KPCI_RAT
ID KPCI_RAT Reviewed; 596 AA.
AC F1M7Y5; B1PZT8;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 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 [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-596.
RC STRAIN=Wistar;
RX PubMed=19090727; DOI=10.1515/bc.2009.031;
RA Stross C., Keitel V., Winands E., Haussinger D., Kubitz R.;
RT "Expression and localization of atypical PKC isoforms in liver parenchymal
RT cells.";
RL Biol. Chem. 390:235-244(2009).
RN [3]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-265, AND MUTAGENESIS OF
RP TYR-265.
RX PubMed=11891849; DOI=10.1002/jcb.10101.abs;
RA White W.O., Seibenhener M.L., Wooten M.W.;
RT "Phosphorylation of tyrosine 256 facilitates nuclear import of atypical
RT protein kinase C.";
RL J. Cell. Biochem. 85:42-53(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564, AND IDENTIFICATION BY
RP 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 [5]
RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-564, AND DISRUPTION
RP PHENOTYPE.
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 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. Downstream of PI3K is required
CC for insulin-stimulated glucose transport. Activates RAB4A and promotes
CC its association with KIF3A which is required for the insulin-induced
CC SLC2A4/GLUT4 translocation in adipocytes. Is essential in early
CC embryogenesis and development of differentiating photoreceptors by
CC playing a role in the establishment of epithelial and neuronal polarity
CC (By similarity). Involved in early synaptic long term potentiation
CC phase in CA1 hippocampal cells and short term memory formation
CC (PubMed:27498875). {ECO:0000250, 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 -!- 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-412 (activation loop of the kinase domain) and Thr-564 (turn
CC motif), need to be phosphorylated for its full activation. Might also
CC be a target for novel lipid activators that are elevated during
CC nutrient-stimulated insulin secretion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with SQSTM1 and MP2K5 (By similarity).
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). Part of a complex with LLGL1 and
CC PARD6B. Interacts with ADAP1/CENTA1. Interaction with SMG1, through the
CC ZN-finger domain, activates the kinase activity. Interacts with CDK7.
CC Forms a complex with RAB2A and GAPDH involved in recruitment onto the
CC membrane of vesicular tubular clusters (VTCs). Interacts with ECT2
CC ('Thr-359' phosphorylated form). Interacts with VAMP2. Interacts with
CC WDFY2 (via WD repeats 1-3) (By similarity).
CC {ECO:0000250|UniProtKB:P41743, ECO:0000305}.
CC -!- INTERACTION:
CC F1M7Y5; Q62824: Exoc4; NbExp=2; IntAct=EBI-8795211, EBI-6959516;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891849}. Membrane
CC {ECO:0000250|UniProtKB:P41743}. Endosome
CC {ECO:0000250|UniProtKB:P41743}. Nucleus {ECO:0000269|PubMed:11891849}.
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 -!- TISSUE SPECIFICITY: Expressed in dorsal hippocampus (at protein level).
CC {ECO:0000269|PubMed:27498875}.
CC -!- DOMAIN: The PB1 domain mediates interaction with SQSTM1. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Thr-412 in the activation loop is not mandatory
CC for activation (By similarity). Upon neuronal growth factor (NGF)
CC stimulation, phosphorylated by SRC at Tyr-265, Tyr-280 and Tyr-334 (By
CC similarity). Phosphorylation at Tyr-265 facilitates binding to
CC KPNB1/importin-beta regulating entry of PRKCI into the nucleus
CC (PubMed:11891849). Phosphorylation on Tyr-334 is important for NF-
CC kappa-B stimulation (By similarity). Phosphorylated at Thr-564 during
CC the initial phase of long term potentiation (PubMed:27498875).
CC {ECO:0000250|UniProtKB:P41743, ECO:0000250|UniProtKB:Q62074,
CC ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:27498875}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the dorsal hippocampus
CC impairs the early phase of long-term potentiation and the formation of
CC short term memory. {ECO:0000269|PubMed:27498875}.
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; EU517502; ACA66272.1; -; mRNA.
DR RefSeq; NP_114448.1; NM_032059.1.
DR AlphaFoldDB; F1M7Y5; -.
DR SMR; F1M7Y5; -.
DR BioGRID; 249872; 4.
DR CORUM; F1M7Y5; -.
DR IntAct; F1M7Y5; 3.
DR MINT; F1M7Y5; -.
DR STRING; 10116.ENSRNOP00000012924; -.
DR iPTMnet; F1M7Y5; -.
DR PhosphoSitePlus; F1M7Y5; -.
DR jPOST; F1M7Y5; -.
DR PaxDb; F1M7Y5; -.
DR PRIDE; F1M7Y5; -.
DR Ensembl; ENSRNOT00000012924; ENSRNOP00000012924; ENSRNOG00000009652.
DR GeneID; 84006; -.
DR KEGG; rno:84006; -.
DR UCSC; RGD:620961; rat.
DR CTD; 5584; -.
DR RGD; 620961; Prkci.
DR eggNOG; KOG0695; Eukaryota.
DR GeneTree; ENSGT00940000153497; -.
DR HOGENOM; CLU_000288_63_29_1; -.
DR InParanoid; F1M7Y5; -.
DR OMA; RIQCFIC; -.
DR OrthoDB; 614710at2759; -.
DR TreeFam; TF102004; -.
DR Reactome; R-RNO-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-RNO-209543; p75NTR recruits signalling complexes.
DR Reactome; R-RNO-420029; Tight junction interactions.
DR PRO; PR:F1M7Y5; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000009652; Expressed in stomach and 20 other tissues.
DR Genevisible; F1M7Y5; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0031252; C:cell leading edge; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0120157; C:PAR polarity complex; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0004697; F:protein kinase C activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0016477; P:cell migration; IMP:RGD.
DR GO; GO:0045216; P:cell-cell junction organization; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:RGD.
DR GO; GO:0035089; P:establishment of apical/basal cell polarity; ISO:RGD.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISO:RGD.
DR GO; GO:0042462; P:eye photoreceptor cell development; ISO:RGD.
DR GO; GO:0048194; P:Golgi vesicle budding; IDA:RGD.
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:RGD.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
DR GO; GO:0070555; P:response to interleukin-1; IMP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IDA:RGD.
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 Acetylation; ATP-binding; Cytoplasm; Developmental protein; Endosome;
KW 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..596
FT /note="Protein kinase C iota type"
FT /id="PRO_0000414090"
FT DOMAIN 25..108
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 254..522
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 523..594
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..253
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 /evidence="ECO:0000250"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 260..268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 283
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 265
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:11891849"
FT MOD_RES 280
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT MOD_RES 334
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT MOD_RES 412
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:P41743"
FT MOD_RES 564
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27498875,
FT ECO:0007744|PubMed:22673903"
FT MUTAGEN 265
FT /note="Y->F: Loss of phosphorylation and nuclear import."
FT /evidence="ECO:0000269|PubMed:11891849"
FT CONFLICT 171
FT /note="C -> R (in Ref. 2; ACA66272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 68276 MW; 60035F56E7547C57 CRC64;
MPTQRDSSTM SHTVACGGGG DHSHQVRVKA YYRGDIMITH FEPSISFEGL CSEVRDMCSF
DNEQPFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE LLIHVFPCVP ERPGMPCPGE
DKSIYRRGAR RWRKLYCANG HTFQAKRFNR RAHCAICTDR IWGLGRQGYK CINCKLLVHK
KCHKLVTIEC GRHSLPPEPM MPMDQSSMHP DHTQTVIPYN PSSHESLDQV GEEKEAMNTR
ESGKASSSLG LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ
TEKHVFEQAS NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL PEEHARFYSA
EISLALNYLH ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC KEGLRPGDTT STFCGTPNYI
APEILRGEDY GFSVDWWALG VLMFEMMAGR SPFDIVGSSD NPDQNTEDYL FQVILEKQIR
IPRSLSVKAA SVLKSFLNKD PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK
PNISGEFGLD NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECV
