Reviewed, UniProtKB/Swiss-Prot P04409 (KPCA_BOVIN)

Names and origin

Protein names

Recommended name:
    Protein kinase C alpha type
      Short name(s)=PKC-alpha, PKC-A
    EC=2.7.11.13

Gene names

Name:

PRKCA

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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
Gene Ontology (GO)
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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 Probable
	Modified residue	495	1	Phosphothreonine Probable
	Modified residue	497	1	Phosphothreonine Probable
	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
	Modified residue	658	1	Phosphotyrosine By similarity
Experimental info
	Mutagenesis	494	1	T → A: Abolishes phosphorylation and catalytic activity; when associated with A-495 and A-497
	Mutagenesis	495	1	T → A: Abolishes phosphorylation and catalytic activity; when associated with A-494 and A-497
	Mutagenesis	497	1	T → A: Abolishes phosphorylation and catalytic activity; when associated with A-494 and A-495

Sequences

	Sequence		Length	Mass (Da)
	P04409-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 97BF46DB80FCF21A	FASTA	672	76,837
	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

References

[1]	"The complete primary structure of protein kinase C -- the major phorbol ester receptor." Parker P.J., Coussens L., Totty N., Rhee L., Young S., Chen E., Stabel S., Waterfield M.D., Ullrich A. Science 233:853-859(1986) [PubMed: 3755547] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"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.
[3]	"Identification of the phosphorylated region responsible for the permissive activation of protein kinase C." Cazaubon S.M., Parker P.J. J. Biol. Chem. 268:17559-17563(1993) [PubMed: 8349635] [Abstract] Cited for: MUTAGENESIS OF THR-494; THR-495 AND THR-497, PHOSPHORYLATION AT THR-494; THR-495 AND THR-497.
[4]	"Phosphorylation of protein kinase C-alpha on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state." Bornancin F., Parker P.J. J. Biol. Chem. 272:3544-3549(1997) [PubMed: 9013603] [Abstract] Cited for: PHOSPHORYLATION AT SER-657.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M13973 mRNA. Translation: AAA30706.1.
PIR	KIBOC. A00621.
RefSeq	NP_776860.1.
UniGene	Bt.62458
3D structure databases
HSSP	HSSP built from PDB template 1DSY based on UniProtKB P05696.
SMR	P04409. Positions 94-158, 95-159, 156-287, 157-288, 336-666.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:530N.
Genome annotation databases
Ensembl	ENSBTAG00000001061. Bos taurus. [Contig view]
GeneID	282001.
KEGG	bta:282001.
Phylogenomic databases
HOVERGEN	P04409.
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
BindingDB	P04409.
ProtoNet	Search...

Entry information

Entry name

KPCA_BOVIN

Accession

Primary (citable) accession number: P04409

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	July 22, 2008
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)