Protein kinase C gamma type - Oryctolagus cuniculus (Rabbit)

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P10829 (KPCG_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 112. History...

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

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein kinase C gamma type
Short name=PKC-gamma
EC=2.7.11.13

Alternative name(s):
PKC-delta

Gene names

Name:

PRKCG

Organism

Oryctolagus cuniculus (Rabbit) [Complete proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	697 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum By similarity. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Ref.2
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.
Enzyme regulation	Classical (or conventional) PKCs (PRKCA, PRKCB and PRKCG) are activated by calcium and diacylglycerol (DAG) in the presence of phosphatidylserine. Three specific sites; Thr-514 (activation loop of the kinase domain), Thr-655 (turn motif) and Thr-674 (hydrophobic region), need to be phosphorylated for its full activation.
Subunit structure	Interacts with CDCP1 and GRIA4 By similarity.
Subcellular location	Cytoplasm By similarity. Cytoplasm › perinuclear region By similarity. Cell membrane; Peripheral membrane protein By similarity. Cell junction › synapse › synaptosome By similarity. Cell projection › dendrite By similarity. Note: Translocates to synaptic membranes on stimulation By similarity.
Tissue specificity	Expressed specifically in brain. Ref.1
Induction	Activated by hydrogen peroxide. Ref.2
Post-translational modification	Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4 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
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Membrane Synapse Synaptosome
Domain	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	Complete proteome
Gene Ontology (GO)
Biological process	intracellular signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-KW synaptosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase C activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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_0000055691

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

250

Phosphothreonine; by autocatalysis 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 PDPK1 By similarity

Modified residue

518

Phosphothreonine By similarity

Modified residue

648

Phosphothreonine; by autocatalysis By similarity

Modified residue

655

Phosphothreonine; by autocatalysis Potential

Modified residue

674

Phosphothreonine; by autocatalysis By similarity

Modified residue

675

Phosphotyrosine; by SYK By similarity

Modified residue

687

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P10829 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 925D22221F78E5BF
Show »

FASTA

697

78,372

        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 RCVRTVPSLC GVDHTERRGR LQLEIRAPTS DEIHVTVGEA 

       190        200        210        220        230        240 
RNLIPMDPNG LSDPYVKLKL IPDPRNLTKQ KTRTVKATLN 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 MCKENVFPGT 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 APAVTPPDRL 

       670        680        690 
VLASIDQADF QGFTYVNPDF VHPDARSPSS PVPVPVM

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References

[1]	"A fourth type of rabbit protein kinase C." Ohno S., Kawasaki H., Konno Y., Inagaki M., Hidaka H., Suzuki K. Biochemistry 27:2083-2087(1988) [PubMed: 2837282] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"Oxidative activation of protein kinase Cgamma through the C1 domain. Effects on gap junctions." Lin D., Takemoto D.J. J. Biol. Chem. 280:13682-13693(2005) [PubMed: 15642736] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF GJA1/CX43, INDUCTION BY HYDROGEN PEROXIDE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M19338 mRNA. Translation: AAA31449.1.
PIR	KIRBGC. A28708.
RefSeq	NP_001075742.1. NM_001082273.1.
UniGene	Ocu.1950.
3D structure databases
ProteinModelPortal	P10829.
SMR	P10829. Positions 36-293.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1205863.
STRING	P10829.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100009102.
Organism-specific databases
CTD	5582.
Phylogenomic databases
GeneTree	ENSGT00590000082854.
HOVERGEN	HBG108317.
OrthoDB	EOG40CHGD.
Enzyme and pathway databases
BRENDA	2.7.11.13. 1749.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR020477. C2_dom. IPR018029. C2_membr_targeting. IPR020454. DAG/PE-bd. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR014375. Protein_kinase_C_a/b/g. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
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.
SMART	SM00109. C1. 2 hits. SM00239. C2. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF56112. Kinase_like. 1 hit.
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...

Entry information

Entry name

KPCG_RABIT

Accession

Primary (citable) accession number: P10829

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	January 25, 2012
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents