KPCB_DANRE
ID KPCB_DANRE Reviewed; 670 AA.
AC Q7SY24;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein kinase C beta type;
DE Short=PKC-B;
DE Short=PKC-beta;
DE EC=2.7.11.13;
GN Name=prkcbb; Synonyms=prkcb1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-activated and phospholipid-dependent
CC serine/threonine-protein kinase involved in various processes such as
CC regulation of the B-cell receptor (BCR) signalosome, apoptosis and
CC transcription regulation. Plays a key role in B-cell activation and
CC function by regulating BCR-induced NF-kappa-B activation and B-cell
CC survival. Required for recruitment and activation of the IKK kinase to
CC lipid rafts and mediates phosphorylation of card11/carma1, leading to
CC activate the NF-kappa-B signaling. Involved in apoptosis following
CC oxidative damage: in case of oxidative conditions, specifically
CC phosphorylates isoform p66Shc of shc1, leading to mitochondrial
CC accumulation of p66Shc, where p66Shc acts as a reactive oxygen species
CC producer. Acts as a coactivator of androgen receptor (andr)-dependent
CC transcription, by being recruited to ANDR target genes and specifically
CC mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific
CC tag for epigenetic transcriptional activation (By similarity).
CC {ECO:0000250}.
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 Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domain. {ECO:0000250|UniProtKB:P68403};
CC -!- ACTIVITY REGULATION: Activated by diacylglycerol which in turn
CC phosphorylates a range of cellular proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- PTM: Phosphorylation on Thr-497 within the activation loop renders it
CC competent to autophosphorylate. Subsequent autophosphorylation of Thr-
CC 638 maintains catalytic competence, and autophosphorylation on Ser-657
CC appears to release the kinase into the cytosol (By similarity).
CC {ECO:0000250}.
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; BC055154; AAH55154.1; -; mRNA.
DR RefSeq; NP_957272.1; NM_200978.1.
DR AlphaFoldDB; Q7SY24; -.
DR SMR; Q7SY24; -.
DR STRING; 7955.ENSDARP00000038918; -.
DR PaxDb; Q7SY24; -.
DR PRIDE; Q7SY24; -.
DR Ensembl; ENSDART00000029451; ENSDARP00000038918; ENSDARG00000022254.
DR GeneID; 393953; -.
DR KEGG; dre:393953; -.
DR CTD; 393953; -.
DR ZFIN; ZDB-GENE-040426-1178; prkcbb.
DR eggNOG; KOG0696; Eukaryota.
DR GeneTree; ENSGT00940000155217; -.
DR HOGENOM; CLU_000288_54_2_1; -.
DR InParanoid; Q7SY24; -.
DR OMA; FRRIDWV; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; Q7SY24; -.
DR TreeFam; TF351133; -.
DR Reactome; R-DRE-114516; Disinhibition of SNARE formation.
DR Reactome; R-DRE-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-DRE-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-DRE-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-DRE-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-DRE-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-DRE-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-DRE-76005; Response to elevated platelet cytosolic Ca2+.
DR PRO; PR:Q7SY24; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000022254; Expressed in granulocyte and 34 other tissues.
DR ExpressionAtlas; Q7SY24; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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:0007596; P:blood coagulation; IMP:ZFIN.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:ZFIN.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Adaptive immunity; Apoptosis; ATP-binding; Calcium; Chromatin regulator;
KW Cytoplasm; Immunity; Kinase; Membrane; Metal-binding; Nucleotide-binding;
KW 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"
FT CHAIN 2..670
FT /note="Protein kinase C beta type"
FT /id="PRO_0000394258"
FT DOMAIN 157..274
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 339..597
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 598..668
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 463
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 345..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 497
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 501
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 631
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT MOD_RES 638
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 657
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 670 AA; 76306 MW; DF2D78CFF9BDDCA1 CRC64;
MAEPANSDGE ERSAPMRGFA RQGALRQKNV HEVKNHKFIA RFFKQPTFCS HCTDFIWGFG
KQGFQCQVCC FVVHKRCHEF VTFSCPGADK GPASDDPRSK HKFKVHTYSS PTFCDHCGSL
LYGLIHQGMR CDHCMMNIHK RCVANVPSLC GTDHTERRGR IQITAEIKNN VLTVSIKEAK
NLVPMDPNGL SDPYVKLKLI PDPKSESKQK TKTIKCCLNP TWNETFTFNL KESDKDRRLS
VEIWDWDLTS RNDFMGSLSF GISELQKQGV DGWFKLLSQE EGEYFNVPVP PEGEEGNEEL
RQKFERAKIG PSKTDGSSSN AISKFDSNGN RDRMKLSDFN FLMVLGKGSF GKVMLAERKG
ADELFAIKIL KKDVVIQDDD VECTMVEKRV LALSGKPPFL TQLHSCFQTM DRLYFVMEYI
NGGDLMYHIQ QVGKFKEPHA VFYAAEIAIG LFFLHSKGVI YRDLKLDNVM LDAEGHIKIA
DFGMCKENML DGVTTKTFCG TPDYIAPEII AYQPYGKSVD WWAFGVLLYE MLAGQPPFDG
EDEDELFQSI MEHHVSYPKS MSKEAVAICK GLMTKHPGKR LGCGPEGERD IREHGFFRYM
DWEKLEHREV QPPFKPKACG RDAENFDRFF TRHPPVLTPP DQEVIMNLDQ DEFEGFSFIN
PEFPAMEAQS
