P10829 (KPCG_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 112.
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: Protein kinase C gamma type Short name=PKC-gamma EC=2.7.11.13 Alternative name(s): PKC-delta | ||
| Gene names |
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| Organism | Oryctolagus cuniculus (Rabbit) [Complete proteome] | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 697 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum By similarity. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Ref.2 |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Cofactor | Binds 3 calcium ions per subunit. The ions are bound to the C2 domain By similarity. |
| Enzyme regulation | Classical (or conventional) PKCs (PRKCA, PRKCB and PRKCG) are activated by calcium and diacylglycerol (DAG) in the presence of phosphatidylserine. Three specific sites; Thr-514 (activation loop of the kinase domain), Thr-655 (turn motif) and Thr-674 (hydrophobic region), need to be phosphorylated for its full activation. |
| Subunit structure | Interacts with CDCP1 and GRIA4 By similarity. |
| Subcellular location | Cytoplasm By similarity. Cytoplasm › perinuclear region By similarity. Cell membrane; Peripheral membrane protein By similarity. Cell junction › synapse › synaptosome By similarity. Cell projection › dendrite By similarity. Note: Translocates to synaptic membranes on stimulation By similarity. |
| Tissue specificity | Expressed specifically in brain. Ref.1 |
| Induction | Activated by hydrogen peroxide. Ref.2 |
| Post-translational modification | Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4 By similarity. |
| Sequence similarities | Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 C2 domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 697 | 697 | Protein kinase C gamma type | PRO_0000055691 | |||||
Regions | |||||||||
| Domain | 170 – 260 | 91 | C2 | ||||||
| Domain | 351 – 614 | 264 | Protein kinase | ||||||
| Domain | 615 – 685 | 71 | AGC-kinase C-terminal | ||||||
| Zinc finger | 35 – 85 | 51 | Phorbol-ester/DAG-type 1 | ||||||
| Zinc finger | 100 – 150 | 51 | Phorbol-ester/DAG-type 2 | ||||||
| Nucleotide binding | 357 – 365 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 480 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 186 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 187 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 187 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 193 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 246 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 246 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 247 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 248 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 248 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 248 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 251 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 252 | 1 | Calcium 3; via carbonyl oxygen By similarity | ||||||
| Metal binding | 254 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 254 | 1 | Calcium 3 By similarity | ||||||
| Binding site | 380 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 195 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 197 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 250 | 1 | Phosphothreonine; by autocatalysis By similarity | ||||||
| Modified residue | 312 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 322 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 330 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 514 | 1 | Phosphothreonine; by PDPK1 By similarity | ||||||
| Modified residue | 518 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 648 | 1 | Phosphothreonine; by autocatalysis By similarity | ||||||
| Modified residue | 655 | 1 | Phosphothreonine; by autocatalysis Potential | ||||||
| Modified residue | 674 | 1 | Phosphothreonine; by autocatalysis By similarity | ||||||
| Modified residue | 675 | 1 | Phosphotyrosine; by SYK By similarity | ||||||
| Modified residue | 687 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "A fourth type of rabbit protein kinase C." Ohno S., Kawasaki H., Konno Y., Inagaki M., Hidaka H., Suzuki K. Biochemistry 27:2083-2087(1988) [PubMed: 2837282] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. |
| [2] | "Oxidative activation of protein kinase Cgamma through the C1 domain. Effects on gap junctions." Lin D., Takemoto D.J. J. Biol. Chem. 280:13682-13693(2005) [PubMed: 15642736] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF GJA1/CX43, INDUCTION BY HYDROGEN PEROXIDE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M19338 mRNA. Translation: AAA31449.1. |
| PIR | KIRBGC. A28708. |
| RefSeq | NP_001075742.1. NM_001082273.1. |
| UniGene | Ocu.1950. |
3D structure databases | |
| ProteinModelPortal | P10829. |
| SMR | P10829. Positions 36-293. |
| ModBase | Search... |
Protein-protein interaction databases | |
| MINT | MINT-1205863. |
| STRING | P10829. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100009102. |
Organism-specific databases | |
| CTD | 5582. |
Phylogenomic databases | |
| GeneTree | ENSGT00590000082854. |
| HOVERGEN | HBG108317. |
| OrthoDB | EOG40CHGD. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.13. 1749. |
Family and domain databases | |
| InterPro | IPR000961. AGC-kinase_C. IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR020477. C2_dom. IPR018029. C2_membr_targeting. IPR020454. DAG/PE-bd. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR014375. Protein_kinase_C_a/b/g. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view] |
| Pfam | PF00130. C1_1. 2 hits. PF00168. C2. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view] |
| PIRSF | PIRSF000550. PKC_alpha. 1 hit. |
| PRINTS | PR00360. C2DOMAIN. PR00008. DAGPEDOMAIN. |
| SMART | SM00109. C1. 2 hits. SM00239. C2. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view] |
| SUPFAM | SSF49562. C2_CaLB. 1 hit. SSF56112. Kinase_like. 1 hit. |
| PROSITE | PS51285. AGC_KINASE_CTER. 1 hit. PS50004. C2. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS00479. ZF_DAG_PE_1. 2 hits. PS50081. ZF_DAG_PE_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KPCG_RABIT | ||||||||
| Accession | Primary (citable) accession number: P10829 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with