KPCB_XENTR
ID KPCB_XENTR Reviewed; 670 AA.
AC A8KBH6;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=prkcb1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2007) 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:0000250|UniProtKB:P68403,
CC 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; BC154114; AAI54115.1; -; mRNA.
DR RefSeq; NP_001103513.1; NM_001110043.1.
DR AlphaFoldDB; A8KBH6; -.
DR SMR; A8KBH6; -.
DR STRING; 8364.ENSXETP00000033079; -.
DR PaxDb; A8KBH6; -.
DR GeneID; 100038043; -.
DR KEGG; xtr:100038043; -.
DR CTD; 5579; -.
DR Xenbase; XB-GENE-486491; prkcb.
DR eggNOG; KOG0696; Eukaryota.
DR InParanoid; A8KBH6; -.
DR OrthoDB; 614710at2759; -.
DR Reactome; R-XTR-114516; Disinhibition of SNARE formation.
DR Reactome; R-XTR-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-XTR-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-XTR-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-XTR-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-XTR-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-XTR-76005; Response to elevated platelet cytosolic Ca2+.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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_0000394260"
FT DOMAIN 155..272
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 33..83
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 98..148
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 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 244
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 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 249
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="1"
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 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; 76517 MW; 2C21D9AD75091FCD CRC64;
MADPAACEPG EDTTTRFARK GALRQKNVHE VKEHKFTARF FKQPTFCSHC TDFIWGFGKQ
GFQCQVCCFV VHKRCHEFVT FSCPGADKGP ASDDPRSKHK FKIHTYSSPT FCDHCGSLLY
GLIHQGMKCE TCMMNVHKRC VMNVPSLCGT DHTERRGRIH IKAEIREEVL TVTVGDARNL
VPMDPNGLSD PYVKLKLIPD PKSESKQKTK TIKCSLNPTW NESFKFQLKE SDKDRRLSVE
IWDWDLTSRN DFMGSLSFGI SELLKAGVDG WFKLLSQEEG EYFNVPVPPE GEEGNEELRQ
KFERAKIGPG TKAVEEKVVN PMPKVDNNET RDRMKVSDFN FLKVLGKGSF GKVILAERKG
TDELYAIKIL KKDVVIQDDD VECTMVEKRV LALSGKPPFL TQLHSCFQTM DRLYFVMEYV
NGGDLMYQIQ QVGRFKEPHA VFYAAEIAIG LLFLHSKGIV YRDLKLDNVM LDSEGHIKIA
DFGMCKENMW DGVTTKTFCG TPDYIAPEII AYQPYAKSVD WWAFGILLYE MLAGQAPFEG
EDEDELFQSI MEHNVAYPKS MSKEAVAICK GLMTKHPGKR LGCGPEGERD IKDHAFFRYI
DWEKLERNEI QPPYKPKACG RNAENFDKFF TRHPPVLTPP DHEVIRNIDQ SEFEGFSYVN
SDFAKEEEKD
