ID KPCG_RAT Reviewed; 697 AA. AC P63319; P05697; Q5FWS3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 170. DE RecName: Full=Protein kinase C gamma type; DE Short=PKC-gamma; DE EC=2.7.11.13; GN Name=Prkcg; Synonyms=Pkcc, Pkcg, Prkcc; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=3387228; DOI=10.1093/nar/16.11.5199; RA Ono Y., Fujii T., Igarashi K., Kikkawa U., Ogita K., Nishizuka Y.; RT "Nucleotide sequences of cDNAs for alpha and gamma subspecies of rat brain RT protein kinase C."; RL Nucleic Acids Res. 16:5199-5200(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3755379; DOI=10.1016/0092-8674(86)90874-3; RA Knopf J.L., Lee M.-H., Sultzman L.A., Kriz R.W., Loomis C.R., Hewick R.M., RA Bell R.M.; RT "Cloning and expression of multiple protein kinase C cDNAs."; RL Cell 46:491-502(1986). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. RX PubMed=2246272; DOI=10.1016/s0021-9258(17)45468-8; RA Chen K.H., Widen S.G., Wilson S.H., Huang K.P.; RT "Characterization of the 5'-flanking region of the rat protein kinase C RT gamma gene."; RL J. Biol. Chem. 265:19961-19965(1990). RN [5] RP FUNCTION. RX PubMed=9287082; RX DOI=10.1002/(sici)1098-1063(1997)7:4<427::aid-hipo8>3.0.co;2-f; RA Krugers H.J., Douma B.R., Andringa G., Bohus B., Korf J., Luiten P.G.; RT "Exposure to chronic psychosocial stress and corticosterone in the rat: RT effects on spatial discrimination learning and hippocampal protein kinase RT Cgamma immunoreactivity."; RL Hippocampus 7:427-436(1997). RN [6] RP FUNCTION IN INFLAMMATORY PAIN, AND SUBCELLULAR LOCATION. RX PubMed=10336135; DOI=10.1016/s0306-4522(98)00314-5; RA Martin W.J., Liu H., Wang H., Malmberg A.B., Basbaum A.I.; RT "Inflammation-induced up-regulation of protein kinase Cgamma RT immunoreactivity in rat spinal cord correlates with enhanced nociceptive RT processing."; RL Neuroscience 88:1267-1274(1999). RN [7] RP FUNCTION IN PHOSPHORYLATION OF GRIA4/GLUR4, INTERACTION WITH GRIA4/GLUR4, RP AND SUBCELLULAR LOCATION. RX PubMed=12471040; DOI=10.1074/jbc.m205587200; RA Correia S.S., Duarte C.B., Faro C.J., Pires E.V., Carvalho A.L.; RT "Protein kinase C gamma associates directly with the GluR4 alpha-amino-3- RT hydroxy-5-methyl-4-isoxazole propionate receptor subunit. Effect on RT receptor phosphorylation."; RL J. Biol. Chem. 278:6307-6313(2003). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=14688616; DOI=10.1097/01.wcb.0000095920.70924.f5; RA Matsumoto S., Shamloo M., Matsumoto E., Isshiki A., Wieloch T.; RT "Protein kinase C-gamma and calcium/calmodulin-dependent protein kinase II- RT alpha are persistently translocated to cell membranes of the rat brain RT during and after middle cerebral artery occlusion."; RL J. Cereb. Blood Flow Metab. 24:54-61(2004). RN [9] RP FUNCTION IN PHOSPHORYLATION OF GRIN1/NMDAR1. RX PubMed=15936117; DOI=10.1016/j.neuint.2005.04.011; RA Sanchez-Perez A.M., Felipo V.; RT "Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially RT phosphorylated by protein kinase C isoforms."; RL Neurochem. Int. 47:84-91(2005). RN [10] RP FUNCTION IN CELL SURVIVAL. RX PubMed=15705736; DOI=10.1124/jpet.104.082735; RA Hamabe W., Fujita R., Ueda H.; RT "Insulin receptor-protein kinase C-gamma signaling mediates inhibition of RT hypoxia-induced necrosis of cortical neurons."; RL J. Pharmacol. Exp. Ther. 313:1027-1034(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-328; SER-330; RP THR-655 AND SER-687, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [12] RP STRUCTURE BY NMR OF 91-172 IN COMPLEX WITH PHORBOL-12,13-DIBUTYRATE, AND RP FUNCTION. RX PubMed=9271501; DOI=10.1021/bi970833a; RA Xu R.X., Pawelczyk T., Xia T.-H., Brown S.C.; RT "NMR structure of a protein kinase C-gamma phorbol-binding domain and study RT of protein-lipid micelle interactions."; RL Biochemistry 36:10709-10717(1997). CC -!- FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)- CC dependent serine/threonine-protein kinase that plays diverse roles in CC neuronal cells and eye tissues, such as regulation of the neuronal CC receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and CC neuronal functions related to sensitivity to opiates, pain and alcohol, CC mediation of synaptic function and cell survival after ischemia, and CC inhibition of gap junction activity after oxidative stress. Binds and CC phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its CC function by increasing plasma membrane-associated GRIA4 expression. In CC primary cerebellar neurons treated with the agonist 3,5- CC dihyidroxyphenylglycine, functions downstream of the metabotropic CC glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor CC which plays a key role in synaptic plasticity, synaptogenesis, CC excitotoxicity, memory acquisition and learning. May be involved in the CC regulation of hippocampal long-term potentiation (LTP), but may be not CC necessary for the process of synaptic plasticity. May be involved in CC desensitization of mu-type opioid receptor-mediated G-protein CC activation in the spinal cord, and may be critical for the development CC and/or maintenance of morphine-induced reinforcing effects in the CC limbic forebrain. May modulate the functionality of mu-type-opioid CC receptors by participating in a signaling pathway which leads to the CC phosphorylation and degradation of opioid receptors. May also CC contributes to chronic morphine-induced changes in nociceptive CC processing. Plays a role in neuropathic pain mechanisms and contributes CC to the maintenance of the allodynia pain produced by peripheral CC inflammation. Plays an important role in initial sensitivity and CC tolerance to ethanol, by mediating the behavioral effects of ethanol as CC well as the effects of this drug on the GABA(A) receptors. During and CC after cerebral ischemia modulate neurotransmission and cell survival in CC synaptic membranes, and is involved in insulin-induced inhibition of CC necrosis, an important mechanism for minimizing ischemic injury. CC Required for the elimination of multiple climbing fibers during CC innervation of Purkinje cells in developing cerebellum. Is activated in CC lens epithelial cells upon hydrogen peroxide treatment, and CC phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of CC GJA1 gap junction plaques and inhibition of gap junction activity which CC could provide a protective effect against oxidative stress. CC Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in CC response to DNA damage. Involved in the phase resetting of the cerebral CC cortex circadian clock during temporally restricted feeding. Stabilizes CC the core clock component BMAL1 by interfering with its ubiquitination, CC thus suppressing its degradation, resulting in phase resetting of the CC cerebral cortex clock (By similarity). {ECO:0000250|UniProtKB:P63318, CC ECO:0000269|PubMed:10336135, ECO:0000269|PubMed:12471040, CC ECO:0000269|PubMed:15705736, ECO:0000269|PubMed:15936117, CC ECO:0000269|PubMed:9271501, ECO:0000269|PubMed:9287082}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.13; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00041}; CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 CC domain. {ECO:0000250|UniProtKB:P05129}; CC -!- ACTIVITY REGULATION: Classical (or conventional) PKCs (PRKCA, PRKCB and CC PRKCG) are activated by calcium and diacylglycerol (DAG) in the CC presence of phosphatidylserine. Three specific sites; Thr-514 CC (activation loop of the kinase domain), Thr-655 (turn motif) and Thr- CC 674 (hydrophobic region), need to be phosphorylated for its full CC activation. CC -!- SUBUNIT: Interacts with GRIA4. Interacts with CDCP1, TP53INP1 and CC p53/TP53 (By similarity). Interacts with BMAL1 (By similarity). CC {ECO:0000250|UniProtKB:P05129, ECO:0000250|UniProtKB:P63318, CC ECO:0000269|PubMed:12471040}. CC -!- INTERACTION: CC P63319; P53667: LIMK1; Xeno; NbExp=3; IntAct=EBI-12598030, EBI-444403; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P63318}. CC Cytoplasm, perinuclear region. Cell membrane CC {ECO:0000269|PubMed:12471040, ECO:0000269|PubMed:14688616}; Peripheral CC membrane protein. Synapse, synaptosome {ECO:0000269|PubMed:14688616}. CC Cell projection, dendrite {ECO:0000269|PubMed:10336135}. CC Note=Translocates to synaptic membranes on stimulation. CC {ECO:0000269|PubMed:14688616}. CC -!- PTM: Autophosphorylation on Thr-674 appears to regulate motor functions CC of junctophilins, JPH3 and JPH4. {ECO:0000250|UniProtKB:P63318}. CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P05129}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. PKC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X07287; CAA30267.1; -; mRNA. DR EMBL; M13707; AAA41874.1; -; mRNA. DR EMBL; BC089226; AAH89226.1; -; mRNA. DR EMBL; M55417; AAA41873.1; -; Genomic_DNA. DR PIR; A05105; KIRTGC. DR RefSeq; NP_036760.1; NM_012628.1. DR PDB; 1TBN; NMR; -; A=91-172. DR PDB; 1TBO; NMR; -; A=91-172. DR PDBsum; 1TBN; -. DR PDBsum; 1TBO; -. DR AlphaFoldDB; P63319; -. DR SMR; P63319; -. DR BioGRID; 246813; 24. DR IntAct; P63319; 2. DR MINT; P63319; -. DR STRING; 10116.ENSRNOP00000071203; -. DR BindingDB; P63319; -. DR ChEMBL; CHEMBL3604; -. DR DrugCentral; P63319; -. DR GlyGen; P63319; 10 sites, 1 O-linked glycan (10 sites). DR iPTMnet; P63319; -. DR PhosphoSitePlus; P63319; -. DR PaxDb; 10116-ENSRNOP00000019825; -. DR Ensembl; ENSRNOT00000080032.2; ENSRNOP00000071203.1; ENSRNOG00000054371.2. DR Ensembl; ENSRNOT00055050273; ENSRNOP00055041368; ENSRNOG00055029017. DR Ensembl; ENSRNOT00060043546; ENSRNOP00060036092; ENSRNOG00060025148. DR Ensembl; ENSRNOT00065053043; ENSRNOP00065043570; ENSRNOG00065030766. DR GeneID; 24681; -. DR KEGG; rno:24681; -. DR UCSC; RGD:3397; rat. DR AGR; RGD:3397; -. DR CTD; 5582; -. DR RGD; 3397; Prkcg. DR eggNOG; KOG0696; Eukaryota. DR GeneTree; ENSGT00940000161219; -. DR HOGENOM; CLU_000288_54_2_1; -. DR InParanoid; P63319; -. DR OMA; DADNCGL; -. DR OrthoDB; 841660at2759; -. DR PhylomeDB; P63319; -. DR TreeFam; TF351133; -. DR Reactome; R-RNO-111933; Calmodulin induced events. DR Reactome; R-RNO-114516; Disinhibition of SNARE formation. DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors. DR Reactome; R-RNO-5099900; WNT5A-dependent internalization of FZD4. DR Reactome; R-RNO-76005; Response to elevated platelet cytosolic Ca2+. DR EvolutionaryTrace; P63319; -. DR PRO; PR:P63319; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000054371; Expressed in frontal cortex and 19 other cell types or tissues. DR GO; GO:0044305; C:calyx of Held; ISO:RGD. DR GO; GO:0005911; C:cell-cell junction; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0030425; C:dendrite; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO. DR GO; GO:0014069; C:postsynaptic density; ISO:RGD. DR GO; GO:0099523; C:presynaptic cytosol; ISO:RGD. DR GO; GO:0097060; C:synaptic membrane; IDA:RGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004698; F:calcium,diacylglycerol-dependent serine/threonine kinase activity; IDA:RGD. DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IDA:RGD. DR GO; GO:0004672; F:protein kinase activity; ISO:RGD. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:RGD. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD. DR GO; GO:0007635; P:chemosensory behavior; ISO:RGD. DR GO; GO:0060384; P:innervation; ISO:RGD. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0007611; P:learning or memory; IEP:RGD. DR GO; GO:0060291; P:long-term synaptic potentiation; IDA:RGD. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB. DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; ISS:UniProtKB. DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:RGD. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB. DR GO; GO:0016310; P:phosphorylation; ISO:RGD. DR GO; GO:0032425; P:positive regulation of mismatch repair; ISO:RGD. DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:RGD. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0050764; P:regulation of phagocytosis; ISO:RGD. DR GO; GO:0032095; P:regulation of response to food; ISS:UniProtKB. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD. DR GO; GO:0043278; P:response to morphine; ISS:UniProtKB. DR GO; GO:0048265; P:response to pain; ISS:UniProtKB. DR GO; GO:1990911; P:response to psychosocial stress; IDA:UniProtKB. DR GO; GO:0009636; P:response to toxic substance; IEP:RGD. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR CDD; cd20833; C1_cPKC_rpt1; 1. DR CDD; cd20836; C1_cPKC_rpt2; 1. DR CDD; cd04026; C2_PKC_alpha_gamma; 1. DR CDD; cd05587; STKc_cPKC; 1. DR Gene3D; 3.30.60.20; -; 2. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR020454; DAG/PE-bd. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR002219; PE/DAG-bd. DR InterPro; IPR017892; Pkinase_C. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR014375; Protein_kinase_C_a/b/g. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR22968:SF27; PROTEIN KINASE C; 1. DR PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1. DR Pfam; PF00130; C1_1; 2. DR Pfam; PF00168; C2; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR PIRSF; PIRSF000550; PKC_alpha; 1. DR PRINTS; PR00360; C2DOMAIN. DR PRINTS; PR00008; DAGPEDOMAIN. DR SMART; SM00109; C1; 2. DR SMART; SM00239; C2; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; 2. DR PROSITE; PS50081; ZF_DAG_PE_2; 2. DR Genevisible; P63319; RN. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Biological rhythms; Calcium; Cell membrane; KW Cell projection; Cytoplasm; Kinase; Membrane; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Synapse; Synaptosome; Transferase; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..697 FT /note="Protein kinase C gamma type" FT /id="PRO_0000055692" FT DOMAIN 157..275 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 351..614 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 615..685 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT ZN_FING 35..85 FT /note="Phorbol-ester/DAG-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT ZN_FING 100..150 FT /note="Phorbol-ester/DAG-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT ACT_SITE 480 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 186 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P63318" FT BINDING 187 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 187 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 193 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 246 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 246 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 247 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 248 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 248 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 248 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 251 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 252 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 254 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 254 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P05129" FT BINDING 357..365 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 380 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 250 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63318" FT MOD_RES 322 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63318" FT MOD_RES 326 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 328 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 330 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 332 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P63318" FT MOD_RES 373 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63318" FT MOD_RES 514 FT /note="Phosphothreonine; by PDPK1" FT /evidence="ECO:0000250|UniProtKB:P63318" FT MOD_RES 648 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 655 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 674 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P63318" FT MOD_RES 675 FT /note="Phosphotyrosine; by SYK" FT /evidence="ECO:0000250" FT MOD_RES 687 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:1TBN" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:1TBN" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:1TBN" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:1TBN" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:1TBN" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:1TBN" FT TURN 140..145 FT /evidence="ECO:0007829|PDB:1TBN" SQ SEQUENCE 697 AA; 78358 MW; E6E2F7A3B93042FF CRC64; MAGLGPGGGD SEGGPRPLFC RKGALRQKVV HEVKSHKFTA RFFKQPTFCS HCTDFIWGIG KQGLQCQVCS FVVHRRCHEF VTFECPGAGK GPQTDDPRNK HKFRLHSYSS PTFCDHCGSL LYGLVHQGMK CSCCEMNVHR RCVRSVPSLC GVDHTERRGR LQLEIRAPTS DEIHITVGEA RNLIPMDPNG LSDPYVKLKL IPDPRNLTKQ KTKTVKATLN PVWNETFVFN LKPGDVERRL SVEVWDWDRT SRNDFMGAMS FGVSELLKAP VDGWYKLLNQ EEGEYYNVPV ADADNCSLLQ KFEACNYPLE LYERVRMGPS SSPIPSPSPS PTDSKRCFFG ASPGRLHISD FSFLMVLGKG SFGKVMLAER RGSDELYAIK ILKKDVIVQD DDVDCTLVEK RVLALGGRGP GGRPHFLTQL HSTFQTPDRL YFVMEYVTGG DLMYHIQQLG KFKEPHAAFY AAEIAIGLFF LHNQGIIYRD LKLDNVMLDA EGHIKITDFG MCKENVFPGS TTRTFCGTPD YIAPEIIAYQ PYGKSVDWWS FGVLLYEMLA GQPPFDGEDE EELFQAIMEQ TVTYPKSLSR EAVAICKGFL TKHPGKRLGS GPDGEPTIRA HGFFRWIDWE RLERLEIAPP FRPRPCGRSG ENFDKFFTRA APALTPPDRL VLASIDQADF QGFTYVNPDF VHPDARSPTS PVPVPVM //