Protein kinase C alpha type - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot P20444 (KPCA_MOUSE)

Last modified November 3, 2009. Version 111. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

Name:	Prkca
Synonyms:	Pkca

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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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.

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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 ADAP1/CENTA1, CSPG4 and PRKCABP. Binds to SDPR in the presence of phosphatidylserine By similarity. Interacts with PICK1 (via PDZ domain) By similarity. Interacts with TRIM41 By similarity.
Subcellular location	Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity.
Involvement in disease	Expression of the mutant form UV25 causes malignant transformation of cells.
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.

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Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
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	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	cellular calcium ion homeostasis Inferred from mutant phenotype. Source: MGI chondrocyte differentiation Inferred from direct assay. Source: MGI inactivation of MAPK activity Inferred from mutant phenotype. Source: MGI induction of apoptosis by intracellular signals Inferred from mutant phenotype. Source: MGI induction of positive chemotaxis Inferred from mutant phenotype. Source: MGI negative regulation of cell proliferation Inferred from genetic interaction. Source: MGI negative regulation of glucose import Inferred from mutant phenotype. Source: MGI negative regulation of insulin receptor signaling pathway Inferred from mutant phenotype. Source: MGI negative regulation of protein amino acid phosphorylation Inferred from mutant phenotype. Source: MGI neutrophil chemotaxis Inferred from mutant phenotype. Source: MGI positive regulation of inflammatory response Inferred from mutant phenotype. Source: MGI positive regulation of protein amino acid phosphorylation Inferred from mutant phenotype. Source: MGI protein amino acid phosphorylation Inferred from direct assay. Source: MGI regulation of muscle contraction Inferred from mutant phenotype. Source: MGI regulation of peptidyl-tyrosine phosphorylation Inferred from mutant phenotype. Source: MGI regulation of the force of heart contraction Inferred from mutant phenotype. Source: MGI
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: MGI nucleus Inferred from direct assay. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-dependent protein kinase C activity Inferred from direct assay. Source: MGI diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: MGI zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 672

671

Protein kinase C alpha type

PRO_0000055680

Regions

Domain

172 – 260

Domain

339 – 597

259

Protein kinase

Domain

598 – 668

AGC-kinase C-terminal

Zinc finger

36 – 86

Phorbol-ester/DAG-type 1

Zinc finger

101 – 151

Phorbol-ester/DAG-type 2

Nucleotide binding

345 – 353

ATP By similarity

Sites

Active site

463

Proton acceptor By similarity

Metal binding

186

Calcium 1; via carbonyl oxygen By similarity

Metal binding

187

Calcium 1 By similarity

Metal binding

187

Calcium 2 By similarity

Metal binding

193

Calcium 2 By similarity

Metal binding

246

Calcium 1 By similarity

Metal binding

246

Calcium 2 By similarity

Metal binding

247

Calcium 2; via carbonyl oxygen By similarity

Metal binding

248

Calcium 1 By similarity

Metal binding

248

Calcium 2 By similarity

Metal binding

248

Calcium 3 By similarity

Metal binding

252

Calcium 3; via carbonyl oxygen By similarity

Metal binding

254

Calcium 1 By similarity

Metal binding

254

Calcium 3 By similarity

Binding site

195

Inositol phosphate group By similarity

Binding site

245

Inositol phosphate group By similarity

Binding site

368

ATP By similarity

Amino acid modifications

Modified residue

195

Phosphotyrosine By similarity

Modified residue

208

Phosphoserine By similarity

Modified residue

226

Phosphoserine By similarity

Modified residue

319

Phosphoserine Ref.4

Modified residue

494

Phosphothreonine By similarity

Modified residue

495

Phosphothreonine By similarity

Modified residue

497

Phosphothreonine By similarity

Modified residue

501

Phosphothreonine By similarity

Modified residue

604

N6-acetyllysine By similarity

Modified residue

628

N6-acetyllysine By similarity

Modified residue

631

Phosphothreonine; by autocatalysis Potential

Modified residue

638

Phosphothreonine; by autocatalysis By similarity

Modified residue

657

Phosphoserine By similarity

Modified residue

658

Phosphotyrosine By similarity

Natural variations

Natural variant

106

I → V in mutant form UV25. Ref.2

Natural variant

111

S → G in mutant form UV25. Ref.2

Natural variant

240

L → Q in mutant form UV25. Ref.2

Natural variant

339

F → L in mutant form UV25. Ref.2

Experimental info

Sequence conflict

147

D → V in CAA36908. Ref.2

Sequence conflict

147

D → V in CAA36907. Ref.2

Sequence conflict

218

N → T in CAA36908. Ref.2

Sequence conflict

218

N → T in CAA36907. Ref.2

Sequence conflict

277 – 278

AH → LL in CAA36908. Ref.2

Sequence conflict

277 – 278

AH → LL in CAA36907. Ref.2

Sequence conflict

313

V → A in CAA36908. Ref.2

Sequence conflict

313

V → A in CAA36907. Ref.2

Sequence conflict

467

N → D in CAA36908. Ref.2

Sequence conflict

467

N → D in CAA36907. Ref.2

Sequence conflict

472

N → D in CAA36908. Ref.2

Sequence conflict

472

N → D in CAA36907. Ref.2

Sequence conflict

576

Q → H in CAA36908. Ref.2

Sequence conflict

576

Q → H in CAA36907. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P20444-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 394B48C952BB6D50
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FASTA

672

76,852

        10         20         30         40         50         60 
MADVYPANDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC SHCTDFIWGF 

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

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

       190        200        210        220        230        240 
KNLIPMDPNG LSDPYVKLKL IPDPKNESKQ KTKTIRSNLN PQWNESFTFK LKPSDKDRRL 

       250        260        270        280        290        300 
SVEIWDWDRT TRNDFMGSLS FGVSELMKMP ASGWYKAHNQ EEGEYYNVPI PEGDEEGNME 

       310        320        330        340        350        360 
LRQKFEKAKL GPVGNKVISP SEDRKQPSNN 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 YRDLKLNNVM LNSEGHIKIA 

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

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

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

       670 
PQFVHPILQS AV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of mouse protein kinase C (PKC) cDNA from Swiss 3T3 fibroblasts." Rose-John S., Dietrich A., Marks F. Gene 74:465-471(1988) [PubMed: 2469625] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A mutant protein kinase C that can transform fibroblasts." Megidish T., Mazurek N. Nature 342:807-811(1989) [PubMed: 2601739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-106; GLY-111; GLN-240 AND LEU-339. Strain: BALB/c. Tissue: Brain.
[3]	"PICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system." Staudinger J., Zhou J., Burgess R., Elledge S.J., Olson E.N. J. Cell Biol. 128:263-271(1995) [PubMed: 7844141] [Abstract] Cited for: INTERACTION WITH PRKCABP.
[4]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M25811 mRNA. Translation: AAA39934.1. Sequence problems. X52685 mRNA. Translation: CAA36908.1. X52684 mRNA. Translation: CAA36907.1.
IPI	IPI00321446.
PIR	KIMSCA. S07104.
RefSeq	NP_035231.2.
UniGene	Mm.222178
3D structure databases
HSSP	HSSP built from PDB template 1DSY based on UniProtKB P05696.
SMR	P20444. Positions 94-158, 95-159, 156-287, 157-288, 336-666.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:532N.
STRING	P20444.
PTM databases
PhosphoSite	P20444.
Proteomic databases
PRIDE	P20444.
Genome annotation databases
Ensembl	ENSMUST00000059595; ENSMUSP00000062392; ENSMUSG00000050965; Mus musculus. [Genome view]
GeneID	18750.
KEGG	mmu:18750.
Organism-specific databases
MGI	MGI:97595. Prkca.
Phylogenomic databases
HOGENOM	P20444.
HOVERGEN	P20444.
Enzyme and pathway databases
BRENDA	2.7.11.13. 244.
Gene expression databases
ArrayExpress	P20444.
Bgee	P20444.
CleanEx	MM_PRKCA.
Genevestigator	P20444.
GermOnline	ENSMUSG00000050965. Mus musculus.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR000008. C2_Ca-dep. IPR018029. C2_membr_targeting. IPR020477. C2_region. IPR020454. DAG/PE_bd. IPR015745. PKC. IPR017892. Pkinase_C. IPR002219. Prot_Kinase_C-like_PE/DAG_bd. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR014375. Protein_kinase_C_a/b/g. 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.
PRINTS	PR00360. C2DOMAIN. PR00008. DAGPEDOMAIN.
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]
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

KPCA_MOUSE

Accession

Primary (citable) accession number: P20444

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents