KPCB_RAT
ID KPCB_RAT Reviewed; 671 AA.
AC P68403; P04410; P04411;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein kinase C beta type;
DE Short=PKC-B;
DE Short=PKC-beta;
DE EC=2.7.11.13;
GN Name=Prkcb; Synonyms=Pkcb, Prkcb1;
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] (ISOFORMS BETA-I AND BETA-II).
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS BETA-I AND BETA-II).
RC TISSUE=Brain;
RX PubMed=2428667; DOI=10.1016/0014-5793(86)81010-9;
RA Ono Y., Kurokawa T., Fujii T., Kawahara K., Igarashi K., Kikkawa U.,
RA Ogita K., Nishizuka Y.;
RT "Two types of complementary DNAs of rat brain protein kinase C.
RT Heterogeneity determined by alternative splicing.";
RL FEBS Lett. 206:347-352(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-I).
RC TISSUE=Fibroblast;
RX PubMed=3345563; DOI=10.1016/s0092-8674(88)80027-8;
RA Housey G.M., Johnson M.D., Hsiao W.L.W., O'Brian C.A., Murphy J.P.,
RA Kirschmeier P., Weinstein I.B.;
RT "Overproduction of protein kinase C causes disordered growth control in rat
RT fibroblasts.";
RL Cell 52:343-354(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 448-671 (ISOFORM BETA-I).
RX PubMed=3755404; DOI=10.1016/0014-5793(86)80724-4;
RA Ono Y., Kurokawa T., Kawahara K., Nishimura O., Marumoto R., Igarashi K.,
RA Sugino Y., Kikkawa U., Ogita K., Nishizuka Y.;
RT "Cloning of rat brain protein kinase C complementary DNA.";
RL FEBS Lett. 203:111-115(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 448-671 (ISOFORM BETA-I).
RX PubMed=3469647; DOI=10.1073/pnas.84.4.1065;
RA Housey G.M., O'Brian C.A., Johnson M.D., Kirschmeier P., Weinstein I.B.;
RT "Isolation of cDNA clones encoding protein kinase C: evidence for a protein
RT kinase C-related gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1065-1069(1987).
RN [6]
RP PROTEIN SEQUENCE OF 500-520 AND 636-663 (ISOFORM BETA-II), AND
RP PHOSPHORYLATION AT THR-500; THR-642 AND SER-661.
RX PubMed=8749392; DOI=10.1016/s0960-9822(95)00277-6;
RA Keranen L.M., Dutil E.M., Newton A.C.;
RT "Protein kinase C is regulated in vivo by three functionally distinct
RT phosphorylations.";
RL Curr. Biol. 5:1394-1403(1995).
RN [7]
RP PHOSPHORYLATION AT SER-16; THR-17; THR-314; THR-324; THR-635 AND THR-642,
RP AND MUTAGENESIS OF 16-SER-THR-17; THR-314; THR-324; THR-635 AND THR-642.
RX PubMed=8327493; DOI=10.1073/pnas.90.13.6130;
RA Zhang J., Wang L., Petrin J., Bishop W.R., Bond R.W.;
RT "Characterization of site-specific mutants altered at protein kinase C beta
RT 1 isozyme autophosphorylation sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6130-6134(1993).
RN [8]
RP PHOSPHORYLATION AT THR-642 (ISOFORM BETA-I), AND MUTAGENESIS OF THR-635 AND
RP THR-642.
RX PubMed=8034726; DOI=10.1016/s0021-9258(17)32208-1;
RA Zhang J., Wang L., Schwartz J., Bond R.W., Bishop W.R.;
RT "Phosphorylation of Thr642 is an early event in the processing of newly
RT synthesized protein kinase C beta 1 and is essential for its activation.";
RL J. Biol. Chem. 269:19578-19584(1994).
RN [9]
RP PHOSPHORYLATION AT THR-500, AND MUTAGENESIS OF THR-500.
RX PubMed=7961692; DOI=10.1016/s0021-9258(18)47044-5;
RA Orr J.W., Newton A.C.;
RT "Requirement for negative charge on 'activation loop' of protein kinase
RT C.";
RL J. Biol. Chem. 269:27715-27718(1994).
RN [10]
RP FUNCTION IN INSULIN SIGNALING.
RX PubMed=10938109; DOI=10.1128/mcb.20.17.6323-6333.2000;
RA Formisano P., Oriente F., Fiory F., Caruso M., Miele C., Maitan M.A.,
RA Andreozzi F., Vigliotta G., Condorelli G., Beguinot F.;
RT "Insulin-activated protein kinase Cbeta bypasses Ras and stimulates
RT mitogen-activated protein kinase activity and cell proliferation in muscle
RT cells.";
RL Mol. Cell. Biol. 20:6323-6333(2000).
RN [11]
RP FUNCTION IN INSULIN SIGNALING.
RX PubMed=11714718; DOI=10.1074/jbc.m109647200;
RA Kaneto H., Suzuma K., Sharma A., Bonner-Weir S., King G.L., Weir G.C.;
RT "Involvement of protein kinase C beta 2 in c-myc induction by high glucose
RT in pancreatic beta-cells.";
RL J. Biol. Chem. 277:3680-3685(2002).
RN [12]
RP FUNCTION.
RX PubMed=19176525; DOI=10.1074/jbc.m808719200;
RA Yamasaki T., Takahashi A., Pan J., Yamaguchi N., Yokoyama K.K.;
RT "Phosphorylation of activation transcription factor-2 at serine 121 by
RT protein kinase c controls c-Jun-mediated activation of transcription.";
RL J. Biol. Chem. 284:8567-8581(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND THR-642,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641; SER-654; SER-660 AND
RP SER-664 (ISOFORM BETA-II), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE 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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 157-288 IN COMPLEX WITH CALCIUM
RP IONS, AND COFACTOR.
RX PubMed=9817842; DOI=10.1016/s0969-2126(98)00139-7;
RA Sutton R.B., Sprang S.R.;
RT "Structure of the protein kinase Cbeta phospholipid-binding C2 domain
RT complexed with Ca2+.";
RL Structure 6:1395-1405(1998).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 1-661 IN COMPLEX WITH CALCIUM
RP IONS, COFACTOR, AND PHOSPHORYLATION AT THR-500; THR-642 AND SER-661.
RX PubMed=21215369; DOI=10.1016/j.cell.2010.12.013;
RA Leonard T.A., Rozycki B., Saidi L.F., Hummer G., Hurley J.H.;
RT "Crystal structure and allosteric activation of protein kinase C betaII.";
RL Cell 144:55-66(2011).
CC -!- FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-
CC dependent serine/threonine-protein kinase involved in various cellular
CC processes such as regulation of the B-cell receptor (BCR) signalosome,
CC oxidative stress-induced apoptosis, androgen receptor-dependent
CC transcription regulation, insulin signaling and endothelial cells
CC proliferation. Plays a key role in B-cell activation by regulating BCR-
CC induced NF-kappa-B activation. Mediates the activation of the canonical
CC NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1
CC at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces
CC CARD11/CARMA1 association with lipid rafts and recruitment of the
CC BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK
CC complex, resulting in nuclear translocation and activation of NFKB1.
CC Plays a direct role in the negative feedback regulation of the BCR
CC signaling, by down-modulating BTK function via direct phosphorylation
CC of BTK at 'Ser-180', which results in the alteration of BTK plasma
CC membrane localization and in turn inhibition of BTK activity. Involved
CC in apoptosis following oxidative damage: in case of oxidative
CC conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of
CC SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc
CC acts as a reactive oxygen species producer. Acts as a coactivator of
CC androgen receptor (ANDR)-dependent transcription, by being recruited to
CC ANDR target genes and specifically mediating phosphorylation of 'Thr-6'
CC of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional
CC activation that prevents demethylation of histone H3 'Lys-4' (H3K4me)
CC by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in
CC muscle cells and mediate insulin-dependent DNA synthesis through the
CC RAF1-MAPK/ERK signaling cascade. Participates in the regulation of
CC glucose transport in adipocytes by negatively modulating the insulin-
CC stimulated translocation of the glucose transporter SLC2A4/GLUT4.
CC Phosphorylates SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1.
CC Under high glucose in pancreatic beta-cells, is probably involved in
CC the inhibition of the insulin gene transcription, via regulation of MYC
CC expression. In endothelial cells, activation of PRKCB induces increased
CC phosphorylation of RB1, increased VEGFA-induced cell proliferation, and
CC inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS)
CC regulation by insulin, which causes endothelial dysfunction. Also
CC involved in triglyceride homeostasis (By similarity). Phosphorylates
CC ATF2 which promotes cooperation between ATF2 and JUN, activating
CC transcription. {ECO:0000250|UniProtKB:P05771,
CC ECO:0000250|UniProtKB:P68404, ECO:0000269|PubMed:10938109,
CC ECO:0000269|PubMed:11714718, ECO:0000269|PubMed:19176525}.
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;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842};
CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domain. {ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842};
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-500
CC (activation loop of the kinase domain), Thr-642 (turn motif) and Ser-
CC 661 (hydrophobic region), need to be phosphorylated for its full
CC activation. Specifically inhibited by enzastaurin (LY317615) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PDK1. Interacts in vitro with PRKCBP1.
CC Interacts with PHLPP1 and PHLPP2; both proteins mediate its
CC dephosphorylation. Interacts with KDM1A/LSD1, PKN1 and ANDR (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P68403; P18052: Ptpra; Xeno; NbExp=3; IntAct=EBI-397072, EBI-6597520;
CC P68403-1; Q62920: Pdlim5; NbExp=5; IntAct=EBI-12559950, EBI-918433;
CC P68403-2; Q8WV44-2: TRIM41; Xeno; NbExp=3; IntAct=EBI-397092, EBI-726015;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Membrane;
CC Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Beta-I;
CC IsoId=P68403-1, P04410-1;
CC Sequence=Displayed;
CC Name=Beta-II;
CC IsoId=P68403-2, P04410-2;
CC Sequence=VSP_004739;
CC -!- PTM: Phosphorylation on Thr-500 of isoform beta-I, within the
CC activation loop, renders it competent to autophosphorylate. Subsequent
CC autophosphorylation of Thr-642 maintains catalytic competence, and
CC autophosphorylation on Ser-661 appears to release the kinase into the
CC cytosol. Similarly, isoform beta-II is autophosphorylated on 'Thr-641'
CC and 'Ser-660', subsequent to phosphorylation on Thr-500.
CC Autophosphorylated on other sites i.e. in the N-terminal and hinge
CC regions have no effect on enzyme activity. Phosphorylation at Tyr-662
CC by SYK induces binding with GRB2 and contributes to the activation of
CC MAPK/ERK signaling cascade. {ECO:0000269|PubMed:21215369,
CC ECO:0000269|PubMed:7961692, ECO:0000269|PubMed:8327493,
CC ECO:0000269|PubMed:8749392}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; M13706; AAA41875.1; -; mRNA.
DR EMBL; K03485; AAA41864.1; -; mRNA.
DR EMBL; K03486; AAA41865.1; -; mRNA.
DR EMBL; X04439; CAA28035.1; -; Genomic_DNA.
DR EMBL; X04440; CAA28036.1; -; mRNA.
DR EMBL; M19007; AAA41868.1; -; mRNA.
DR EMBL; X04139; CAA27756.1; -; mRNA.
DR EMBL; M15522; AAA41876.1; -; mRNA.
DR PIR; A00622; KIRTC1.
DR RefSeq; NP_001165776.1; NM_001172305.1.
DR PDB; 1A25; X-ray; 2.70 A; A/B=154-289.
DR PDB; 3PFQ; X-ray; 4.00 A; A=1-661.
DR PDBsum; 1A25; -.
DR PDBsum; 3PFQ; -.
DR AlphaFoldDB; P68403; -.
DR SMR; P68403; -.
DR BioGRID; 247103; 17.
DR IntAct; P68403; 7.
DR MINT; P68403; -.
DR STRING; 10116.ENSRNOP00000016417; -.
DR BindingDB; P68403; -.
DR ChEMBL; CHEMBL3020; -.
DR DrugCentral; P68403; -.
DR iPTMnet; P68403; -.
DR PhosphoSitePlus; P68403; -.
DR jPOST; P68403; -.
DR PaxDb; P68403; -.
DR PRIDE; P68403; -.
DR Ensembl; ENSRNOT00000016418; ENSRNOP00000016417; ENSRNOG00000012061. [P68403-1]
DR Ensembl; ENSRNOT00000078705; ENSRNOP00000073511; ENSRNOG00000012061. [P68403-2]
DR GeneID; 25023; -.
DR KEGG; rno:25023; -.
DR UCSC; RGD:3396; rat.
DR CTD; 5579; -.
DR RGD; 3396; Prkcb.
DR eggNOG; KOG0696; Eukaryota.
DR GeneTree; ENSGT00940000155217; -.
DR InParanoid; P68403; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; P68403; -.
DR BRENDA; 2.7.1.107; 5301.
DR Reactome; R-RNO-114516; Disinhibition of SNARE formation.
DR Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-RNO-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-RNO-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-RNO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-RNO-76005; Response to elevated platelet cytosolic Ca2+.
DR EvolutionaryTrace; P68403; -.
DR PRO; PR:P68403; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0044305; C:calyx of Held; ISO:RGD.
DR GO; GO:0005813; C:centrosome; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:RGD.
DR GO; GO:0008091; C:spectrin; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:RGD.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0035403; F:histone kinase activity (H3-T6 specific); ISS:UniProtKB.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0004697; F:protein kinase C activity; IDA:RGD.
DR GO; GO:0005080; F:protein kinase C binding; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042113; P:B cell activation; ISS:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; ISO:RGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEP:RGD.
DR GO; GO:0035408; P:histone H3-T6 phosphorylation; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0042488; P:positive regulation of odontogenesis of dentin-containing tooth; IEP:RGD.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0014059; P:regulation of dopamine secretion; IMP:RGD.
DR GO; GO:0010827; P:regulation of glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IMP:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0033280; P:response to vitamin D; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:RGD.
DR CDD; cd00029; C1; 2.
DR CDD; cd05616; STKc_cPKC_beta; 1.
DR Gene3D; 2.60.40.150; -; 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; IPR034664; cPKC-beta.
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 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; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Adaptive immunity; Alternative splicing;
KW Apoptosis; ATP-binding; Calcium; Chromatin regulator; Cytoplasm;
KW Direct protein sequencing; Immunity; Kinase; Membrane; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P05771"
FT CHAIN 2..671
FT /note="Protein kinase C beta type"
FT /id="PRO_0000055687"
FT DOMAIN 158..275
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 342..600
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 601..671
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 36..86
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 101..151
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 614..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 466
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:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:9817842"
FT BINDING 348..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P05771"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 16
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8327493"
FT MOD_RES 17
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8327493"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05771"
FT MOD_RES 250
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 314
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8327493"
FT MOD_RES 324
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8327493"
FT MOD_RES 500
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000305|PubMed:21215369,
FT ECO:0000305|PubMed:7961692, ECO:0000305|PubMed:8749392"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05771"
FT MOD_RES 635
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8327493"
FT MOD_RES 642
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:8327493, ECO:0000269|PubMed:8749392,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 661
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:21215369,
FT ECO:0000269|PubMed:8749392"
FT MOD_RES 662
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000250|UniProtKB:P68404"
FT VAR_SEQ 622..671
FT /note="RDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV
FT -> CGRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEFEGFSFVNSEFLKPEVKS (in
FT isoform Beta-II)"
FT /evidence="ECO:0000303|PubMed:2428667,
FT ECO:0000303|PubMed:3755379"
FT /id="VSP_004739"
FT MUTAGEN 16..17
FT /note="ST->AA: No effect."
FT /evidence="ECO:0000269|PubMed:8327493"
FT MUTAGEN 314
FT /note="T->A: No effect; when associated with A-323."
FT /evidence="ECO:0000269|PubMed:8327493"
FT MUTAGEN 324
FT /note="T->A: No effect; when associated with A-313."
FT /evidence="ECO:0000269|PubMed:8327493"
FT MUTAGEN 500
FT /note="T->E: 50% increase of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:7961692"
FT MUTAGEN 500
FT /note="T->S: 50% decrease of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:7961692"
FT MUTAGEN 500
FT /note="T->V,D: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:7961692"
FT MUTAGEN 635
FT /note="T->A: Loss of enzymatic activity; when associated
FT with T-643 change in subcellular location, loss of PMA-
FT induced down-regulation and loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:8034726,
FT ECO:0000269|PubMed:8327493"
FT MUTAGEN 642
FT /note="T->A: Loss of enzymatic activity; when associated
FT with T-636 change in subcellular location, loss of PMA-
FT induced down-regulation and loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:8034726,
FT ECO:0000269|PubMed:8327493"
FT CONFLICT 25
FT /note="A -> P (in Ref. 3; AAA41868)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="I -> V (in Ref. 1; AAA41875)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="N -> S (in Ref. 1; AAA41875)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="K -> R (in Ref. 1; AAA41875)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="S -> G (in Ref. 1; AAA41875)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="I -> V (in Ref. 1; AAA41875)"
FT /evidence="ECO:0000305"
FT CONFLICT 170..171
FT /note="RE -> GG (in Ref. 1; AAA41875)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="I -> V (in Ref. 1; AAA41875)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="G -> E (in Ref. 3; AAA41868)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="V -> M (in Ref. 2; CAA28035/CAA28036)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="Missing (in Ref. 1; AAA41865)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="Missing (in Ref. 1; AAA41865)"
FT /evidence="ECO:0000305"
FT STRAND 161..182
FT /evidence="ECO:0007829|PDB:1A25"
FT STRAND 194..202
FT /evidence="ECO:0007829|PDB:1A25"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:1A25"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:1A25"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:1A25"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1A25"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:1A25"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:1A25"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1A25"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:1A25"
FT MOD_RES P68403-2:641
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES P68403-2:654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES P68403-2:660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES P68403-2:664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 671 AA; 76751 MW; A1935030F758513C CRC64;
MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF
GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS
LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIDR EVLIVVVRDA
KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL
SVEIWDWDLT SRNDFMGSLS FGISELQKAG VDGWFKLLSQ EEGEYFNVPV PPEGSEGNEE
LRQKFERAKI GQGTKAPEEK TANTISKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE
RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM
EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI
KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP
FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF
RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM NLDQNEFAGF
SYTNPEFVIN V
