EKS-HOS-00178
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00178
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
AGC/PKC454.18.2E-136351614264
StatusReviewed
Ensembl ProteinENSP00000263431
UniProt AccessionP05129;
Protein NameProtein kinase C gamma type
Protein Synonyms/Alias PKC-gamma;
Gene NamePRKCG
Gene Synonyms/Alias PRKCG; PKCG;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000126583ENSP00000387919ENST00000419486
ENSG00000126583ENSP00000471271ENST00000474397
ENSG00000126583ENSP00000471544ENST00000479081
ENSG00000126583ENSP00000440541ENST00000536044
ENSG00000126583ENSP00000263431ENST00000263431
ENSG00000126583ENSP00000438090ENST00000542049
ENSG00000126583ENSP00000443493ENST00000540413
OrganismHomo sapiens
Functional DescriptionCalcium-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). Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage.
Protein Length697
Protein Sequence
(FASTA)
MAGLGPGVGD SEGGPRPLFC RKGALRQKVV HEVKSHKFTA RFFKQPTFCS HCTDFIWGIG 60
KQGLQCQVCS FVVHRRCHEF VTFECPGAGK GPQTDDPRNK HKFRLHSYSS PTFCDHCGSL 120
LYGLVHQGMK CSCCEMNVHR RCVRSVPSLC GVDHTERRGR LQLEIRAPTA DEIHVTVGEA 180
RNLIPMDPNG LSDPYVKLKL IPDPRNLTKQ KTRTVKATLN PVWNETFVFN LKPGDVERRL 240
SVEVWDWDRT SRNDFMGAMS FGVSELLKAP VDGWYKLLNQ EEGEYYNVPV ADADNCSLLQ 300
KFEACNYPLE LYERVRMGPS SSPIPSPSPS PTDPKRCFFG ASPGRLHISD FSFLMVLGKG 360
SFGKVMLAER RGSDELYAIK ILKKDVIVQD DDVDCTLVEK RVLALGGRGP GGRPHFLTQL 420
HSTFQTPDRL YFVMEYVTGG DLMYHIQQLG KFKEPHAAFY AAEIAIGLFF LHNQGIIYRD 480
LKLDNVMLDA EGHIKITDFG MCKENVFPGT TTRTFCGTPD YIAPEIIAYQ PYGKSVDWWS 540
FGVLLYEMLA GQPPFDGEDE EELFQAIMEQ TVTYPKSLSR EAVAICKGFL TKHPGKRLGS 600
GPDGEPTIRA HGFFRWIDWE RLERLEIPPP FRPRPCGRSG ENFDKFFTRA APALTPPDRL 660
VLASIDQADF QGFTYVNPDF VHPDARSPTS PVPVPVM 697
Nucleotide Sequence
(FASTA)
ATGGCTGGTC TGGGCCCCGG CGTAGGCGAT TCAGAGGGGG GACCCCGGCC CCTGTTTTGC 60
AGAAAGGGGG CCCTGAGGCA GAAGGTGGTC CACGAAGTCA AGAGCCACAA GTTCACCGCT 120
CGCTTCTTCA AGCAGCCCAC CTTCTGCAGC CACTGCACCG ACTTCATCTG GGGTATCGGA 180
AAGCAGGGCC TGCAATGTCA AGTCTGCAGC TTTGTGGTTC ATCGACGATG CCACGAATTT 240
GTGACCTTCG AGTGTCCAGG CGCTGGGAAG GGCCCCCAGA CGGACGACCC CCGGAACAAA 300
CACAAGTTCC GCCTGCATAG CTACAGCAGC CCCACCTTCT GCGACCACTG TGGCTCCCTC 360
CTCTACGGGC TTGTGCACCA GGGCATGAAA TGCTCCTGCT GCGAGATGAA CGTGCACCGG 420
CGCTGTGTGC GTAGCGTGCC CTCCCTGTGC GGTGTGGACC ACACCGAGCG CCGCGGGCGC 480
CTGCAGCTGG AGATCCGGGC TCCCACAGCA GATGAGATCC ACGTAACTGT TGGCGAGGCC 540
CGTAACCTAA TTCCTATGGA CCCCAATGGT CTCTCTGATC CCTATGTGAA ACTGAAGCTC 600
ATCCCAGACC CTCGGAACCT GACGAAACAG AAGACCCGAA CGGTGAAAGC CACGCTAAAC 660
CCTGTGTGGA ATGAGACCTT TGTGTTCAAC CTGAAGCCAG GGGATGTGGA GCGCCGGCTC 720
AGCGTGGAGG TGTGGGACTG GGACCGGACC TCCCGCAACG ACTTCATGGG GGCCATGTCC 780
TTTGGCGTCT CGGAGCTGCT CAAGGCGCCC GTGGATGGCT GGTACAAGTT ACTGAACCAG 840
GAGGAGGGCG AGTATTACAA TGTGCCGGTG GCCGATGCTG ACAACTGCAG CCTCCTCCAG 900
AAGTTTGAGG CTTGTAACTA CCCCCTGGAA TTGTATGAGC GGGTGCGGAT GGGCCCCTCT 960
TCCTCTCCCA TCCCCTCCCC TTCCCCTAGT CCCACCGACC CCAAGCGCTG CTTCTTCGGG 1020
GCGAGTCCAG GACGCCTGCA CATCTCCGAC TTCAGCTTCC TCATGGTTCT AGGAAAAGGC 1080
AGTTTTGGGA AGGTGATGCT GGCCGAGCGC AGGGGCTCTG ATGAGCTCTA CGCCATCAAG 1140
ATCTTGAAAA AGGACGTGAT CGTCCAGGAC GACGATGTGG ACTGCACGCT GGTGGAGAAA 1200
CGTGTGCTGG CGCTGGGGGG CCGGGGTCCT GGCGGCCGGC CCCACTTCCT CACCCAGCTC 1260
CACTCCACCT TCCAGACCCC GGACCGCCTG TATTTCGTGA TGGAGTACGT CACCGGGGGA 1320
GACTTGATGT ACCACATTCA ACAGCTGGGC AAGTTTAAGG AGCCCCATGC AGCGTTCTAC 1380
GCGGCAGAAA TCGCTATCGG CCTCTTCTTC CTTCACAATC AGGGCATCAT CTACAGGGAC 1440
CTGAAGCTGG ACAATGTGAT GCTGGATGCT GAGGGACACA TCAAGATCAC TGACTTTGGC 1500
ATGTGTAAGG AGAACGTCTT CCCCGGGACG ACAACCCGCA CCTTCTGCGG GACCCCGGAC 1560
TACATAGCCC CGGAGATCAT TGCCTACCAG CCCTATGGGA AGTCTGTCGA TTGGTGGTCC 1620
TTTGGAGTTC TGCTGTATGA GATGTTGGCA GGACAGCCTC CCTTCGATGG GGAGGACGAG 1680
GAGGAGCTGT TTCAGGCCAT CATGGAACAA ACTGTCACCT ACCCCAAGTC GCTTTCCCGG 1740
GAAGCCGTGG CCATCTGCAA GGGGTTCCTG ACCAAGCACC CAGGGAAGCG CCTGGGCTCA 1800
GGGCCTGATG GGGAACCTAC CATCCGTGCA CATGGCTTTT TCCGCTGGAT TGACTGGGAG 1860
CGGCTGGAAC GATTGGAGAT CCCGCCTCCT TTCAGACCCC GCCCGTGTGG CCGCAGCGGC 1920
GAGAACTTTG ACAAGTTCTT CACGCGGGCG GCGCCAGCGC TGACCCCTCC AGACCGCCTA 1980
GTCCTGGCCA GCATCGACCA GGCCGATTTC CAGGGCTTCA CCTACGTGAA CCCCGACTTC 2040
GTGCACCCGG ATGCCCGCAG CCCCACCAGC CCAGTGCCTG TGCCCGTCAT GTAA 2094
Domain Profile
S: 1     fellkvlGkGsfgkvllaelkktdelyaikvlkkdvvlqdddveltlvekrvlal.....  55
         f++l+vlGkGsfgkv+lae++++delyaik+lkkdv++qdddv++tlvekrvlal     
Q: 351   FSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALggrgp  410
         89*****************************************************66666
S: 56    askkpflvqlfscfqtedrlffvleyvnGGdlmfhiqkarklkeerarfyaaeiilalkf  115
           +++fl+ql+s+fqt drl+fv+eyv+GGdlm+hiq+ +k+ke++a+fyaaei+++l+f
Q: 411   GGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFF  470
         67889*******************************************************
S: 116   lhekgiiyrdlkldnvlldaeGhikladfGlckeeilegkttstfcGtPdyiaPeilkee  175
         lh++giiyrdlkldnv+ldaeGhik++dfG+cke+++ g+tt+tfcGtPdyiaPei++++
Q: 471   LHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQ  530
         ************************************************************
S: 176   eygksvdwwalGvllyemlagqsPfegededelfesilekevlyPkslskeaveilkgll  235
         +ygksvdww++Gvllyemlagq+Pf+gede+elf++i+e++v+yPksls+eav+i+kg+l
Q: 531   PYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFL  590
         ************************************************************
S: 236   tkdpekrlGvkeegeedikehaff  259
         tk+p krlG+ ++ge +i++h ff
Q: 591   TKHPGKRLGSGPDGEPTIRAHGFF  614
         ***********************8
Domain Sequence
(FASTA)
FSFLMVLGKG SFGKVMLAER RGSDELYAIK ILKKDVIVQD DDVDCTLVEK RVLALGGRGP 60
GGRPHFLTQL HSTFQTPDRL YFVMEYVTGG DLMYHIQQLG KFKEPHAAFY AAEIAIGLFF 120
LHNQGIIYRD LKLDNVMLDA EGHIKITDFG MCKENVFPGT TTRTFCGTPD YIAPEIIAYQ 180
PYGKSVDWWS FGVLLYEMLA GQPPFDGEDE EELFQAIMEQ TVTYPKSLSR EAVAICKGFL 240
TKHPGKRLGS GPDGEPTIRA HGFF 264
Keyword3D-structure; Acetylation; ATP-binding; Calcium; Cell junction; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Disease mutation; Kinase; Membrane; Metal-binding; Neurodegeneration; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Spinocerebellar ataxia; Synapse; Synaptosome; Transferase; Zinc; Zinc-finger.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Equus caballus"; ?>Felis catus"; ?>Gorilla gorilla"; ?>Ictidomys tridecemlineatus"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Nomascus leucogenys"; ?>Oryctolagus cuniculus"; ?>Otolemur garnettii"; ?>Pongo abelii"; ?>Rattus norvegicus"; ?>Sus scrofa"; ?>Tursiops truncatus"; ?>
EKS-AIM-00164
EKS-ANC-00163
EKS-BOT-00172
EKS-CAJ-00176
EKS-CAF-00179
EKS-CAP-00172
EKS-EQC-00169
EKS-FEC-00162
EKS-GOG-00170
EKS-ICT-00167
EKS-LOA-00170
EKS-MAM-00170
EKS-MUM-00177
EKS-MUP-00176
EKS-NOL-00165
EKS-ORC-00161
EKS-OTG-00178
EKS-POA-00170
EKS-RAN-00167
EKS-SUS-00147
EKS-TUT-00154
Gene Ontology
GO:0030054; C:cell junction
GO:0005829; C:cytosol
GO:0030425; C:dendrite
GO:0005634; C:nucleus
GO:0048471; C:perinuclear region of cytoplasm
GO:0005886; C:plasma membrane
GO:0097060; C:synaptic membrane
GO:0005524; F:ATP binding
GO:0004697; F:protein kinase C activity
GO:0008270; F:zinc ion binding
GO:0007202; P:activation of phospholipase C activity
GO:0008219; P:cell death
GO:0007635; P:chemosensory behavior
GO:0007173; P:epidermal growth factor receptor signaling pathway
GO:0008543; P:fibroblast growth factor receptor signaling pathway
GO:0060384; P:innervation
GO:0035556; P:intracellular signal transduction
GO:0007611; P:learning or memory
GO:0043524; P:negative regulation of neuron apoptotic process
GO:0042177; P:negative regulation of protein catabolic process
GO:0031397; P:negative regulation of protein ubiquitination
GO:0048011; P:nerve growth factor receptor signaling pathway
GO:0030168; P:platelet activation
GO:0032425; P:positive regulation of mismatch repair
GO:0043278; P:response to morphine
GO:0048265; P:response to pain
GO:0007268; P:synaptic transmission
KEGG
hsa:5582;
InterPros
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.
IPR002290; Ser/Thr_dual-sp_kinase_dom.
IPR008271; Ser/Thr_kinase_AS.
Pfam
PF00130; C1_1; 2.
PF00168; C2; 1.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
SMARTs
SM00109; C1; 2.
SM00239; C2; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
Prosites
PS51285; AGC_KINASE_CTER; 1.
PS50004; C2; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS00479; ZF_DAG_PE_1; 2.
PS50081; ZF_DAG_PE_2; 2.
Prints
PR00360; C2DOMAIN.
PR00008; DAGPEDOMAIN.
Created Date20-Feb-2013