Reviewed,
UniProtKB/Swiss-Prot Q63651 (RK_RAT)
Last modified
February 9, 2010.
Version 94.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Rhodopsin kinase Short name=RK EC=2.7.11.14 Alternative name(s): G protein-coupled receptor kinase 1 | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 564 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Phosphorylates rhodopsin thereby initiating its deactivation. |
| Catalytic activity | ATP + [rhodopsin] = ADP + [rhodopsin] phosphate. |
| Subcellular location | |
| Post-translational modification | Autophosphorylated By similarity. Farnesylation is required for full activity By similarity. |
| Sequence similarities | Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain. Contains 1 RGS domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Lipoprotein Methylation Phosphoprotein Prenylation |
| Gene Ontology (GO) | |
| Biological process | protein amino acid autophosphorylation Inferred from direct assay. Source: RGD response to drugInferred from expression pattern. Source: RGD rhodopsin mediated phototransduction Ref.1Traceable author statement. Source: RGD |
| Cellular component | anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW G-protein coupled receptor kinase activityInferred from electronic annotation. Source: InterPro rhodopsin kinase activity Ref.1Inferred from direct assay. Source: RGD signal transducer activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 561 | 561 | Rhodopsin kinase | PRO_0000024379 | |||||
| Propeptide | 562 – 564 | 3 | Removed in mature form By similarity | PRO_0000024380 | |||||
Regions | |||||||||
| Domain | 58 – 175 | 118 | RGS | ||||||
| Domain | 190 – 455 | 266 | Protein kinase | ||||||
| Domain | 456 – 521 | 66 | AGC-kinase C-terminal | ||||||
| Nucleotide binding | 196 – 204 | 9 | ATP By similarity | ||||||
| Region | 1 – 189 | 189 | N-terminal | ||||||
| Region | 456 – 564 | 109 | C-terminal | ||||||
Sites | |||||||||
| Active site | 317 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 219 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 21 | 1 | Phosphoserine; by autocatalysis By similarity | ||||||
| Modified residue | 491 | 1 | Phosphoserine; by autocatalysis By similarity | ||||||
| Modified residue | 492 | 1 | Phosphothreonine; by autocatalysis By similarity | ||||||
| Modified residue | 561 | 1 | Cysteine methyl ester By similarity | ||||||
| Lipidation | 561 | 1 | S-farnesyl cysteine By similarity | ||||||
Sequences
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References
| [1] | "Molecular cloning and localization of rhodopsin kinase in the mammalian pineal." Zhao X., Haeseleer F., Fariss R.N., Huang J., Baehr W., Milam A.H., Palczewski K. Vis. Neurosci. 14:225-232(1997) [PubMed: 9147475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Retina. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U63971 mRNA. Translation: AAB05930.1. |
| IPI | IPI00211058. |
| RefSeq | NP_112358.1. |
| UniGene | Rn.10548 |
3D structure databases | |
| SMR | Q63651. Positions 30-536. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q63651. |
PTM databases | |
| PhosphoSite | Q63651. |
Proteomic databases | |
| PRIDE | Q63651. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000024999; ENSRNOP00000024999; ENSRNOG00000018430; Rattus norvegicus. [Genome view] |
| GeneID | 81760. |
| KEGG | rno:81760. |
| UCSC | NM_031096. rat. |
Organism-specific databases | |
| CTD | 81760. |
| RGD | 619712. Grk1. |
Phylogenomic databases | |
| eggNOG | roNOG15472. |
| HOVERGEN | Q63651. |
| InParanoid | Q63651. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.14. 248. |
Gene expression databases | |
| Genevestigator | Q63651. |
| GermOnline | ENSRNOG00000018430. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000961. AGC-kinase_C. IPR000239. GPCR_kinase. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR000342. Regulat_G_prot_signal. IPR016137. Regulat_G_prot_signal_superfam. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view] |
| Pfam | PF00069. Pkinase. 1 hit. PF00615. RGS. 1 hit. [Graphical view] |
| PRINTS | PR00717. GPCRKINASE. |
| SMART | SM00315. RGS. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view] |
| PROSITE | PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS50132. RGS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 615542. |
Entry information
| Entry name | RK_RAT | ||||||||
| Accession | Primary (citable) accession number: Q63651 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


