KPCB_XENLA
ID KPCB_XENLA Reviewed; 671 AA.
AC Q7LZQ8;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=3272298;
RA Chen K.H., Peng Z.G., Lavu S., Kung H.F.;
RT "Molecular cloning and sequence analysis of two distinct types of Xenopus
RT laevis protein kinase C.";
RL Second Messengers Phosphoproteins 12:251-260(1988).
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 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 PIR; B37237; B37237.
DR AlphaFoldDB; Q7LZQ8; -.
DR SMR; Q7LZQ8; -.
DR Proteomes; UP000186698; Genome assembly.
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: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: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..671
FT /note="Protein kinase C beta type"
FT /id="PRO_0000394259"
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 REGION 308..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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 671 AA; 76524 MW; FE2421982270A62A CRC64;
MSDSEACEPG DDTTTRFARK GALRQKNVHE VKEHKFTARF FKQPTFCSHC TDFIWGFGKQ
GFQCQVCCFV VHKRCHEFVT FSCPGADKGP ASDDPRSKHK FRIHTYSSPT FCDHCGSLLY
GLIHQGMKCE TCMMNVHKRC VMNVPSLCGT DHTERRGRIH IKAEIKEEVM TVTVGDAKNL
VPMDPNGLSD PYVKLKLIPD PKSETKQKTK TIKCSLNPSW NETFKFQLKE SDKDRRLSVE
IWDWELTSRN DFMGSLSFGI SELLKAGVDG WFKLLSQEEG EYFNVPVPPE GEEGNEELRQ
KFERAKIGPG NKAAGREGGK PSVQGGQQGN RDHMKVSDFN FLKVLGKGSF GKVTLAERKG
TDELYAIKIL KKDVVIQDDD VECTMVEKRV LALSGKPPFL THLHSCFQTM DRLYFVMEFV
NGGDLMYQIQ QVGRFKEPHA VFYAAEIRVG LLFLHSKGIV YRDLKLDNVM LDSEGHIKIA
DFGMCKENMW DGITTKTFCG TPDYIAPGII RYQPYAKSVD WWAFGILLYE MLAGHVPFEG
EDEDELFQSI MEHNVAYPKS MSKEAVAICK GLMTKHPGKR LGCGPEGERD IKDHAFFRYI
DWEKLERNEI QPPYKPKACG RNAENFDKFF TRHPPVLTPP DHEVIRNIDQ SEFEGFSYVN
SDFSKEEEKK D
