Protein kinase C alpha type - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P05696 (KPCA_RAT)

Last modified November 3, 2009. Version 115. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · 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

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

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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. Cell membrane; Peripheral membrane protein. Ref.6
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
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
Technical term	3D-structure
Gene Ontology (GO)
Biological process	aging Inferred from expression pattern. Source: RGD central nervous system neuron axonogenesis Inferred from mutant phenotype. Source: RGD establishment of protein localization Traceable author statement. Source: UniProtKB intracellular signaling cascade Inferred from direct assay. Source: RGD learning or memory Inferred from mutant phenotype. Source: RGD negative regulation of heart contraction Inferred from mutant phenotype. Source: RGD negative regulation of translation Inferred from mutant phenotype. Source: RGD peptidyl-serine phosphorylation Inferred from direct assay. Source: RGD peptidyl-threonine phosphorylation Inferred from direct assay. Source: RGD positive regulation of exocytosis Inferred from mutant phenotype. Source: RGD positive regulation of smooth muscle cell proliferation Inferred from mutant phenotype. Source: RGD positive regulation of synaptogenesis Inferred from mutant phenotype. Source: RGD regulation of receptor-mediated endocytosis Inferred from mutant phenotype. Source: RGD response to antibiotic Inferred from expression pattern. Source: RGD response to corticosterone stimulus Inferred from expression pattern. Source: RGD response to estradiol stimulus Inferred from mutant phenotype. Source: RGD response to ethanol Inferred from mutant phenotype. Source: RGD response to mechanical stimulus Inferred from expression pattern. Source: RGD response to organic cyclic substance Inferred from expression pattern. Source: RGD response to peptide hormone stimulus Inferred from expression pattern. Source: RGD response to reactive oxygen species Inferred from mutant phenotype. Source: RGD response to toxin Inferred from expression pattern. Source: RGD
Cellular component	cytosol Inferred from direct assay. Source: RGD extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane raft Inferred from direct assay. Source: RGD mitochondrion Inferred from direct assay. Source: RGD plasma membrane Inferred from direct assay. Source: RGD protein complex Inferred from direct assay. Source: RGD synaptosome Inferred from direct assay. Source: RGD
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: RGD diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.3 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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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.

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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_0000055682

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

Metal binding

187

Calcium 1

Metal binding

187

Calcium 2

Metal binding

193

Calcium 2

Metal binding

246

Calcium 1

Metal binding

246

Calcium 2

Metal binding

247

Calcium 2; via carbonyl oxygen

Metal binding

248

Calcium 1

Metal binding

248

Calcium 2

Metal binding

248

Calcium 3

Metal binding

252

Calcium 3; via carbonyl oxygen

Metal binding

254

Calcium 1

Metal binding

254

Calcium 3

Binding site

195

Inositol phosphate group

Binding site

245

Inositol phosphate group

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 By similarity

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

Experimental info

Mutagenesis

195

Y → S: Reduced phosphatidylinositol 4,5-bisphosphate recognition and impaired membrane docking. Loss of phosphatidylinositol 4,5-bisphosphate-binding and strong decrease of membrane docking; when associated with A-209, A-211 and A-245. Ref.6

Mutagenesis

209

K → A: Loss of phosphatidylinositol 4,5-bisphosphate-binding and strong decrease of membrane docking; when associated with S-195, A-211 and A-245. Ref.6

Mutagenesis

211

K → A: Loss of phosphatidylinositol 4,5-bisphosphate-binding and strong decrease of membrane docking; when associated with S-195, A-209 and A-245. Ref.6

Mutagenesis

245

W → A: Reduced phosphatidylinositol 4,5-bisphosphate recognition and impaired membrane docking. Loss of phosphatidylinositol 4,5-bisphosphate-binding and strong decrease of membrane docking; when associated with S-195, A-209 and A-211. Ref.6

Secondary structure

672

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P05696-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 94889E7339C17719
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FASTA

672

76,792

        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 KQCVINVPSL CGMDHTEKRG RIYLKAEVTD EKLHVTVRDA 

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

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

       310        320        330        340        350        360 
LRQKFEKAKL GPAGNKVISP 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 YRDLKLDNVM LDSEGHIKIA 

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

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

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

       670 
PQFVHPILQS AV

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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.
[5]	"Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine." Verdaguer N., Corbalan-Garcia S., Ochoa W.F., Fita I., Gomez-Fernandez J.C. EMBO J. 18:6329-6338(1999) [PubMed: 10562545] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 155-293 IN COMPLEX WITH PHOSPHATIDYLSERINE.
[6]	"Structural and mechanistic insights into the association of PKCalpha-C2 domain to PtdIns(4,5)P2." Guerrero-Valero M., Ferrer-Orta C., Querol-Audi J., Marin-Vicente C., Fita I., Gomez-Fernandez J.C., Verdaguer N., Corbalan-Garcia S. Proc. Natl. Acad. Sci. U.S.A. 106:6603-6607(2009) [PubMed: 19346474] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 156-292 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE, MUTAGENESIS OF TYR-195; LYS-209; LYS-211 AND TRP-245, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X07286 mRNA. Translation: CAA30266.1.

IPI

IPI00201792.

PIR

KIRTC. S02248.

UniGene

Rn.207908

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DSY	X-ray	2.60	A	155-293	[»]
3GPE	X-ray	2.00	A	156-292	[»]

SMR

P05696. Positions 94-158, 95-159, 336-666.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05696. 2 interactions.

STRING

P05696.

PTM databases

PhosphoSite

P05696.

Proteomic databases

PRIDE

P05696.

Genome annotation databases

Ensembl

ENSRNOT00000004699; ENSRNOP00000004699; ENSRNOG00000003491; Rattus norvegicus. [Genome view]
ENSRNOT00000055073; ENSRNOP00000051949; ENSRNOG00000003491; Rattus norvegicus. [Genome view]

Organism-specific databases

RGD

3395. Prkca.

Phylogenomic databases

HOVERGEN

P05696.

Enzyme and pathway databases

BRENDA

2.7.11.13. 248.

Gene expression databases

ArrayExpress

P05696.

Genevestigator

P05696.

GermOnline

ENSRNOG00000003491. Rattus norvegicus.

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...

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Entry information

Entry name

KPCA_RAT

Accession

Primary (citable) accession number: P05696

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 115 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

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

Entry information

Relevant documents