Protein kinase C gamma type - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P63319 (KPCG_RAT)

Last modified November 3, 2009. Version 60. 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 gamma type
      Short name=PKC-gamma
    EC=2.7.11.13

Gene names

Name:	Prkcg
Synonyms:	Pkcc, Pkcg, Prkcc

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	697 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. 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 CDCP1 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.

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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	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	intracellular signaling cascade Non-traceable author statement. Source: RGD learning or memory Inferred from expression pattern. Source: RGD protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro synaptic transmission Non-traceable author statement. Source: RGD
Cellular component	cytosol 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 diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase C activity Inferred from direct assay. Source: RGD 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

Chain

1 – 697

697

Protein kinase C gamma type

PRO_0000055692

Regions

Domain

170 – 260

Domain

351 – 614

264

Protein kinase

Domain

615 – 685

AGC-kinase C-terminal

Zinc finger

35 – 85

Phorbol-ester/DAG-type 1

Zinc finger

100 – 150

Phorbol-ester/DAG-type 2

Nucleotide binding

357 – 365

ATP By similarity

Sites

Active site

480

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

251

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

380

ATP By similarity

Amino acid modifications

Modified residue

195

Phosphotyrosine By similarity

Modified residue

197

N6-acetyllysine By similarity

Modified residue

312

Phosphotyrosine By similarity

Modified residue

322

Phosphoserine By similarity

Modified residue

330

Phosphoserine By similarity

Modified residue

514

Phosphothreonine By similarity

Modified residue

518

Phosphothreonine By similarity

Modified residue

648

Phosphothreonine; by autocatalysis Potential

Modified residue

655

Phosphothreonine; by autocatalysis Potential

Modified residue

687

Phosphoserine By similarity

Secondary structure

697

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P63319-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: E6E2F7A3B93042FF
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FASTA

697

78,358

        10         20         30         40         50         60 
MAGLGPGGGD SEGGPRPLFC RKGALRQKVV HEVKSHKFTA RFFKQPTFCS HCTDFIWGIG 

        70         80         90        100        110        120 
KQGLQCQVCS FVVHRRCHEF VTFECPGAGK GPQTDDPRNK HKFRLHSYSS PTFCDHCGSL 

       130        140        150        160        170        180 
LYGLVHQGMK CSCCEMNVHR RCVRSVPSLC GVDHTERRGR LQLEIRAPTS DEIHITVGEA 

       190        200        210        220        230        240 
RNLIPMDPNG LSDPYVKLKL IPDPRNLTKQ KTKTVKATLN PVWNETFVFN LKPGDVERRL 

       250        260        270        280        290        300 
SVEVWDWDRT SRNDFMGAMS FGVSELLKAP VDGWYKLLNQ EEGEYYNVPV ADADNCSLLQ 

       310        320        330        340        350        360 
KFEACNYPLE LYERVRMGPS SSPIPSPSPS PTDSKRCFFG ASPGRLHISD FSFLMVLGKG 

       370        380        390        400        410        420 
SFGKVMLAER RGSDELYAIK ILKKDVIVQD DDVDCTLVEK RVLALGGRGP GGRPHFLTQL 

       430        440        450        460        470        480 
HSTFQTPDRL YFVMEYVTGG DLMYHIQQLG KFKEPHAAFY AAEIAIGLFF LHNQGIIYRD 

       490        500        510        520        530        540 
LKLDNVMLDA EGHIKITDFG MCKENVFPGS TTRTFCGTPD YIAPEIIAYQ PYGKSVDWWS 

       550        560        570        580        590        600 
FGVLLYEMLA GQPPFDGEDE EELFQAIMEQ TVTYPKSLSR EAVAICKGFL TKHPGKRLGS 

       610        620        630        640        650        660 
GPDGEPTIRA HGFFRWIDWE RLERLEIAPP FRPRPCGRSG ENFDKFFTRA APALTPPDRL 

       670        680        690 
VLASIDQADF QGFTYVNPDF VHPDARSPTS PVPVPVM

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References

	« Hide 'large scale' referencesShow 'large scale' 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]	"Cloning and expression of multiple protein kinase C cDNAs." Knopf J.L., Lee M.-H., Sultzman L.A., Kriz R.W., Loomis C.R., Hewick R.M., Bell R.M. Cell 46:491-502(1986) [PubMed: 3755379] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"Characterization of the 5'-flanking region of the rat protein kinase C gamma gene." Chen K.H., Widen S.G., Wilson S.H., Huang K.P. J. Biol. Chem. 265:19961-19965(1990) [PubMed: 2246272] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
[5]	"NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions." Xu R.X., Pawelczyk T., Xia T.-H., Brown S.C. Biochemistry 36:10709-10717(1997) [PubMed: 9271501] [Abstract] Cited for: STRUCTURE BY NMR OF 91-172.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X07287 mRNA. Translation: CAA30267.1.
M13707 mRNA. Translation: AAA41874.1.
BC089226 mRNA. Translation: AAH89226.1.
M55417 Genomic DNA. Translation: AAA41873.1.

IPI

IPI00201797.

PIR

KIRTGC. A05105.

RefSeq

NP_036760.1.

UniGene

Rn.9747

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TBN	NMR	-	A	91-172	[»]
1TBO	NMR	-	A	91-172	[»]

SMR

P63319. Positions 93-158, 348-683.

ModBase

Search...

Protein-protein interaction databases

STRING

P63319.

PTM databases

PhosphoSite

P63319.

Proteomic databases

PRIDE

P63319.

Genome annotation databases

Ensembl

ENSRNOT00000019825; ENSRNOP00000019825; ENSRNOG00000014688; Rattus norvegicus. [Genome view]

GeneID

24681.

KEGG

rno:24681.

UCSC

NM_012628. rat.

Organism-specific databases

CTD

24681.

RGD

3397. Prkcc.

Phylogenomic databases

HOVERGEN

P63319.

OMA

ICKGFLT.

Enzyme and pathway databases

BRENDA

2.7.11.13. 248.

Gene expression databases

ArrayExpress

P63319.

Genevestigator

P63319.

GermOnline

ENSRNOG00000014688. 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...

Other Resources

NextBio

604095.

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Entry information

Entry name

KPCG_RAT

Accession

Primary (citable) accession number: P63319
Secondary accession number(s): P05697, Q5FWS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	November 3, 2009
This is version 60 of the entry and version 1 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