Protein kinase C gamma type - Bos taurus (Bovine)

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P05128 (KPCG_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 119. 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

Gene names

Name:

PRKCG

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	682 AA.
Sequence status	Fragment.
Protein existence	Evidence at transcript 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. 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 By similarity.
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-499 (activation loop of the kinase domain), Thr-640 (turn motif) and Thr-659 (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.
Post-translational modification	Autophosphorylation on Thr-659 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 Reference 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 – 682

›682

Protein kinase C gamma type

PRO_0000055688

Regions

Domain

155 – 245

Domain

336 – 599

264

Protein kinase

Domain

600 – 670

AGC-kinase C-terminal

Zinc finger

20 – 70

Phorbol-ester/DAG-type 1

Zinc finger

85 – 135

Phorbol-ester/DAG-type 2

Nucleotide binding

342 – 350

ATP By similarity

Sites

Active site

465

Proton acceptor By similarity

Metal binding

171

Calcium 1; via carbonyl oxygen By similarity

Metal binding

172

Calcium 1 By similarity

Metal binding

172

Calcium 2 By similarity

Metal binding

178

Calcium 2 By similarity

Metal binding

231

Calcium 1 By similarity

Metal binding

231

Calcium 2 By similarity

Metal binding

232

Calcium 2; via carbonyl oxygen By similarity

Metal binding

233

Calcium 1 By similarity

Metal binding

233

Calcium 2 By similarity

Metal binding

233

Calcium 3 By similarity

Metal binding

236

Calcium 3 By similarity

Metal binding

237

Calcium 3; via carbonyl oxygen By similarity

Metal binding

239

Calcium 1 By similarity

Metal binding

239

Calcium 3 By similarity

Binding site

365

ATP By similarity

Amino acid modifications

Modified residue

180

Phosphotyrosine By similarity

Modified residue

182

N6-acetyllysine By similarity

Modified residue

235

Phosphothreonine; by autocatalysis By similarity

Modified residue

297

Phosphotyrosine By similarity

Modified residue

307

Phosphoserine By similarity

Modified residue

315

Phosphoserine By similarity

Modified residue

499

Phosphothreonine; by PDPK1 By similarity

Modified residue

503

Phosphothreonine By similarity

Modified residue

633

Phosphothreonine; by autocatalysis Potential

Modified residue

640

Phosphothreonine; by autocatalysis By similarity

Modified residue

659

Phosphothreonine; by autocatalysis By similarity

Modified residue

660

Phosphotyrosine; by SYK By similarity

Modified residue

672

Phosphoserine By similarity

Experimental info

Non-terminal residue

Sequences

Sequence

Length

Mass (Da)

Tools

P05128 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 20392D11188C731C
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FASTA

682

77,156

        10         20         30         40         50         60 
RPLFCRKGAL RQKVVHEVKS HKFTARFFKQ PTFCSHCTDF IWGIGKQGLQ CQVCSFVVHR 

        70         80         90        100        110        120 
RCHEFVTFEC PGAGKGPQTD DPRNKHKFRL HSYSSPTFCD HCGSLLYGLV HQGMKCSCCE 

       130        140        150        160        170        180 
MNVHRRCVRS VPSLCGVDHT ERRGRLQLEI RAPTSDEIHV TVGEARNLIP MDPNGLSDPY 

       190        200        210        220        230        240 
VKLKLIPDPR NLTKQKTRTV KATLNPVWNE TFVFNLKPGD VERRLSVEVW DWDRTSRNDF 

       250        260        270        280        290        300 
MGAMSFGVSE LLKAPVDGWY KLLNQEEGEY YNVPVADADN CNLLQKFEAC NYPLELYERV 

       310        320        330        340        350        360 
RTGPSSSPIP SPSPSPTDSK RCFFGASPGR LHISDFSFLM VLGKGSFGKV MLAERRGSDE 

       370        380        390        400        410        420 
LYAIKILKKD VIVQDDDVDC TLVEKRVLAL GGRGPGGRPH FLTQLHSTFQ TPDRLYFVME 

       430        440        450        460        470        480 
YVTGGDLMYH IQQLGKFKEP HAAFYAAEIA IGLFFLHNQG IIYRDLKLDN VMLDAEGHIK 

       490        500        510        520        530        540 
ITDFGMCKEN VFPGSTTRTF CGTPDYIAPE IIAYQPYGKS VDWWSFGVLL YEMLAGQPPF 

       550        560        570        580        590        600 
DGEDEEELFQ AIMEQTVTYP KSLSREAVAI CKGFLTKHPA KRLGSGPDGE PTIRAHGFFR 

       610        620        630        640        650        660 
WIDWDRLERL EIAPPFRPRP CGRSGENFDK FFTRAAPALT PPDRLVLASI DQAEFQGFTY 

       670        680 
VNPDFVHPDA RSPISPTPVP VM

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References

[1]	"Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways." Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., Waterfield M.D., Francke U., Ullrich A. Science 233:859-866(1986) [PubMed: 3755548] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M13976 mRNA. Translation: AAA30704.1.
IPI	IPI00685679.
PIR	KIBOGC. C24664.
RefSeq	NP_001159974.1. NM_001166502.1.
UniGene	Bt.12762.
3D structure databases
ProteinModelPortal	P05128.
SMR	P05128. Positions 21-278.
ModBase	Search...
Protein-protein interaction databases
STRING	P05128.
Proteomic databases
PRIDE	P05128.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	282002.
KEGG	bta:282002.
Organism-specific databases
CTD	5582.
Phylogenomic databases
eggNOG	maNOG08253.
GeneTree	ENSGT00590000082854.
HOVERGEN	HBG108317.
InParanoid	P05128.
OrthoDB	EOG40CHGD.
PhylomeDB	P05128.
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]
KO	K02677.
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_BOVIN

Accession

Primary (citable) accession number: P05128

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	January 25, 2012
This is version 119 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents