gln/Pro-rich | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 298 | 1 | N6-(retinylidene)lysine By similarity | ||||||||
| Lipidation | 329 | 1 | S-palmitoyl cysteine By similarity | ||||||||
| Lipidation | 330 | 1 | S-palmitoyl cysteine By similarity | ||||||||
| Glycosylation | 1 | 1 | N-linked (GlcNAc...) Probable | ||||||||
| Disulfide bond | 101 ↔ 179 | By similarity | |||||||||
Experimental info | |||||||||||
| Non-terminal residue | 1 | 1 | |||||||||
| Non-terminal residue | 439 | 1 | |||||||||
Sequences
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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. |
| PIR | S60755. |
3D structure databases | |
| ProteinModelPortal | Q17094. |
| SMR | Q17094. Positions 1-351. |
| ModBase | Search... |
Protein family/group databases | |
| GPCRDB | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. IPR001760. Opsin. IPR006031. XYPPX. [Graphical view] |
| Pfam | PF00001. 7tm_1. 1 hit. PF02162. XYPPX. 3 hits. [Graphical view] |
| PRINTS | PR00237. GPCRRHODOPSN. PR00238. OPSIN. |
| PROSITE | PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. PS00238. OPSIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | OPSD_ALLSU | ||||||||
| Accession | Primary (citable) accession number: Q17094 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| 7-transmembrane G-linked receptors List of 7-transmembrane G-linked receptor entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
