[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; PubMed=3755547 [NCBI, ExPASy, EBI, Israel, Japan] Parker P.J., Coussens L., Totty N., Rhee L., Young S., Chen E., Stabel S., Waterfield M.D., Ullrich A.; "The complete primary structure of protein kinase C -- the major phorbol ester receptor."; Science 233:853-859(1986).
[2]	REVIEW. DOI=10.1038/334661a0; PubMed=3045562 [NCBI, ExPASy, EBI, Israel, Japan] Nishizuka Y.; "The molecular heterogeneity of protein kinase C and its implications for cellular regulation."; Nature 334:661-665(1988).
[3]	MUTAGENESIS OF THR-494; THR-495 AND THR-497, AND PHOSPHORYLATION AT THR-494; THR-495 AND THR-497. PubMed=8349635 [NCBI, ExPASy, EBI, Israel, Japan] Cazaubon S.M., Parker P.J.; "Identification of the phosphorylated region responsible for the permissive activation of protein kinase C."; J. Biol. Chem. 268:17559-17563(1993).
[4]	PHOSPHORYLATION AT SER-657. DOI=10.1074/jbc.272.6.3544; PubMed=9013603 [NCBI, ExPASy, EBI, Israel, Japan] Bornancin F., Parker P.J.; "Phosphorylation of protein kinase C-alpha on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state."; J. Biol. Chem. 272:3544-3549(1997).

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).
FUNCTION: 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: Interacts with CENTA1, CSPG4 and PRKCABP. Binds to SDPR in the presence of phosphatidylserine (By similarity).
SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
SIMILARITY: Contains 1 C2 domain.
SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M13973; AAA30706.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A00621; KIBOC.

NP_776860.1; -.

3D structure databases

HSSP

P05696; 1DSY. [HSSP ENTRY / PDB]

SMR

P04409; 94-158, 95-159, 156-287, 157-288, 336-666.

ModBase

P04409.

Protein-protein interaction databases

DIP

DIP:530N; -.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
QuickGo view.

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 of domain structure.

PANTHER

PTHR22985:SF86; PKC; 1.

Pfam

PF00130; C1_1; 2.
PF00168; C2; 1.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000550; PKC_alpha; 1.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00109; C1; 2.
SM00239; C2; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS51285; AGC_KINASE_CTER; 1.
PS50004; C2; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS00479; ZF_DAG_PE_1; 2.
PS50081; ZF_DAG_PE_2; 2.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSBTAG00000001061; Bos taurus. [Contig view]

GeneID

282001; -.

KEGG

bta:282001; -.

Phylogenomic databases

HOVERGEN

P04409; -.

Other

BindingDB

P04409; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Calcium; Kinase; Metal-binding; Nucleotide-binding; Phorbol-ester binding; Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 672`	`671`	`Protein kinase C alpha type.`	`PRO_0000055678`
`DOMAIN`	`172 260`	`89`	`C2.`
`DOMAIN`	`339 597`	`259`	`Protein kinase.`
`DOMAIN`	`598 668`	`71`	`AGC-kinase C-terminal.`
`ZN_FING`	`36 86`	`51`	`Phorbol-ester/DAG-type 1.`
`ZN_FING`	`101 151`	`51`	`Phorbol-ester/DAG-type 2.`
`NP_BIND`	`345 353`	`9`	`ATP (By similarity).`
`ACT_SITE`	`463 463`		`Proton acceptor (By similarity).`
`METAL`	`186 186`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`187 187`		`Calcium 1 (By similarity).`
`METAL`	`187 187`		`Calcium 2 (By similarity).`
`METAL`	`193 193`		`Calcium 2 (By similarity).`
`METAL`	`246 246`		`Calcium 1 (By similarity).`
`METAL`	`246 246`		`Calcium 2 (By similarity).`
`METAL`	`247 247`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`248 248`		`Calcium 1 (By similarity).`
`METAL`	`248 248`		`Calcium 2 (By similarity).`
`METAL`	`248 248`		`Calcium 3 (By similarity).`
`METAL`	`252 252`		`Calcium 3; via carbonyl oxygen (By similarity).`
`METAL`	`254 254`		`Calcium 1 (By similarity).`
`METAL`	`254 254`		`Calcium 3 (By similarity).`
`BINDING`	`368 368`		`ATP (By similarity).`
`MOD_RES`	`226 226`		`Phosphoserine (By similarity).`
`MOD_RES`	`319 319`		`Phosphoserine (By similarity).`
`MOD_RES`	`494 494`		`Phosphothreonine (Probable).`
`MOD_RES`	`495 495`		`Phosphothreonine (Probable).`
`MOD_RES`	`497 497`		`Phosphothreonine (Probable).`
`MOD_RES`	`501 501`		`Phosphothreonine (By similarity).`
`MOD_RES`	`631 631`		`Phosphothreonine; by autocatalysis (Potential).`
`MOD_RES`	`638 638`		`Phosphothreonine; by autocatalysis (By similarity).`
`MOD_RES`	`657 657`		`Phosphoserine.`
`MOD_RES`	`658 658`		`Phosphotyrosine (By similarity).`
`MUTAGEN`	`494 494`		`T->A: Abolishes phosphorylation and catalytic activity; when associated with A-495 and A-497.`
`MUTAGEN`	`495 495`		`T->A: Abolishes phosphorylation and catalytic activity; when associated with A-494 and A-497.`
`MUTAGEN`	`497 497`		`T->A: Abolishes phosphorylation and catalytic activity; when associated with A-494 and A-495.`

Sequence information

Length: 672 AA [This is the length of the unprocessed precursor]

Molecular weight: 76837 Da [This is the MW of the unprocessed precursor]

CRC64: 97BF46DB80FCF21A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADVFPAAEP AAPQDVANRF ARKGALRQKN VHEVKNHRFI ARFFKQPTFC SHCTDFIWGF 

        70         80         90        100        110        120 
GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS KHKFKIHTYG SPTFCDHCGS 

       130        140        150        160        170        180 
LLYGLIHQGM KCDTCDMNVH KQCVINVPSL CGMDHTEKRG RIYLKAEVTD EKLHVTVRDA 

       190        200        210        220        230        240 
KNLIPMDPNG LSDPYVKLKL IPDPKNESKQ KTKTIRSTLN PRWDESFTFK LKPSDKDRRL 

       250        260        270        280        290        300 
SEEIWDWDRT TRNDFMGSLS FGVSELMKMP ASGWYKLLNQ EEGEYYNVPI PEGDEEGNVE 

       310        320        330        340        350        360 
LRQKFEKAKL GPAGNKVISP SEDRRQPSNN LDRVKLTDFN FLMVLGKGSF GKVMLADRKG 

       370        380        390        400        410        420 
TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALLDKPPFL TQLHSCFQTV DRLYFVMEYV 

       430        440        450        460        470        480 
NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG LFFLHKRGII YRDLKLDNVM LDSEGHIKIA 

       490        500        510        520        530        540 
DFGMCKEHMM DGVTTRTFCG TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG 

       550        560        570        580        590        600 
EDEDELFQSI MEHNVSYPKS LSKEAVSICK GLMTKHPGKR LGCGPEGERD VREHAFFRRI 

       610        620        630        640        650        660 
DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVLTPP DQLVIANIDQ SDFEGFSYVN 

       670 
PQFVHPILQS AV

P04409 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools