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P05128 (KPCG_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein kinase C gamma type

Short name=PKC-gamma
EC=2.7.11.13
Gene names
Name:PRKCG
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length682 AA.
Sequence statusFragment.
Protein existenceEvidence 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. Cytoplasmperinuclear region By similarity. Cell membrane; Peripheral membrane protein By similarity. Cell junctionsynapsesynaptosome By similarity. Cell projectiondendrite 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 682›682Protein kinase C gamma type
PRO_0000055688

Regions

Domain155 – 24591C2
Domain336 – 599264Protein kinase
Domain600 – 67071AGC-kinase C-terminal
Zinc finger20 – 7051Phorbol-ester/DAG-type 1
Zinc finger85 – 13551Phorbol-ester/DAG-type 2
Nucleotide binding342 – 3509ATP By similarity

Sites

Active site4651Proton acceptor By similarity
Metal binding1711Calcium 1; via carbonyl oxygen By similarity
Metal binding1721Calcium 1 By similarity
Metal binding1721Calcium 2 By similarity
Metal binding1781Calcium 2 By similarity
Metal binding2311Calcium 1 By similarity
Metal binding2311Calcium 2 By similarity
Metal binding2321Calcium 2; via carbonyl oxygen By similarity
Metal binding2331Calcium 1 By similarity
Metal binding2331Calcium 2 By similarity
Metal binding2331Calcium 3 By similarity
Metal binding2361Calcium 3 By similarity
Metal binding2371Calcium 3; via carbonyl oxygen By similarity
Metal binding2391Calcium 1 By similarity
Metal binding2391Calcium 3 By similarity
Binding site3651ATP By similarity

Amino acid modifications

Modified residue1801Phosphotyrosine By similarity
Modified residue1821N6-acetyllysine By similarity
Modified residue2351Phosphothreonine; by autocatalysis By similarity
Modified residue2971Phosphotyrosine By similarity
Modified residue3071Phosphoserine By similarity
Modified residue3151Phosphoserine By similarity
Modified residue4991Phosphothreonine; by PDPK1 By similarity
Modified residue5031Phosphothreonine By similarity
Modified residue6331Phosphothreonine; by autocatalysis Potential
Modified residue6401Phosphothreonine; by autocatalysis By similarity
Modified residue6591Phosphothreonine; by autocatalysis By similarity
Modified residue6601Phosphotyrosine; by SYK By similarity
Modified residue6721Phosphoserine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P05128 [UniParc].

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

FASTA68277,156
        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 

« Hide

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.
IPIIPI00685679.
PIRKIBOGC. C24664.
RefSeqNP_001159974.1. NM_001166502.1.
UniGeneBt.12762.

3D structure databases

ProteinModelPortalP05128.
SMRP05128. Positions 21-278.
ModBaseSearch...

Protein-protein interaction databases

STRINGP05128.

Proteomic databases

PRIDEP05128.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID282002.
KEGGbta:282002.

Organism-specific databases

CTD5582.

Phylogenomic databases

eggNOGmaNOG08253.
GeneTreeENSGT00590000082854.
HOVERGENHBG108317.
InParanoidP05128.
OrthoDBEOG40CHGD.
PhylomeDBP05128.

Family and domain databases

InterProIPR000961. 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]
KOK02677.
PfamPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000550. PKC_alpha. 1 hit.
PRINTSPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
SSF56112. Kinase_like. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Entry information

Entry nameKPCG_BOVIN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families