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 24-JAN-2024, entry version 226. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyGen; Q62074; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q62074; -. DR PhosphoSitePlus; Q62074; -. DR EPD; Q62074; -. DR MaxQB; Q62074; -. DR PaxDb; 10090-ENSMUSP00000103884; -. DR ProteomicsDB; 264793; -. DR Pumba; Q62074; -. DR Antibodypedia; 4271; 271 antibodies from 37 providers. DR DNASU; 18759; -. DR Ensembl; ENSMUST00000108249.9; ENSMUSP00000103884.3; ENSMUSG00000037643.15. DR GeneID; 18759; -. DR KEGG; mmu:18759; -. DR UCSC; uc008ovs.1; mouse. DR AGR; MGI:99260; -. 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; FIDWEAL; -. DR OrthoDB; 841660at2759; -. 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 Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway. DR BioGRID-ORCS; 18759; 2 hits in 83 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 277 other cell types or tissues. DR ExpressionAtlas; Q62074; baseline and differential. 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; IEA:Ensembl. DR GO; GO:0005903; C:brush border; IDA: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: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:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IDA:BHF-UCL. 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: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: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: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; cd20794; C1_aPKC; 1. DR CDD; cd06404; PB1_aPKC; 1. DR CDD; cd05618; STKc_aPKC_iota; 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; 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 PANTHER; PTHR24351:SF236; PROTEIN KINASE C IOTA TYPE; 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. DR Genevisible; Q62074; MM. 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 //