KPCI_MOUSE
ID KPCI_MOUSE Reviewed; 595 AA.
AC Q62074;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Protein kinase C iota type;
DE EC=2.7.11.13;
DE AltName: Full=Atypical protein kinase C-lambda/iota;
DE Short=aPKC-lambda/iota;
DE AltName: Full=nPKC-iota;
GN Name=Prkci; Synonyms=Pkcl;
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].
RX PubMed=7513693; DOI=10.1016/s0021-9258(18)99929-1;
RA Akimoto K., Mizuno K., Osada S., Hirai S., Tanuma S., Suzuki K., Ohno S.;
RT "A new member of the third class in the protein kinase C family, PKC
RT lambda, expressed dominantly in an undifferentiated mouse embryonal
RT carcinoma cell line and also in many tissues and cells.";
RL J. Biol. Chem. 269:12677-12683(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=9971737; DOI=10.1083/jcb.144.3.413;
RA Uberall F., Hellbert K., Kampfer S., Maly K., Villunger A., Spitaler M.,
RA Mwanjewe J., Baier-Bitterlich G., Baier G., Grunicke H.H.;
RT "Evidence that atypical protein kinase C-lambda and atypical protein kinase
RT C-zeta participate in Ras-mediated reorganization of the F-actin
RT cytoskeleton.";
RL J. Cell Biol. 144:413-425(1999).
RN [4]
RP SUBUNIT OF A COMPLEX CONTAINING PARD6B; PARD3 AND CDC42.
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 [5]
RP INTERACTION WITH SQSTM1 AND MAP2K5, AND MUTAGENESIS OF ARG-27; VAL-28;
RP LYS-29; TRP-70; ASP-72; GLU-74; ASP-76; GLN-83 AND GLU-85.
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 [6]
RP FUNCTION.
RX PubMed=12832475; DOI=10.1128/mcb.23.14.4892-4900.2003;
RA Imamura T., Huang J., Usui I., Satoh H., Bever J., Olefsky J.M.;
RT "Insulin-induced GLUT4 translocation involves protein kinase C-lambda-
RT mediated functional coupling between Rab4 and the motor protein kinesin.";
RL Mol. Cell. Biol. 23:4892-4900(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15322187; DOI=10.4049/jimmunol.173.5.3250;
RA Soloff R.S., Katayama C., Lin M.Y., Feramisco J.R., Hedrick S.M.;
RT "Targeted deletion of protein kinase C lambda reveals a distribution of
RT functions between the two atypical protein kinase C isoforms.";
RL J. Immunol. 173:3250-3260(2004).
RN [8]
RP FUNCTION.
RX PubMed=14615604; DOI=10.1210/me.2003-0087;
RA Bandyopadhyay G., Standaert M.L., Sajan M.P., Kanoh Y., Miura A., Braun U.,
RA Kruse F., Leitges M., Farese R.V.;
RT "Protein kinase C-lambda knockout in embryonic stem cells and adipocytes
RT impairs insulin-stimulated glucose transport.";
RL Mol. Endocrinol. 18:373-383(2004).
RN [9]
RP FUNCTION.
RX PubMed=16267237; DOI=10.1523/jneurosci.3657-05.2005;
RA Koike C., Nishida A., Akimoto K., Nakaya M.A., Noda T., Ohno S.,
RA Furukawa T.;
RT "Function of atypical protein kinase C lambda in differentiating
RT photoreceptors is required for proper lamination of mouse retina.";
RL J. Neurosci. 25:10290-10298(2005).
RN [10]
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 [11]
RP INTERACTION WITH VAMP2.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-563, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Testis;
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 [14]
RP DEVELOPMENTAL STAGE.
RX PubMed=20399730; DOI=10.1016/j.neuron.2010.03.019;
RA Kim S., Lehtinen M.K., Sessa A., Zappaterra M.W., Cho S.H., Gonzalez D.,
RA Boggan B., Austin C.A., Wijnholds J., Gambello M.J., Malicki J.,
RA LaMantia A.S., Broccoli V., Walsh C.A.;
RT "The apical complex couples cell fate and cell survival to cerebral
RT cortical development.";
RL Neuron 66:69-84(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 231-595 IN COMPLEX WITH RAT PARD3
RP PEPTIDE, PHOSPHORYLATION AT THR-563, AND PSEUDOSUBSTRATE MOTIF.
RX PubMed=22579248; DOI=10.1016/j.str.2012.02.022;
RA Wang C., Shang Y., Yu J., Zhang M.;
RT "Substrate recognition mechanism of atypical protein kinase Cs revealed by
RT the structure of PKCiota in complex with a substrate peptide from Par-3.";
RL Structure 20:791-801(2012).
CC -!- FUNCTION: Calcium- and diacylglycerol-independent serine/ threonine-
CC protein kinase that plays a general protective role against apoptotic
CC stimuli, is involved in NF-kappa-B activation, cell survival,
CC differentiation and polarity, and contributes to the regulation of
CC microtubule dynamics in the early secretory pathway. Is necessary for
CC BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia
CC cells, protecting leukemia cells against drug-induced apoptosis. In
CC cultured neurons, prevents amyloid beta protein-induced apoptosis by
CC interrupting cell death process at a very early step. In glioblastoma
CC cells, may function downstream of phosphatidylinositol 3-kinase (PI3K)
CC and PDPK1 in the promotion of cell survival by phosphorylating and
CC inhibiting the pro-apoptotic factor BAD. Can form a protein complex in
CC non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and
CC regulate ECT2 oncogenic activity by phosphorylation, which in turn
CC promotes transformed growth and invasion. In response to nerve growth
CC factor (NGF), acts downstream of SRC to phosphorylate and activate
CC IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal
CC cell survival. Functions in the organization of the apical domain in
CC epithelial cells by phosphorylating EZR. This step is crucial for
CC activation and normal distribution of EZR at the early stages of
CC intestinal epithelial cell differentiation. Forms a protein complex
CC with LLGL1 and PARD6B independently of PARD3 to regulate epithelial
CC cell polarity. Plays a role in microtubule dynamics in the early
CC secretory pathway through interaction with RAB2A and GAPDH and
CC recruitment to vesicular tubular clusters (VTCs). In human coronary
CC artery endothelial cells (HCAEC), is activated by saturated fatty acids
CC and mediates lipid-induced apoptosis (By similarity). Downstream of
CC PI3K is required for insulin-stimulated glucose transport. Activates
CC RAB4A and promotes its association with KIF3A which is required for the
CC insulin-induced SLC2A4/GLUT4 translocation in adipocytes. Is essential
CC in early embryogenesis and development of differentiating
CC photoreceptors by playing a role in the establishment of epithelial and
CC neuronal polarity. Involved in early synaptic long term potentiation
CC phase in CA1 hippocampal cells and short term memory formation (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:F1M7Y5,
CC ECO:0000269|PubMed:12832475, ECO:0000269|PubMed:14615604,
CC ECO:0000269|PubMed:15322187, ECO:0000269|PubMed:16267237,
CC ECO:0000269|PubMed:9971737}.
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 -!- 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-411 (activation loop of the kinase domain) and Thr-563 (turn
CC motif), need to be phosphorylated for its full activation (By
CC similarity). Might also be a target for novel lipid activators that are
CC elevated during nutrient-stimulated insulin secretion. {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with SQSTM1 and MP2K5 (PubMed:12813044).
CC Interacts directly with SQSTM1 (Probable). Interacts with IKBKB.
CC Interacts with PARD6A, PARD6B and PARD6G. Part of a quaternary complex
CC containing aPKC, PARD3, a PARD6 protein (PARD6A, PARD6B or PARD6G) and
CC a GTPase protein (CDC42 or RAC1) (PubMed:10934474). Part of a complex
CC with LLGL1 and PARD6B. Interacts with ADAP1/CENTA1. Interaction with
CC SMG1, through the ZN-finger domain, activates the kinase activity.
CC Interacts with CDK7. Forms a complex with RAB2A and GAPDH involved in
CC recruitment onto the membrane of vesicular tubular clusters (VTCs).
CC Interacts with ECT2 ('Thr-359' phosphorylated form) (By similarity).
CC Interacts with VAMP2 (PubMed:17313651). Interacts with WDFY2 (via WD
CC repeats 1-3) (PubMed:16792529). {ECO:0000250|UniProtKB:P41743,
CC ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:12813044,
CC ECO:0000269|PubMed:16792529, ECO:0000269|PubMed:17313651, ECO:0000305}.
CC -!- INTERACTION:
CC Q62074; Q8R1S4: Mtss1; NbExp=4; IntAct=EBI-82016, EBI-15622277;
CC Q62074; Q8TEW0: PARD3; Xeno; NbExp=7; IntAct=EBI-82016, EBI-81968;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41743}.
CC Membrane {ECO:0000250|UniProtKB:P41743}. Endosome
CC {ECO:0000250|UniProtKB:P41743}. Nucleus {ECO:0000250|UniProtKB:P41743}.
CC Note=Transported into the endosome through interaction with SQSTM1/p62.
CC After phosphorylation by SRC, transported into the nucleus through
CC interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and
CC nucleus. Transported to vesicular tubular clusters (VTCs) through
CC interaction with RAB2A. {ECO:0000250|UniProtKB:P41743}.
CC -!- DEVELOPMENTAL STAGE: Expressed apically in the cortical neuroepithelium
CC along the ventricular surface at 14.5 dpc.
CC {ECO:0000269|PubMed:20399730}.
CC -!- DOMAIN: The PB1 domain mediates interaction with SQSTM1.
CC -!- DOMAIN: The C1 zinc finger does not bind diacylglycerol (DAG).
CC {ECO:0000250}.
CC -!- DOMAIN: The pseudosubstrate motif resembles the sequence around sites
CC phosphorylated on target proteins, except the presence of a non-
CC phosphorylatable residue in place of Ser, it modulates activity by
CC competing with substrates.
CC -!- PTM: Phosphorylation at Thr-411 in the activation loop is not mandatory
CC for activation (PubMed:22579248). Upon neuronal growth factor (NGF)
CC stimulation, phosphorylated by SRC at Tyr-264, Tyr-279 and Tyr-333 (By
CC similarity). Phosphorylation on Tyr-264 facilitates binding to
CC KPNB1/importin-beta regulating entry of PRKCI into the nucleus (By
CC similarity). Phosphorylation on Tyr-333 is important for NF-kappa-B
CC stimulation (By similarity). Phosphorylated at Thr-563 during the
CC initial phase of long term potentiation (By similarity).
CC {ECO:0000250|UniProtKB:F1M7Y5, ECO:0000250|UniProtKB:P41743,
CC ECO:0000269|PubMed:22579248}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal at 9.5 dpc.
CC {ECO:0000269|PubMed:15322187}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21630.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA32499.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D28577; BAA32499.1; ALT_INIT; mRNA.
DR EMBL; BC021630; AAH21630.1; ALT_INIT; mRNA.
DR CCDS; CCDS17289.2; -.
DR PIR; A53758; A53758.
DR RefSeq; NP_032883.2; NM_008857.3.
DR PDB; 4DC2; X-ray; 2.40 A; A=231-595.
DR PDBsum; 4DC2; -.
DR AlphaFoldDB; Q62074; -.
DR SMR; Q62074; -.
DR BioGRID; 202200; 35.
DR CORUM; Q62074; -.
DR DIP; DIP-32555N; -.
DR IntAct; Q62074; 32.
DR STRING; 10090.ENSMUSP00000103884; -.
DR iPTMnet; Q62074; -.
DR PhosphoSitePlus; Q62074; -.
DR EPD; Q62074; -.
DR MaxQB; Q62074; -.
DR PaxDb; Q62074; -.
DR PRIDE; Q62074; -.
DR ProteomicsDB; 264793; -.
DR Antibodypedia; 4271; 233 antibodies from 37 providers.
DR DNASU; 18759; -.
DR Ensembl; ENSMUST00000108249; ENSMUSP00000103884; ENSMUSG00000037643.
DR GeneID; 18759; -.
DR KEGG; mmu:18759; -.
DR UCSC; uc008ovs.1; mouse.
DR CTD; 5584; -.
DR MGI; MGI:99260; Prkci.
DR VEuPathDB; HostDB:ENSMUSG00000037643; -.
DR eggNOG; KOG0695; Eukaryota.
DR GeneTree; ENSGT00940000153497; -.
DR HOGENOM; CLU_000288_63_29_1; -.
DR InParanoid; Q62074; -.
DR OMA; RIQCFIC; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; Q62074; -.
DR TreeFam; TF102004; -.
DR BRENDA; 2.7.11.13; 3474.
DR Reactome; R-MMU-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-MMU-209543; p75NTR recruits signalling complexes.
DR Reactome; R-MMU-420029; Tight junction interactions.
DR BioGRID-ORCS; 18759; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Prkci; mouse.
DR PRO; PR:Q62074; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q62074; protein.
DR Bgee; ENSMUSG00000037643; Expressed in molar tooth and 274 other tissues.
DR ExpressionAtlas; Q62074; baseline and differential.
DR Genevisible; Q62074; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:HGNC.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0120157; C:PAR polarity complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
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:0005543; F:phospholipid binding; ISS:HGNC.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0004697; F:protein kinase C activity; IDA:BHF-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:HGNC.
DR GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0045216; P:cell-cell junction organization; ISS:HGNC.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
DR GO; GO:0035089; P:establishment of apical/basal cell polarity; IMP:MGI.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISO:MGI.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR GO; GO:0048194; P:Golgi vesicle budding; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISS:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; ISO:MGI.
DR GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR CDD; cd00029; C1; 1.
DR CDD; cd06404; PB1_aPKC; 1.
DR CDD; cd05618; STKc_aPKC_iota; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR034661; aPKC_iota.
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 3D-structure; Acetylation; ATP-binding; Cytoplasm; Developmental protein;
KW Endosome; Kinase; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tumor suppressor; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT CHAIN 2..595
FT /note="Protein kinase C iota type"
FT /id="PRO_0000055711"
FT DOMAIN 25..108
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 253..521
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 522..593
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 140..190
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..252
FT /note="Regulatory domain"
FT /evidence="ECO:0000250"
FT REGION 2..28
FT /note="Required for interaction with RAB2"
FT /evidence="ECO:0000250"
FT REGION 72..91
FT /note="Interaction with PARD6A"
FT /evidence="ECO:0000250"
FT MOTIF 125..134
FT /note="Pseudosubstrate"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 259..267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT MOD_RES 264
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT MOD_RES 279
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT MOD_RES 333
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 563
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22579248,
FT ECO:0007744|PubMed:21183079"
FT MUTAGEN 27
FT /note="R->A: No effect on interaction with SQSTM1."
FT /evidence="ECO:0000269|PubMed:12813044"
FT MUTAGEN 28
FT /note="V->A: No effect on interaction with SQSTM1; when
FT associated with A-29."
FT /evidence="ECO:0000269|PubMed:12813044"
FT MUTAGEN 29
FT /note="K->A: No effect on interaction with SQSTM1; when
FT associated with A-118."
FT /evidence="ECO:0000269|PubMed:12813044"
FT MUTAGEN 70
FT /note="W->A: Loss of interaction with SQSTM1."
FT /evidence="ECO:0000269|PubMed:12813044"
FT MUTAGEN 72
FT /note="D->A: Loss of interaction with SQSTM1."
FT /evidence="ECO:0000269|PubMed:12813044"
FT MUTAGEN 74
FT /note="E->A: Loss of interaction with SQSTM1."
FT /evidence="ECO:0000269|PubMed:12813044"
FT MUTAGEN 76
FT /note="D->A: Loss of interaction with SQSTM1."
FT /evidence="ECO:0000269|PubMed:12813044"
FT MUTAGEN 83
FT /note="Q->A: No effect on interaction with SQSTM1."
FT /evidence="ECO:0000269|PubMed:12813044"
FT MUTAGEN 85
FT /note="E->A: Loss of interaction with SQSTM1."
FT /evidence="ECO:0000269|PubMed:12813044"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:4DC2"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:4DC2"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:4DC2"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4DC2"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:4DC2"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:4DC2"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 351..370
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:4DC2"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:4DC2"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 432..447
FT /evidence="ECO:0007829|PDB:4DC2"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 466..475
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 486..495
FT /evidence="ECO:0007829|PDB:4DC2"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:4DC2"
FT TURN 508..510
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 511..517
FT /evidence="ECO:0007829|PDB:4DC2"
FT TURN 519..523
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 526..530
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 553..556
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:4DC2"
FT HELIX 575..578
FT /evidence="ECO:0007829|PDB:4DC2"
SQ SEQUENCE 595 AA; 68203 MW; 6AC612D1E9264825 CRC64;
MPTQRDSSTM SHTVACGGGG DHSHQVRVKA YYRGDIMITH FEPSISFEGL CSEVRDMCSF
DNEQPFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE LLIHVFPCVP ERPGMPCPGE
DKSIYRRGAR RWRKLYCANG HTFQAKRFNR RAHCAICTDR IWGLGRQGYK CINCKLLVHK
KCHKLVTIEC GRHSLPPEPM MPMDQTMHPD HTQTVIPYNP SSHESLDQVG EEKEAMNTRE
SGKASSSLGL QDFDLLRVIG RGSYAKVLLV RLKKTDRIYA MKVVKKELVN DDEDIDWVQT
EKHVFEQASN HPFLVGLHSC FQTESRLFFV IEYVNGGDLM FHMQRQRKLP EEHARFYSAE
ISLALNYLHE RGIIYRDLKL DNVLLDSEGH IKLTDYGMCK EGLRPGDTTS TFCGTPNYIA
PEILRGEDYG FSVDWWALGV LMFEMMAGRS PFDIVGSSDN PDQNTEDYLF QVILEKQIRI
PRSLSVKAAS VLKSFLNKDP KERLGCHPQT GFADIQGHPF FRNVDWDMME QKQVVPPFKP
NISGEFGLDN FDSQFTNEPV QLTPDDDDIV RKIDQSEFEG FEYINPLLMS AEECV
