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Protein

Protein kinase C gamma type

Gene

PRKCG

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock.By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Ca2+By similarityNote: Binds 3 Ca2+ ions per subunit. The ions are bound to the C2 domain.By similarity

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi171 – 1711Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi172 – 1721Calcium 1By similarity
Metal bindingi172 – 1721Calcium 2By similarity
Metal bindingi178 – 1781Calcium 2By similarity
Metal bindingi231 – 2311Calcium 1By similarity
Metal bindingi231 – 2311Calcium 2By similarity
Metal bindingi232 – 2321Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi233 – 2331Calcium 1By similarity
Metal bindingi233 – 2331Calcium 2By similarity
Metal bindingi233 – 2331Calcium 3By similarity
Metal bindingi236 – 2361Calcium 3By similarity
Metal bindingi237 – 2371Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi239 – 2391Calcium 1By similarity
Metal bindingi239 – 2391Calcium 3By similarity
Binding sitei365 – 3651ATPPROSITE-ProRule annotation
Active sitei465 – 4651Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri20 – 7051Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri85 – 13551Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi342 – 3509ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C gamma type (EC:2.7.11.13)
Short name:
PKC-gamma
Gene namesi
Name:PRKCG
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmperinuclear region By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity
  • Cell junctionsynapsesynaptosome By similarity
  • Cell projectiondendrite By similarity

  • Note: Translocates to synaptic membranes on stimulation.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Synapse, Synaptosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 682›682Protein kinase C gamma typePRO_0000055688Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei235 – 2351Phosphothreonine; by autocatalysisBy similarity
Modified residuei305 – 3051PhosphoserineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei311 – 3111PhosphoserineBy similarity
Modified residuei313 – 3131PhosphoserineBy similarity
Modified residuei315 – 3151PhosphoserineBy similarity
Modified residuei317 – 3171PhosphothreonineBy similarity
Modified residuei358 – 3581PhosphoserineBy similarity
Modified residuei499 – 4991Phosphothreonine; by PDPK1By similarity
Modified residuei633 – 6331Phosphothreonine; by autocatalysisSequence analysis
Modified residuei640 – 6401Phosphothreonine; by autocatalysisBy similarity
Modified residuei659 – 6591Phosphothreonine; by autocatalysisBy similarity
Modified residuei660 – 6601Phosphotyrosine; by SYKBy similarity
Modified residuei672 – 6721PhosphoserineBy similarity

Post-translational modificationi

Autophosphorylation on Thr-659 appears to regulate motor functions of junctophilins, JPH3 and JPH4.By similarity
Ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP05128.
PRIDEiP05128.

Interactioni

Subunit structurei

Interacts with CDCP1 and GRIA4. Interacts with TP53INP1 and p53/TP53. Interacts with ARNTL/BMAL1.By similarity

Protein-protein interaction databases

BioGridi159291. 1 interaction.
STRINGi9913.ENSBTAP00000018020.

Structurei

3D structure databases

ProteinModelPortaliP05128.
SMRiP05128. Positions 21-278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini155 – 24591C2PROSITE-ProRule annotationAdd
BLAST
Domaini336 – 599264Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini600 – 67071AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri20 – 7051Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri85 – 13551Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP05128.
KOiK19663.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000550. PKC_alpha. 1 hit.
PRINTSiPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]

Sequencei

Sequence statusi: Fragment.

P05128-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
RPLFCRKGAL RQKVVHEVKS HKFTARFFKQ PTFCSHCTDF IWGIGKQGLQ
60 70 80 90 100
CQVCSFVVHR RCHEFVTFEC PGAGKGPQTD DPRNKHKFRL HSYSSPTFCD
110 120 130 140 150
HCGSLLYGLV HQGMKCSCCE MNVHRRCVRS VPSLCGVDHT ERRGRLQLEI
160 170 180 190 200
RAPTSDEIHV TVGEARNLIP MDPNGLSDPY VKLKLIPDPR NLTKQKTRTV
210 220 230 240 250
KATLNPVWNE TFVFNLKPGD VERRLSVEVW DWDRTSRNDF MGAMSFGVSE
260 270 280 290 300
LLKAPVDGWY KLLNQEEGEY YNVPVADADN CNLLQKFEAC NYPLELYERV
310 320 330 340 350
RTGPSSSPIP SPSPSPTDSK RCFFGASPGR LHISDFSFLM VLGKGSFGKV
360 370 380 390 400
MLAERRGSDE LYAIKILKKD VIVQDDDVDC TLVEKRVLAL GGRGPGGRPH
410 420 430 440 450
FLTQLHSTFQ TPDRLYFVME YVTGGDLMYH IQQLGKFKEP HAAFYAAEIA
460 470 480 490 500
IGLFFLHNQG IIYRDLKLDN VMLDAEGHIK ITDFGMCKEN VFPGSTTRTF
510 520 530 540 550
CGTPDYIAPE IIAYQPYGKS VDWWSFGVLL YEMLAGQPPF DGEDEEELFQ
560 570 580 590 600
AIMEQTVTYP KSLSREAVAI CKGFLTKHPA KRLGSGPDGE PTIRAHGFFR
610 620 630 640 650
WIDWDRLERL EIAPPFRPRP CGRSGENFDK FFTRAAPALT PPDRLVLASI
660 670 680
DQAEFQGFTY VNPDFVHPDA RSPISPTPVP VM
Length:682
Mass (Da):77,156
Last modified:August 13, 1987 - v1
Checksum:i20392D11188C731C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13976 mRNA. Translation: AAA30704.1.
PIRiC24664. KIBOGC.
RefSeqiNP_001159974.1. NM_001166502.2.
UniGeneiBt.12762.

Genome annotation databases

GeneIDi282002.
KEGGibta:282002.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13976 mRNA. Translation: AAA30704.1.
PIRiC24664. KIBOGC.
RefSeqiNP_001159974.1. NM_001166502.2.
UniGeneiBt.12762.

3D structure databases

ProteinModelPortaliP05128.
SMRiP05128. Positions 21-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159291. 1 interaction.
STRINGi9913.ENSBTAP00000018020.

Proteomic databases

PaxDbiP05128.
PRIDEiP05128.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282002.
KEGGibta:282002.

Organism-specific databases

CTDi5582.

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP05128.
KOiK19663.

Miscellaneous databases

NextBioi20805870.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000550. PKC_alpha. 1 hit.
PRINTSiPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiKPCG_BOVIN
AccessioniPrimary (citable) accession number: P05128
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 11, 2016
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.