KPCZ_MOUSE
ID KPCZ_MOUSE Reviewed; 592 AA.
AC Q02956; A2AD76; Q3UHM5; Q7TST7;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Protein kinase C zeta type;
DE EC=2.7.11.13 {ECO:0000269|PubMed:27187150};
DE AltName: Full=nPKC-zeta;
GN Name=Prkcz; Synonyms=Pkcz;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY (ISOFORM 1).
RX PubMed=1487145; DOI=10.1016/0378-1119(92)90219-f;
RA Goodnight J., Kazanietz M.G., Blumberg P.M., Mushinski F.J., Mischak H.;
RT "The cDNA sequence, expression pattern and protein characteristics of mouse
RT protein kinase C-zeta.";
RL Gene 122:305-311(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY (ISOFORMS 1
RP AND 2).
RC TISSUE=Brain;
RX PubMed=12932816; DOI=10.1016/s0304-3940(03)00780-8;
RA Hirai T., Niino Y.S., Chida K.;
RT "PKC zeta II, a small molecule of protein kinase C zeta, specifically
RT expressed in the mouse brain.";
RL Neurosci. Lett. 348:151-154(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH PARD6B.
RC TISSUE=Embryo;
RX PubMed=10934474; DOI=10.1038/35019573;
RA Joberty G., Petersen C., Gao L., Macara I.G.;
RT "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to
RT Cdc42.";
RL Nat. Cell Biol. 2:531-539(2000).
RN [7]
RP FUNCTION IN INFLAMMATORY RESPONSE.
RX PubMed=15987782; DOI=10.1073/pnas.0501202102;
RA Martin P., Villares R., Rodriguez-Mascarenhas S., Zaballos A., Leitges M.,
RA Kovac J., Sizing I., Rennert P., Marquez G., Martinez-A C., Diaz-Meco M.T.,
RA Moscat J.;
RT "Control of T helper 2 cell function and allergic airway inflammation by
RT PKCzeta.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9866-9871(2005).
RN [8]
RP INTERACTION WITH WDFY2.
RX PubMed=16792529; DOI=10.1042/bj20060511;
RA Fritzius T., Burkard G., Haas E., Heinrich J., Schweneker M., Bosse M.,
RA Zimmermann S., Frey A.D., Caelers A., Bachmann A.S., Moelling K.;
RT "A WD-FYVE protein binds to the kinases Akt and PKCzeta/lambda.";
RL Biochem. J. 399:9-20(2006).
RN [9]
RP INTERACTION WITH VAMP2, COMPLEX FORMATION WITH VAMP2 AND WDFY2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17313651; DOI=10.1111/j.1742-4658.2007.05702.x;
RA Fritzius T., Frey A.D., Schweneker M., Mayer D., Moelling K.;
RT "WD-repeat-propeller-FYVE protein, ProF, binds VAMP2 and protein kinase
RT Czeta.";
RL FEBS J. 274:1552-1566(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-560, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION.
RX PubMed=21131967; DOI=10.1038/ni.1968;
RA Levy D., Kuo A.J., Chang Y., Schaefer U., Kitson C., Cheung P., Espejo A.,
RA Zee B.M., Liu C.L., Tangsombatvisit S., Tennen R.I., Kuo A.Y., Tanjing S.,
RA Cheung R., Chua K.F., Utz P.J., Shi X., Prinjha R.K., Lee K., Garcia B.A.,
RA Bedford M.T., Tarakhovsky A., Cheng X., Gozani O.;
RT "Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity
RT of the histone methyltransferase GLP at chromatin to tonic repression of
RT NF-kappaB signaling.";
RL Nat. Immunol. 12:29-36(2011).
RN [12]
RP TISSUE SPECIFICITY (ISOFORMS 1 AND 2), AND DISRUPTION PHENOTYPE (ISOFORMS 1
RP AND 2).
RX PubMed=23283171; DOI=10.1038/nature11803;
RA Lee A.M., Kanter B.R., Wang D., Lim J.P., Zou M.E., Qiu C., McMahon T.,
RA Dadgar J., Fischbach-Weiss S.C., Messing R.O.;
RT "Prkcz null mice show normal learning and memory.";
RL Nature 493:416-419(2013).
RN [13]
RP FUNCTION (ISOFORM 2), CATALYTIC ACTIVITY (ISOFORM 2), INDUCTION (ISOFORM
RP 2), AND DISRUPTION PHENOTYPE (ISOFORMS 1 AND 2).
RX PubMed=27187150; DOI=10.7554/elife.14846;
RA Tsokas P., Hsieh C., Yao Y., Lesburgueres E., Wallace E.J.C.,
RA Tcherepanov A., Jothianandan D., Hartley B.R., Pan L., Rivard B.,
RA Farese R.V., Sajan M.P., Bergold P.J., Hernandez A.I., Cottrell J.E.,
RA Shouval H.Z., Fenton A.A., Sacktor T.C.;
RT "Compensation for PKMzeta in long-term potentiation and spatial long-term
RT memory in mutant mice.";
RL Elife 5:0-0(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:15987782,
CC ECO:0000269|PubMed:21131967}.
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:27187150}.
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:27187150};
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:27187150};
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 (By similarity). Isoform 2: Constitutively active (By
CC similarity). {ECO:0000250|UniProtKB:P09217}.
CC -!- SUBUNIT: Interacts directly with SQSTM1. Forms a ternary complex with
CC SQSTM1 and KCNAB2. Forms another ternary complex with SQSTM1 and
CC GABRR3. Forms a complex with SQSTM1 and MAP2K5 (By similarity).
CC Interacts with PARD6A, PARD6B and PARD6G. Part of a complex with PARD3,
CC PARD6A or PARD6B or PARD6G and CDC42 or RAC1. Interacts with
CC ADAP1/CENTA1. Interacts (via the protein kinase domain) with WWC1.
CC Forms a tripartite complex with WWC1 and DDR1, but predominantly in the
CC absence of collagen. Interacts with PDPK1 (via N-terminal region) (By
CC similarity). Interacts with WDFY2 (via WD repeats 1-3)
CC (PubMed:16792529). Interacts with VAMP2 (PubMed:17313651). Forms a
CC complex with WDFY2 and VAMP2 (PubMed:17313651). Interacts with APPL1
CC (By similarity). {ECO:0000250|UniProtKB:P09217,
CC ECO:0000250|UniProtKB:Q05513, ECO:0000269|PubMed:16792529,
CC ECO:0000269|PubMed:17313651}.
CC -!- INTERACTION:
CC Q02956; Q62151: Ager; NbExp=7; IntAct=EBI-642057, EBI-6665091;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05513}.
CC Endosome {ECO:0000250|UniProtKB:Q05513}. Cell junction
CC {ECO:0000250|UniProtKB:Q05513}. Membrane
CC {ECO:0000250|UniProtKB:P09217}; Peripheral membrane protein
CC {ECO:0000305}. Note=In the retina, localizes in the terminals of the
CC rod bipolar cells (By similarity). Associated with endosomes (By
CC similarity). Presence of KRIT1, CDH5 and RAP1B is required for its
CC localization to the cell junction (By similarity). Colocalizes with
CC VAMP2 and WDFY2 in intracellular vesicles (PubMed:17313651).
CC Transiently translocates to the membrane of CA1 hippocampal cells in
CC response to the induction of long term potentiation (By similarity).
CC {ECO:0000250|UniProtKB:P09217, ECO:0000250|UniProtKB:Q05513,
CC ECO:0000269|PubMed:17313651}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000250|UniProtKB:P09217}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=Q02956-1; Sequence=Displayed;
CC Name=2; Synonyms=PKCzetaII {ECO:0000303|PubMed:12932816}, PMKzeta
CC {ECO:0000303|PubMed:23283171};
CC IsoId=Q02956-2; Sequence=VSP_059934;
CC -!- TISSUE SPECIFICITY: Isoform 1: In brain, highly expressed in cerebellar
CC granule neurons and cerebellar astrocytes (at protein level)
CC (PubMed:1487145, PubMed:12932816). Expressed at low levels in testes,
CC lung and kidney (PubMed:1487145, PubMed:23283171). Isoform 2:
CC Specifically expressed in brain where it localizes to cerebellar
CC granule neurons (at protein level) (PubMed:12932816, PubMed:23283171).
CC {ECO:0000269|PubMed:12932816, ECO:0000269|PubMed:1487145,
CC ECO:0000269|PubMed:23283171}.
CC -!- INDUCTION: [Isoform 2]: Induced during synaptic long term potentiation.
CC {ECO:0000269|PubMed:27187150}.
CC -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
CC -!- DOMAIN: The PB1 domain mediate mutually exclusive interactions with
CC SQSTM1 and PARD6B. {ECO:0000250}.
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: No visible phenotype (PubMed:23283171). Reduced
CC anxiety-like behavior in males (PubMed:23283171). Does not affect long
CC term memory maintenance (PubMed:23283171, PubMed:27187150). However,
CC when the conditions during the establishment of memory are more
CC demanding, spatial long term memory maintenance is slightly affected
CC (PubMed:27187150). Up-regulation of PRKCI/PKCiota protein levels
CC following induction of synaptic long term potentiation abnormally
CC persist. This compensatory mechanism is responsible for the lack of
CC defect in long term memory maintenance in absence of isoform 1 and
CC isoform 2 (PubMed:27187150). Isoform 2: RNAi-mediated knockdown
CC prevents late synaptic long term potentiation and spatial long term
CC memory (PubMed:27187150). {ECO:0000269|PubMed:23283171,
CC ECO:0000269|PubMed:27187150}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:12932816}.
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; M94632; AAA39983.1; -; mRNA.
DR EMBL; AB110830; BAC76975.1; -; mRNA.
DR EMBL; AK147300; BAE27832.1; -; mRNA.
DR EMBL; AL670227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL670413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466594; EDL15000.1; -; Genomic_DNA.
DR CCDS; CCDS19026.1; -. [Q02956-1]
DR CCDS; CCDS19027.1; -. [Q02956-2]
DR PIR; JC1480; JC1480.
DR RefSeq; NP_032886.2; NM_008860.3. [Q02956-1]
DR AlphaFoldDB; Q02956; -.
DR SMR; Q02956; -.
DR BioGRID; 202203; 34.
DR CORUM; Q02956; -.
DR ELM; Q02956; -.
DR IntAct; Q02956; 18.
DR MINT; Q02956; -.
DR STRING; 10090.ENSMUSP00000030922; -.
DR iPTMnet; Q02956; -.
DR PhosphoSitePlus; Q02956; -.
DR MaxQB; Q02956; -.
DR PaxDb; Q02956; -.
DR PRIDE; Q02956; -.
DR ProteomicsDB; 264865; -. [Q02956-1]
DR Antibodypedia; 3869; 854 antibodies from 45 providers.
DR DNASU; 18762; -.
DR Ensembl; ENSMUST00000030922; ENSMUSP00000030922; ENSMUSG00000029053. [Q02956-1]
DR Ensembl; ENSMUST00000103178; ENSMUSP00000099467; ENSMUSG00000029053. [Q02956-2]
DR GeneID; 18762; -.
DR KEGG; mmu:18762; -.
DR UCSC; uc008wdc.2; mouse. [Q02956-1]
DR CTD; 5590; -.
DR MGI; MGI:97602; Prkcz.
DR VEuPathDB; HostDB:ENSMUSG00000029053; -.
DR eggNOG; KOG0695; Eukaryota.
DR GeneTree; ENSGT00940000153497; -.
DR HOGENOM; CLU_000288_63_29_1; -.
DR InParanoid; Q02956; -.
DR OMA; IPEEPGM; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; Q02956; -.
DR TreeFam; TF102004; -.
DR BRENDA; 2.7.11.13; 3474.
DR Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-MMU-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-MMU-9634635; Estrogen-stimulated signaling through PRKCZ.
DR BioGRID-ORCS; 18762; 1 hit in 75 CRISPR screens.
DR PRO; PR:Q02956; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q02956; protein.
DR Bgee; ENSMUSG00000029053; Expressed in superior frontal gyrus and 175 other tissues.
DR ExpressionAtlas; Q02956; baseline and differential.
DR Genevisible; Q02956; MM.
DR GO; GO:0045179; C:apical cortex; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0043203; C:axon hillock; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IGI:MGI.
DR GO; GO:0035748; C:myelin sheath abaxonal region; IDA:BHF-UCL.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISO:MGI.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0015459; F:potassium channel regulator activity; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004697; F:protein kinase C activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031584; P:activation of phospholipase D activity; ISO:MGI.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0007616; P:long-term memory; ISO:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0051899; P:membrane depolarization; ISO:MGI.
DR GO; GO:0060081; P:membrane hyperpolarization; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; ISO:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:1990138; P:neuron projection extension; IGI:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:UniProtKB.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:UniProtKB.
DR GO; GO:0032736; P:positive regulation of interleukin-13 production; IMP:UniProtKB.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IMP:UniProtKB.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0051222; P:positive regulation of protein transport; ISO:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:MGI.
DR GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; IMP:UniProtKB.
DR GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IMP:UniProtKB.
DR GO; GO:0070528; P:protein kinase C signaling; ISO:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISO:MGI.
DR CDD; cd00029; C1; 1.
DR CDD; cd06404; PB1_aPKC; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
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 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; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 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 Alternative promoter usage; ATP-binding; Cell junction; Cytoplasm;
KW Endosome; Inflammatory response; Kinase; Membrane; Metal-binding;
KW 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_0000055702"
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 /evidence="ECO:0000250"
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:0007744|PubMed:21183079"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09217"
FT VAR_SEQ 1..183
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059934"
FT CONFLICT 197
FT /note="D -> G (in Ref. 1; AAA39983 and 2; BAC76975)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="H -> R (in Ref. 3; BAE27832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 67682 MW; 690AD891C25BC311 CRC64;
MPSRTDPKMD RSGGRVRLKA HYGGDILITS VDAMTTFKDL CEEVRDMCGL HQQHPLTLKW
VDSEGDPCTV SSQMELEEAF RLVCQGRDEV LIIHVFPSIP EQPGMPCPGE DKSIYRRGAR
RWRKLYRANG HLFQAKRFNR GAYCGQCSER IWGLSRQGYR 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
