EKS-RAN-00167
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-RAN-00167
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
AGC/PKC454.12.0E-136351614264
StatusReviewed
Ensembl ProteinENSRNOP00000019825
UniProt AccessionP63319; P05697; Q5FWS3;
Protein NameProtein kinase C gamma type
Protein Synonyms/Alias PKC-gamma;
Gene NamePrkcg
Gene Synonyms/Alias Prkcg; Pkcc, Pkcg, Prkcc;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSRNOG00000014688ENSRNOP00000019825ENSRNOT00000019825
OrganismRattus norvegicus
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. Phosphorylates p53/TP53 and promotes p53/TP53- dependent apoptosis in response to DNA damage (By similarity).
Protein Length697
Protein Sequence
(FASTA)
MAGLGPGGGD SEGGPRPLFC RKGALRQKVV HEVKSHKFTA RFFKQPTFCS HCTDFIWGIG 60
KQGLQCQVCS FVVHRRCHEF VTFECPGAGK GPQTDDPRNK HKFRLHSYSS PTFCDHCGSL 120
LYGLVHQGMK CSCCEMNVHR RCVRSVPSLC GVDHTERRGR LQLEIRAPTS DEIHITVGEA 180
RNLIPMDPNG LSDPYVKLKL IPDPRNLTKQ KTKTVKATLN PVWNETFVFN LKPGDVERRL 240
SVEVWDWDRT SRNDFMGAMS FGVSELLKAP VDGWYKLLNQ EEGEYYNVPV ADADNCSLLQ 300
KFEACNYPLE LYERVRMGPS SSPIPSPSPS PTDSKRCFFG ASPGRLHISD FSFLMVLGKG 360
SFGKVMLAER RGSDELYAIK ILKKDVIVQD DDVDCTLVEK RVLALGGRGP GGRPHFLTQL 420
HSTFQTPDRL YFVMEYVTGG DLMYHIQQLG KFKEPHAAFY AAEIAIGLFF LHNQGIIYRD 480
LKLDNVMLDA EGHIKITDFG MCKENVFPGS TTRTFCGTPD YIAPEIIAYQ PYGKSVDWWS 540
FGVLLYEMLA GQPPFDGEDE EELFQAIMEQ TVTYPKSLSR EAVAICKGFL TKHPGKRLGS 600
GPDGEPTIRA HGFFRWIDWE RLERLEIAPP FRPRPCGRSG ENFDKFFTRA APALTPPDRL 660
VLASIDQADF QGFTYVNPDF VHPDARSPTS PVPVPVM 697
Nucleotide Sequence
(FASTA)
ATGGCGGGTC TGGGTCCTGG CGGGGGCGAC TCAGAAGGGG GACCCCGACC CCTGTTTTGC 60
AGAAAGGGGG CGCTGAGGCA GAAGGTGGTC CACGAGGTGA AGAGCCACAA GTTCACCGCT 120
CGTTTCTTCA AGCAGCCAAC CTTCTGCAGT CACTGTACCG ACTTCATCTG GGGCATTGGA 180
AAGCAGGGCC TGCAATGTCA AGTCTGCAGC TTTGTGGTTC ACCGCCGATG CCACGAATTT 240
GTGACCTTCG AGTGTCCAGG CGCTGGAAAG GGCCCCCAGA CGGACGACCC TCGCAACAAG 300
CACAAGTTCC GTCTGCACAG CTACAGCAGT CCCACCTTCT GCGACCACTG TGGTTCCCTC 360
CTCTACGGGC TGGTGCACCA GGGCATGAAA TGTTCCTGTT GCGAAATGAA TGTGCACCGA 420
CGCTGTGTGC GCAGCGTGCC CTCCCTTTGC GGCGTGGACC ATACAGAGCG CCGTGGACGT 480
CTGCAACTGG AAATCCGGGC TCCCACATCA GATGAGATCC ATATTACTGT GGGTGAGGCC 540
CGGAACCTCA TTCCTATGGA CCCCAATGGC CTGTCTGATC CCTATGTGAA ACTGAAGCTC 600
ATCCCGGACC CTCGGAACCT GACAAAACAG AAGACAAAGA CCGTGAAAGC CACACTGAAT 660
CCCGTGTGGA ACGAGACCTT CGTGTTCAAC CTGAAGCCGG GGGATGTGGA GCGCCGGCTC 720
AGTGTGGAGG TGTGGGATTG GGATAGGACA TCCCGAAATG ACTTCATGGG TGCCATGTCC 780
TTTGGTGTCT CAGAGCTACT CAAGGCTCCT GTGGATGGAT GGTACAAGTT ACTGAACCAG 840
GAGGAGGGCG AGTATTACAA TGTACCGGTG GCCGATGCTG ACAACTGCAG CCTCCTCCAG 900
AAGTTTGAGG CCTGTAATTA CCCCTTGGAA TTGTATGAGA GAGTGCGGAT GGGCCCCTCT 960
TCCTCTCCCA TTCCTTCTCC ATCCCCCAGT CCCACGGACT CCAAGAGATG CTTCTTCGGT 1020
GCCAGCCCAG GACGCCTGCA TATCTCTGAC TTCAGCTTCC TCATGGTTCT AGGGAAAGGC 1080
AGTTTTGGGA AGGTGATGCT GGCAGAGCGC AGAGGATCCG ATGAACTCTA TGCCATCAAG 1140
ATACTGAAAA AAGACGTCAT TGTCCAGGAT GATGATGTAG ACTGCACCCT TGTGGAGAAG 1200
CGTGTGCTGG CATTGGGAGG CCGAGGTCCT GGAGGCCGGC CACACTTTCT CACACAACTT 1260
CATTCCACCT TTCAGACTCC GGACCGCCTG TATTTTGTGA TGGAGTACGT CACTGGGGGC 1320
GATTTAATGT ACCACATTCA GCAACTGGGC AAGTTTAAGG AGCCCCACGC AGCATTCTAT 1380
GCCGCGGAAA TCGCCATAGG CCTCTTCTTC CTTCACAACC AGGGCATCAT CTACAGGGAC 1440
CTCAAGTTGG ATAATGTGAT GCTGGATGCT GAAGGACACA TCAAGATCAC AGACTTCGGC 1500
ATGTGTAAAG AGAATGTCTT CCCTGGGTCC ACAACCCGCA CCTTCTGTGG GACCCCAGAC 1560
TACATAGCAC CTGAGATCAT TGCCTATCAG CCCTATGGGA AGTCTGTCGA CTGGTGGTCC 1620
TTTGGAGTCC TGCTGTATGA GATGTTGGCA GGACAGCCAC CCTTTGATGG GGAAGATGAG 1680
GAGGAGCTGT TTCAAGCCAT CATGGAACAA ACTGTCACCT ATCCCAAGTC ACTTTCCCGG 1740
GAAGCTGTGG CCATCTGCAA GGGGTTCCTG ACCAAGCACC CAGGAAAGCG CCTGGGCTCA 1800
GGGCCAGATG GGGAACCCAC CATCCGGGCT CATGGCTTTT TCCGTTGGAT CGATTGGGAG 1860
AGGTTGGAGA GACTGGAAAT TGCGCCTCCT TTTAGACCAC GTCCGTGTGG CCGCAGCGGC 1920
GAAAACTTTG ACAAGTTCTT CACGCGGGCA GCGCCAGCCT TGACCCCGCC AGACCGCTTG 1980
GTCCTAGCCA GCATCGACCA AGCTGATTTC CAGGGCTTTA CTTATGTGAA CCCGGACTTC 2040
GTGCACCCAG ATGCCCGCAG CCCCACAAGC CCTGTGCCTG 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   LHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGSTTRTFCGTPDYIAPEIIAYQ  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 MCKENVFPGS 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; Kinase; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Serine/threonine-protein kinase; 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"; ?>Homo sapiens"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Nomascus leucogenys"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pongo abelii"; ?>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-HOS-00178
EKS-ICT-00167
EKS-LAC-00181
EKS-LOA-00170
EKS-MAM-00170
EKS-MUM-00177
EKS-MUP-00176
EKS-NOL-00165
EKS-ORC-00161
EKS-ORL-00202
EKS-OTG-00178
EKS-POA-00170
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:0004698; F:calcium-dependent protein kinase C activity
GO:0008270; F:zinc ion binding
GO:0007635; P:chemosensory behavior
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:0032425; P:positive regulation of mismatch repair
GO:0046777; P:protein autophosphorylation
GO:0043278; P:response to morphine
GO:0048265; P:response to pain
GO:0007268; P:synaptic transmission
KEGG
rno:24681;
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