Reviewed,
UniProtKB/Swiss-Prot P05696 (KPCA_RAT)
Last modified
September 2, 2008.
Version 103.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Protein kinase C alpha type Short name=PKC-alpha Short name=PKC-A EC=2.7.11.13 | ||||
| Gene names |
| ||||
| 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 | 672 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. May play a role in cell motility by phosphorylating CSPG4 By similarity. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. |
| 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. |
| Subunit structure | Interacts with CENTA1, CSPG4 and PRKCABP. Binds to SDPR in the presence of phosphatidylserine 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
Keywords | |
|---|---|
| Domain | Phorbol-ester binding Repeat Zinc-finger |
| Ligand | ATP-binding Calcium Metal-binding Nucleotide-binding Zinc |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | establishment of protein localization Traceable author statement. Source: UniProtKB |
| Molecular function | protein binding Ref.3 Inferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| TRIM41 | Q8WV44 | 1 | EBI-935801,EBI-725997 | From a different organism. |
| TRIM41 | Q8WV44-2 | 1 | EBI-935801,EBI-726015 | From a different organism. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | |||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||||||||||||||||||||||
| Chain | 2 – 672 | 671 | Protein kinase C alpha type | ||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||
| Domain | 172 – 260 | 89 | C2 | ||||||||||||||||||||||||||||
| Domain | 339 – 597 | 259 | Protein kinase | ||||||||||||||||||||||||||||
| Domain | 598 – 668 | 71 | AGC-kinase C-terminal | ||||||||||||||||||||||||||||
| Zinc finger | 36 – 86 | 51 | Phorbol-ester/DAG-type 1 | ||||||||||||||||||||||||||||
| Zinc finger | 101 – 151 | 51 | Phorbol-ester/DAG-type 2 | ||||||||||||||||||||||||||||
| Nucleotide binding | 345 – 353 | 9 | ATP By similarity | ||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||
| Active site | 463 | 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 | 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 | 368 | 1 | ATP By similarity | ||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||
| Modified residue | 226 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||
| Modified residue | 319 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||
| Modified residue | 494 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||
| Modified residue | 495 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||
| Modified residue | 497 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||
| Modified residue | 501 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||
| Modified residue | 631 | 1 | Phosphothreonine; by autocatalysis Potential | ||||||||||||||||||||||||||||
| Modified residue | 638 | 1 | Phosphothreonine; by autocatalysis By similarity | ||||||||||||||||||||||||||||
| Modified residue | 657 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||
| Modified residue | 658 | 1 | Phosphotyrosine By similarity | ||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||
| Beta strand | 161 – 168 | 8 | |||||||||||||||||||||||||||||
| Beta strand | 170 – 182 | 13 | |||||||||||||||||||||||||||||
| Beta strand | 194 – 202 | 9 | |||||||||||||||||||||||||||||
| Beta strand | 222 – 230 | 9 | |||||||||||||||||||||||||||||
| Helix | 233 – 235 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 239 – 246 | 8 | |||||||||||||||||||||||||||||
| Beta strand | 249 – 251 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 254 – 262 | 9 | |||||||||||||||||||||||||||||
| Helix | 263 – 268 | 6 | |||||||||||||||||||||||||||||
| Beta strand | 271 – 276 | 6 | |||||||||||||||||||||||||||||
| Helix | 280 – 283 | 4 | |||||||||||||||||||||||||||||
| Beta strand | 288 – 290 | 3 | |||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Nucleotide sequences of cDNAs for alpha and gamma subspecies of rat brain protein kinase C." Ono Y., Fujii T., Igarashi K., Kikkawa U., Ogita K., Nishizuka Y. Nucleic Acids Res. 16:5199-5200(1988) [PubMed: 3387228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
| [2] | "The common structure and activities of four subspecies of rat brain protein kinase C family." Kikkawa U., Ogita K., Ono Y., Asaoka Y., Shearman M.S., Fujii T., Ase K., Sekiguchi K., Igarashi K., Nishizuka Y. FEBS Lett. 223:212-216(1987) [PubMed: 3666147] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
| [3] | "Targeting of protein kinase Calpha to caveolae." Mineo C., Ying Y.-S., Chapline C., Jaken S., Anderson R.G.W. J. Cell Biol. 141:601-610(1998) [PubMed: 9566962] [Abstract] Cited for: INTERACTION WITH SDPR. |
| [4] | "The molecular heterogeneity of protein kinase C and its implications for cellular regulation." Nishizuka Y. Nature 334:661-665(1988) [PubMed: 3045562] [Abstract] Cited for: REVIEW. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| X07286 mRNA. Translation: CAA30266.1. | |||||||||||||
| PIR | KIRTC. S02248. | ||||||||||||
| UniGene | Rn.207908 | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| SMR | P05696. Positions 94-158, 95-159, 336-666. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P05696. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P05696. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSRNOG00000003491. Rattus norvegicus. [Contig view] | ||||||||||||
Organism-specific databases | |||||||||||||
| RGD | 3395. Prkca. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | P05696. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P05696. | ||||||||||||
| GermOnline | ENSRNOG00000003491. Rattus norvegicus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR000008. C2_Ca-dep. IPR002219. DAG_PE_bd. IPR015745. PKC. IPR000961. Pkinase_C. IPR014375. Prot_kin_PKC_alpha. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view] | ||||||||||||
| PANTHER | PTHR22985:SF86. PKC. 1 hit. | ||||||||||||
| 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. | ||||||||||||
| ProDom | PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| SMART | SM00109. C1. 2 hits. SM00239. C2. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view] | ||||||||||||
| 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] | ||||||||||||
| BLOCKS | Search... | ||||||||||||
Other Resources | |||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | KPCA_RAT | ||||||||
| Accession | Primary (citable) accession number: P05696 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


