ID KPCZ_RAT Reviewed; 592 AA.
AC P09217;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 24-JAN-2024, entry version 217.
DE RecName: Full=Protein kinase C zeta type;
DE EC=2.7.11.13 {ECO:0000269|PubMed:8378304};
DE AltName: Full=nPKC-zeta;
GN Name=Prkcz; Synonyms=Pkcz;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=2470089; DOI=10.1073/pnas.86.9.3099;
RA Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.;
RT "Protein kinase C zeta subspecies from rat brain: its structure,
RT expression, and properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3099-3103(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 101-592 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=2834397; DOI=10.1016/s0021-9258(18)68732-0;
RA Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.;
RT "The structure, expression, and properties of additional members of the
RT protein kinase C family.";
RL J. Biol. Chem. 263:6927-6932(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 101-180 (ISOFORM 1).
RX PubMed=3691811; DOI=10.1016/0014-5793(87)80564-1;
RA Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.;
RT "Identification of three additional members of rat protein kinase C family:
RT delta-, epsilon- and zeta-subspecies.";
RL FEBS Lett. 226:125-128(1987).
RN [4]
RP CATALYTIC ACTIVITY (ISOFORM 2), ACTIVITY REGULATION (ISOFORM 2),
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY (ISOFORMS 1 AND
RP 2), AND INDUCTION (ISOFORM 2).
RX PubMed=8378304; DOI=10.1073/pnas.90.18.8342;
RA Sacktor T.C., Osten P., Valsamis H., Jiang X., Naik M.U., Sublette E.;
RT "Persistent activation of the zeta isoform of protein kinase C in the
RT maintenance of long-term potentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8342-8346(1993).
RN [5]
RP FUNCTION IN ACTIVATION OF MAP2K1/MEK1 AND MAPK3/ERK1.
RX PubMed=8557035; DOI=10.1002/j.1460-2075.1995.tb00306.x;
RA Berra E., Diaz-Meco M.T., Lozano J., Frutos S., Municio M.M., Sanchez P.,
RA Sanz L., Moscat J.;
RT "Evidence for a role of MEK and MAPK during signal transduction by protein
RT kinase C zeta.";
RL EMBO J. 14:6157-6163(1995).
RN [6]
RP FUNCTION.
RX PubMed=9374484; DOI=10.1074/jbc.272.48.30075;
RA Standaert M.L., Galloway L., Karnam P., Bandyopadhyay G., Moscat J.,
RA Farese R.V.;
RT "Protein kinase C-zeta as a downstream effector of phosphatidylinositol 3-
RT kinase during insulin stimulation in rat adipocytes. Potential role in
RT glucose transport.";
RL J. Biol. Chem. 272:30075-30082(1997).
RN [7]
RP FUNCTION, INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=9177193; DOI=10.1073/pnas.94.12.6191;
RA Puls A., Schmidt S., Grawe F., Stabel S.;
RT "Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-
RT binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6191-6196(1997).
RN [8]
RP FUNCTION IN NF-KAPPA-B ACTIVATION.
RX PubMed=10022904; DOI=10.1128/mcb.19.3.2180;
RA Lallena M.J., Diaz-Meco M.T., Bren G., Paya C.V., Moscat J.;
RT "Activation of IkappaB kinase beta by protein kinase C isoforms.";
RL Mol. Cell. Biol. 19:2180-2188(1999).
RN [9]
RP FUNCTION IN NF-KAPPA-B ACTIVATION.
RX PubMed=10747026; DOI=10.1093/emboj/19.7.1576;
RA Sanz L., Diaz-Meco M.T., Nakano H., Moscat J.;
RT "The atypical PKC-interacting protein p62 channels NF-kappaB activation by
RT the IL-1-TRAF6 pathway.";
RL EMBO J. 19:1576-1586(2000).
RN [10]
RP FUNCTION IN CELL POLARITY.
RX PubMed=11525734; DOI=10.1016/s0092-8674(01)00471-8;
RA Etienne-Manneville S., Hall A.;
RT "Integrin-mediated activation of Cdc42 controls cell polarity in migrating
RT astrocytes through PKCzeta.";
RL Cell 106:489-498(2001).
RN [11]
RP FUNCTION IN ACTIVATION OF MAP2K5/MEK5 AND MAPK7/ERK5.
RX PubMed=11158308; DOI=10.1128/mcb.21.4.1218-1227.2001;
RA Diaz-Meco M.T., Moscat J.;
RT "MEK5, a new target of the atypical protein kinase C isoforms in mitogenic
RT signaling.";
RL Mol. Cell. Biol. 21:1218-1227(2001).
RN [12]
RP FUNCTION (ISOFORM 2).
RX PubMed=11914719; DOI=10.1038/nn829;
RA Ling D.S., Benardo L.S., Serrano P.A., Blace N., Kelly M.T., Crary J.F.,
RA Sacktor T.C.;
RT "Protein kinase Mzeta is necessary and sufficient for LTP maintenance.";
RL Nat. Neurosci. 5:295-296(2002).
RN [13]
RP INTERACTION WITH SQSTM1 AND GABRR3, AND SUBCELLULAR LOCATION.
RX PubMed=12431995; DOI=10.1074/jbc.m205162200;
RA Croci C., Brandstaetter J.H., Enz R.;
RT "ZIP3, a new splice variant of the PKC-zeta-interacting protein family,
RT binds to GABAC receptors, PKC-zeta, and Kv beta 2.";
RL J. Biol. Chem. 278:6128-6135(2003).
RN [14]
RP INTERACTION WITH SQSTM1 AND MAP2K5, AND MUTAGENESIS OF ASP-62.
RX PubMed=12813044; DOI=10.1074/jbc.m303221200;
RA Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A.,
RA Michaelsen E., Bjoerkoey G., Johansen T.;
RT "Interaction codes within the family of mammalian Phox and Bem1p domain-
RT containing proteins.";
RL J. Biol. Chem. 278:34568-34581(2003).
RN [15]
RP TISSUE SPECIFICITY (ISOFORMS 1 AND 2), INDUCTION (ISOFORM 2), AND
RP ALTERNATIVE PROMOTER USAGE (ISOFORM 2).
RX PubMed=12857744; DOI=10.1074/jbc.m307065200;
RA Hernandez A.I., Blace N., Crary J.F., Serrano P.A., Leitges M.,
RA Libien J.M., Weinstein G., Tcherapanov A., Sacktor T.C.;
RT "Protein kinase M zeta synthesis from a brain mRNA encoding an independent
RT protein kinase C zeta catalytic domain. Implications for the molecular
RT mechanism of memory.";
RL J. Biol. Chem. 278:40305-40316(2003).
RN [16]
RP PHOSPHORYLATION AT THR-410 AND THR-560.
RX PubMed=14580237; DOI=10.1042/bj20031194;
RA Le Good J.A., Brindley D.N.;
RT "Molecular mechanisms regulating protein kinase Czeta turnover and cellular
RT transformation.";
RL Biochem. J. 378:83-92(2004).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-560 AND SER-591, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE 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 [18]
RP FUNCTION (ISOFORM 2), TISSUE SPECIFICITY (ISOFORM 2), INDUCTION (ISOFORM
RP 2), AND DISRUPTION PHENOTYPE (ISOFORM 2).
RX PubMed=27498875; DOI=10.1016/j.celrep.2016.07.030;
RA Wang S., Sheng T., Ren S., Tian T., Lu W.;
RT "Distinct Roles of PKCiota/lambda and PKMzeta in the Initiation and
RT Maintenance of Hippocampal Long-Term Potentiation and Memory.";
RL Cell Rep. 16:1954-1961(2016).
CC -!- FUNCTION: Calcium- and diacylglycerol-independent serine/threonine-
CC protein kinase that functions in phosphatidylinositol 3-kinase (PI3K)
CC pathway and mitogen-activated protein (MAP) kinase cascade, and is
CC involved in NF-kappa-B activation, mitogenic signaling, cell
CC proliferation, cell polarity, inflammatory response and maintenance of
CC long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment
CC in macrophages, or following mitogenic stimuli, functions downstream of
CC PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently
CC of RAF1 activation. Required for insulin-dependent activation of AKT3,
CC but may function as an adapter rather than a direct activator. Upon
CC insulin treatment may act as a downstream effector of PI3K and
CC contribute to the activation of translocation of the glucose
CC transporter SLC2A4/GLUT4 and subsequent glucose transport in
CC adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-
CC MAPK7/ERK5 independently of its kinase activity and can activate JUN
CC promoter through MEF2C. Through binding with SQSTM1/p62, functions in
CC interleukin-1 signaling and activation of NF-kappa-B with the specific
CC adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation
CC of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in
CC turn leads to the degradation of NF-kappa-B inhibitors. In migrating
CC astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by
CC CDC42 to function in the establishment of cell polarity along with the
CC microtubule motor and dynein. In association with FEZ1, stimulates
CC neuronal differentiation in PC12 cells. In the inflammatory response,
CC is required for the T-helper 2 (Th2) differentiation process, including
CC interleukin production, efficient activation of JAK1 and the subsequent
CC phosphorylation and nuclear translocation of STAT6. May be involved in
CC development of allergic airway inflammation (asthma), a process
CC dependent on Th2 immune response. In the NF-kappa-B-mediated
CC inflammatory response, can relieve SETD6-dependent repression of NF-
CC kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'.
CC Phosphorylates VAMP2 in vitro (By similarity).
CC {ECO:0000250|UniProtKB:Q05513, ECO:0000269|PubMed:10022904,
CC ECO:0000269|PubMed:10747026, ECO:0000269|PubMed:11158308,
CC ECO:0000269|PubMed:11525734, ECO:0000269|PubMed:8557035,
CC ECO:0000269|PubMed:9177193, ECO:0000269|PubMed:9374484}.
CC -!- FUNCTION: [Isoform 2]: Involved in late synaptic long term potentiation
CC phase in CA1 hippocampal cells and long term memory maintenance.
CC {ECO:0000269|PubMed:11914719, ECO:0000269|PubMed:27498875}.
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 Evidence={ECO:0000269|PubMed:8378304};
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; Evidence={ECO:0000269|PubMed:8378304};
CC -!- ACTIVITY REGULATION: Atypical PKCs (PRKCI and PRKCZ) exhibit an
CC elevated basal enzymatic activity (that may be due to the interaction
CC with SMG1 or SQSTM1) and are not regulated by diacylglycerol,
CC phosphatidylserine, phorbol esters or calcium ions. Two specific sites,
CC Thr-410 (activation loop of the kinase domain) and Thr-560 (turn
CC motif), need to be phosphorylated for its full activation.
CC Phosphatidylinositol 3,4,5-trisphosphate might be a physiological
CC activator (Probable). Isoform 2: Constitutively active
CC (PubMed:8378304). {ECO:0000269|PubMed:8378304, ECO:0000305}.
CC -!- SUBUNIT: Interacts with PARD6A, PARD6B and PARD6G. Part of a complex
CC with PARD3, PARD6A or PARD6B or PARD6G and CDC42 or RAC1. Interacts
CC with ADAP1/CENTA1 (By similarity). Forms a ternary complex with SQSTM1
CC and KCNAB2. Forms another ternary complex with SQSTM1 and GABRR3. Forms
CC a complex with SQSTM1 and MAP2K5. Interacts (via the protein kinase
CC domain) with WWC1. Forms a tripartite complex with WWC1 and DDR1, but
CC predominantly in the absence of collagen. Component of the Par polarity
CC complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1.
CC Interacts with PDPK1 (via N-terminal region). Interacts with WDFY2 (via
CC WD repeats 1-3) (By similarity). Interacts with VAMP2 (By similarity).
CC Forms a complex with WDFY2 and VAMP2 (By similarity). Interacts with
CC APPL1 (By similarity). Interacts with WWC1, WWC2 and WWC3 (By
CC similarity). {ECO:0000250|UniProtKB:Q05513,
CC ECO:0000269|PubMed:12431995, ECO:0000269|PubMed:12813044,
CC ECO:0000269|PubMed:9177193}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12431995,
CC ECO:0000269|PubMed:8378304, ECO:0000269|PubMed:9177193}. Endosome
CC {ECO:0000250|UniProtKB:Q05513}. Cell junction
CC {ECO:0000250|UniProtKB:Q05513}. Membrane {ECO:0000269|PubMed:8378304};
CC Peripheral membrane protein {ECO:0000305}. Note=In the retina,
CC localizes in the terminals of the rod bipolar cells (PubMed:12431995).
CC Associated with endosomes (By similarity). Presence of KRIT1, CDH5 and
CC RAP1B is required for its localization to the cell junction (By
CC similarity). Colocalizes with VAMP2 and WDFY2 in intracellular vesicles
CC (By similarity). Transiently translocates to the membrane of CA1
CC hippocampal cells in response to the induction of long term
CC potentiation (PubMed:8378304). {ECO:0000250|UniProtKB:Q05513,
CC ECO:0000269|PubMed:12431995, ECO:0000269|PubMed:8378304}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:8378304}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=P09217-1; Sequence=Displayed;
CC Name=2; Synonyms=PKMzeta {ECO:0000303|PubMed:12857744};
CC IsoId=P09217-2; Sequence=VSP_059935;
CC -!- TISSUE SPECIFICITY: Isoform 1: In brain, expressed in hippocampus,
CC neocortex and cerebellum (at protein level) (PubMed:8378304,
CC PubMed:12857744). Also expressed in lung, liver, kidney, testis and to
CC a lesser extent in pancreas, intestine and skin (at protein level)
CC (PubMed:12857744). Isoform 2: Specifically expressed in brain where it
CC localizes to the hippocampus, neocortex and cerebellum (at protein
CC level) (PubMed:8378304, PubMed:12857744, PubMed:27498875).
CC {ECO:0000269|PubMed:12857744, ECO:0000269|PubMed:27498875,
CC ECO:0000269|PubMed:8378304}.
CC -!- INDUCTION: [Isoform 2]: Induced during synaptic long term potentiation.
CC {ECO:0000269|PubMed:12857744, ECO:0000269|PubMed:27498875,
CC ECO:0000269|PubMed:8378304}.
CC -!- DOMAIN: The PB1 domain mediate mutually exclusive interactions with
CC SQSTM1 and PARD6B. {ECO:0000250}.
CC -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
CC {ECO:0000269|PubMed:9177193}.
CC -!- PTM: CDH5 is required for its phosphorylation at Thr-410.
CC Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by
CC the apoptotic C-terminal cleavage product of PKN2. Phosphorylation at
CC Thr-410 by PI3K activates the kinase (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: [Isoform 2]: RNAi-mediated knockdown in the
CC dorsal hippocampus impairs the late phase of long-term potentiation and
CC the establishment of long term memory. Formation of short term memory
CC is not affected. {ECO:0000269|PubMed:27498875}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:12857744}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
CC -!- CAUTION: Isoform 2 (PKMzeta) was initially thought to be generated by
CC proteolysis of full-length PRKCZ (PubMed:8378304). However, PKMzeta is
CC a bona fide isoform produced by an alternative promoter in intron 4
CC (PubMed:12857744). {ECO:0000269|PubMed:12857744,
CC ECO:0000303|PubMed:8378304}.
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DR EMBL; J04532; AAA41934.1; -; mRNA.
DR EMBL; M18332; AAA41878.1; -; mRNA.
DR PIR; A30314; A30314.
DR RefSeq; NP_071952.1; NM_022507.1. [P09217-1]
DR PDB; 4MJS; X-ray; 2.50 A; A/C/E/G/I/K/M/O/Q/S/U/W=15-101.
DR PDBsum; 4MJS; -.
DR AlphaFoldDB; P09217; -.
DR SMR; P09217; -.
DR BioGRID; 247554; 20.
DR CORUM; P09217; -.
DR DIP; DIP-40867N; -.
DR IntAct; P09217; 5.
DR MINT; P09217; -.
DR STRING; 10116.ENSRNOP00000021285; -.
DR BindingDB; P09217; -.
DR ChEMBL; CHEMBL2094266; -.
DR DrugCentral; P09217; -.
DR GlyGen; P09217; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P09217; -.
DR PhosphoSitePlus; P09217; -.
DR PaxDb; 10116-ENSRNOP00000021285; -.
DR Ensembl; ENSRNOT00000021285.7; ENSRNOP00000021285.5; ENSRNOG00000015480.8. [P09217-1]
DR GeneID; 25522; -.
DR KEGG; rno:25522; -.
DR AGR; RGD:3399; -.
DR CTD; 5590; -.
DR RGD; 3399; Prkcz.
DR eggNOG; KOG0695; Eukaryota.
DR GeneTree; ENSGT00940000153497; -.
DR HOGENOM; CLU_000288_63_29_1; -.
DR InParanoid; P09217; -.
DR OMA; DKMAGLC; -.
DR OrthoDB; 841660at2759; -.
DR PhylomeDB; P09217; -.
DR BRENDA; 2.7.11.13; 5301.
DR Reactome; R-RNO-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-RNO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-RNO-9634635; Estrogen-stimulated signaling through PRKCZ.
DR PRO; PR:P09217; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000015480; Expressed in frontal cortex and 20 other cell types or tissues.
DR Genevisible; P09217; RN.
DR GO; GO:0045179; C:apical cortex; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0043203; C:axon hillock; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0031252; C:cell leading edge; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
DR GO; GO:0035748; C:myelin sheath abaxonal region; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0001725; C:stress fiber; IDA:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0071889; F:14-3-3 protein binding; IPI:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043274; F:phospholipase binding; IPI:RGD.
DR GO; GO:0015459; F:potassium channel regulator activity; IMP:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0016477; P:cell migration; IMP:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:RGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
DR GO; GO:0007616; P:long-term memory; IMP:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0051899; P:membrane depolarization; IMP:RGD.
DR GO; GO:0060081; P:membrane hyperpolarization; IMP:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:1990138; P:neuron projection extension; ISO:RGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:UniProtKB.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISS:UniProtKB.
DR GO; GO:0032736; P:positive regulation of interleukin-13 production; ISS:UniProtKB.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0051222; P:positive regulation of protein transport; IMP:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD.
DR GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; ISS:UniProtKB.
DR GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; ISS:UniProtKB.
DR GO; GO:0070528; P:protein kinase C signaling; IMP:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0047496; P:vesicle transport along microtubule; IMP:RGD.
DR CDD; cd21095; C1_aPKC_zeta; 1.
DR CDD; cd06404; PB1_aPKC; 1.
DR Gene3D; 3.30.60.20; -; 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; IPR047314; C1_aPKC_zeta.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR034877; PB1_aPKC.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR012233; PKC.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF241; PROTEIN KINASE C; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000554; PKC_zeta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS51745; PB1; 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; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; ATP-binding; Cell junction;
KW Cytoplasm; Endosome; Inflammatory response; Kinase; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..592
FT /note="Protein kinase C zeta type"
FT /id="PRO_0000055704"
FT DOMAIN 15..98
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 252..518
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 519..590
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 130..180
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 79..145
FT /note="Interaction with SQSTM1"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 258..266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 410
FT /note="Phosphothreonine; by PDPK1 and PI3K"
FT /evidence="ECO:0000250|UniProtKB:Q05513"
FT MOD_RES 560
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14580237,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..183
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059935"
FT MUTAGEN 62
FT /note="D->A: Loss of interaction with SQSTM1."
FT /evidence="ECO:0000269|PubMed:12813044"
FT CONFLICT 102..112
FT /note="QPGMPCPGEDK -> FRAEEAAEKAE (in Ref. 2; AAA41878 and
FT 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:4MJS"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:4MJS"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:4MJS"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4MJS"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4MJS"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:4MJS"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:4MJS"
SQ SEQUENCE 592 AA; 67733 MW; 5A3021171C2FD7C7 CRC64;
MPSRTDPKMD RSGGRVRLKA HYGGDILITS VDPTTTFQDL CEEVRDMCGL HQQHPLTLKW
VDSEGDPCTV SSQMELEEAF RLACQGRDEV LIIHVFPSIP EQPGMPCPGE DKSIYRRGAR
RWRKLYRANG HLFQAKRFNR RAYCGQCSER IWGLARQGYR CINCKLLVHK RCHVLVPLTC
RRHMDSVMPS QEPPVDDKND GVDLPSEETD GIAYISSSRK HDNIKDDSED LKPVIDGVDG
IKISQGLGLQ DFDLIRVIGR GSYAKVLLVR LKKNDQIYAM KVVKKELVHD DEDIDWVQTE
KHVFEQASSN PFLVGLHSCF QTTSRLFLVI EYVNGGDLMF HMQRQRKLPE EHARFYAAEI
CIALNFLHER GIIYRDLKLD NVLLDADGHI KLTDYGMCKE GLGPGDTTST FCGTPNYIAP
EILRGEEYGF SVDWWALGVL MFEMMAGRSP FDIITDNPDM NTEDYLFQVI LEKPIRIPRF
LSVKASHVLK GFLNKDPKER LGCRPQTGFS DIKSHAFFRS IDWDLLEKKQ TLPPFQPQIT
DDYGLDNFDT QFTSEPVQLT PDDEDVIKRI DQSEFEGFEY INPLLLSAEE SV
//
