Reviewed,
UniProtKB/Swiss-Prot P02700 (OPSD_SHEEP)
Last modified
June 16, 2009.
Version 75.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Rhodopsin | ||
| Gene names |
| ||
| Organism | Ovis aries (Sheep) | ||
| Taxonomic identifier | 9940 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis |
Protein attributes
| Sequence length | 348 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal By similarity. |
| Subcellular location | |
| Tissue specificity | Rod shaped photoreceptor cells which mediates vision in dim light. |
| Sequence similarities | Belongs to the G-protein coupled receptor 1 family. Opsin subfamily. |
| biophysicochemical properties | Absorption: Abs(max)=495 nm |
Ontologies
| Keywords | |
|---|---|
| Biological process | Sensory transduction Vision |
| Cellular component | Membrane |
| Domain | Transmembrane |
| Ligand | Chromophore |
| Molecular function | G-protein coupled receptor Photoreceptor protein Receptor Retinal protein Transducer |
| PTM | Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | G-protein coupled receptor protein signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW phototransductionInferred from electronic annotation. Source: UniProtKB-KW protein-chromophore linkageInferred 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 – 348 | 348 | Rhodopsin | PRO_0000197719 | |||||||
Regions | |||||||||||
| Topological domain | 1 – 36 | 36 | Extracellular | ||||||||
| Transmembrane | 37 – 61 | 25 | 1 Potential | ||||||||
| Topological domain | 62 – 73 | 12 | Cytoplasmic | ||||||||
| Transmembrane | 74 – 98 | 25 | 2 Potential | ||||||||
| Topological domain | 99 – 113 | 15 | Extracellular | ||||||||
| Transmembrane | 114 – 133 | 20 | 3 Potential | ||||||||
| Topological domain | 134 – 152 | 19 | Cytoplasmic | ||||||||
| Transmembrane | 153 – 176 | 24 | 4 Potential | ||||||||
| Topological domain | 177 – 202 | 26 | Extracellular | ||||||||
| Transmembrane | 203 – 230 | 28 | 5 Potential | ||||||||
| Topological domain | 231 – 252 | 22 | Cytoplasmic | ||||||||
| Transmembrane | 253 – 276 | 24 | 6 Potential | ||||||||
| Topological domain | 277 – 284 | 8 | Extracellular | ||||||||
| Transmembrane | 285 – 309 | 25 | 7 Potential | ||||||||
| Topological domain | 310 – 348 | 39 | Cytoplasmic | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 296 | 1 | N6-(retinylidene)lysine | ||||||||
| Modified residue | 334 | 1 | Phosphoserine; by RK Ref.5 | ||||||||
| Modified residue | 335 | 1 | Phosphothreonine; by RK Ref.5 | ||||||||
| Modified residue | 336 | 1 | Phosphothreonine; by RK Ref.5 | ||||||||
| Modified residue | 338 | 1 | Phosphoserine; by RK Ref.5 | ||||||||
| Modified residue | 343 | 1 | Phosphoserine; by RK Ref.5 | ||||||||
| Lipidation | 322 | 1 | S-palmitoyl cysteine By similarity | ||||||||
| Lipidation | 323 | 1 | S-palmitoyl cysteine By similarity | ||||||||
| Glycosylation | 2 | 1 | N-linked (GlcNAc...) By similarity | ||||||||
| Glycosylation | 15 | 1 | N-linked (GlcNAc...) By similarity | ||||||||
| Disulfide bond | 110 ↔ 187 | By similarity | |||||||||
Sequences
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References
| [1] | "A structural model for ovine rhodopsin." Pappin D.J.C., Elipoulos E., Brett M., Findlay J.B.C. Int. J. Biol. Macromol. 6:73-76(1984) Cited for: PROTEIN SEQUENCE. |
| [2] | "Isolation and characterization of the CNBr peptides from the proteolytically derived N-terminal fragment of ovine opsin." Brett M., Findlay J.B.C. Biochem. J. 211:661-670(1983) [PubMed: 6224479] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-111 AND 144-239. |
| [3] | "Primary structure of C-terminal functional sites in ovine rhodopsin." Findlay J.B.C., Brett M., Pappin D.J.C. Nature 293:314-316(1981) [PubMed: 7278988] [Abstract] Cited for: PROTEIN SEQUENCE OF 240-348. |
| [4] | "Sequence variability in the retinal-attachment domain of mammalian rhodopsins." Pappin D.J.C., Findlay J.B.C. Biochem. J. 217:605-613(1984) [PubMed: 6370231] [Abstract] Cited for: RETINAL-BINDING SITE. |
| [5] | "Phosphorylation of ovine rhodopsin. Identification of the phosphorylated sites." Thompson P., Findlay J.B.C. Biochem. J. 220:773-780(1984) [PubMed: 6466303] [Abstract] Cited for: PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338 AND SER-343. |
Cross-references
Sequence databases | |
|---|---|
| PIR | OOSH. A30407. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EDS based on UniProtKB P02699. |
| SMR | P02700. Positions 1-348. |
| ModBase | Search... |
Protein family/group databases | |
| GPCRDB | Search... |
Phylogenomic databases | |
| HOVERGEN | P02700. |
Family and domain databases | |
| InterPro | IPR000276. 7TM_GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_supfam. IPR001760. Opsin. IPR000732. Rhodopsin. IPR019477. Rhodopsin_N. [Graphical view] |
| Pfam | PF00001. 7tm_1. 1 hit. PF10413. Rhodopsin_N. 1 hit. [Graphical view] |
| PRINTS | PR00237. GPCRRHODOPSN. PR00238. OPSIN. PR00579. RHODOPSIN. |
| 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_SHEEP | ||||||||
| Accession | Primary (citable) accession number: P02700 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
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


