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Protein kinase C iota type (EC 2.7.11.13) (Atypical protein kinase C-lambda/iota) (aPKC-lambda/iota) (nPKC-iota)

 KPCI_RAT                Reviewed;         596 AA.
F1M7Y5; B1PZT8;
14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
03-MAY-2011, sequence version 1.
30-AUG-2017, entry version 58.
RecName: Full=Protein kinase C iota type;
EC=2.7.11.13;
AltName: Full=Atypical protein kinase C-lambda/iota;
Short=aPKC-lambda/iota;
AltName: Full=nPKC-iota;
Name=Prkci; Synonyms=Pkcl;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-596.
STRAIN=Wistar;
PubMed=19090727; DOI=10.1515/BC.2009.031;
Stross C., Keitel V., Winands E., Haussinger D., Kubitz R.;
"Expression and localization of atypical PKC isoforms in liver
parenchymal cells.";
Biol. Chem. 390:235-244(2009).
[3]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-265, AND MUTAGENESIS OF
TYR-265.
PubMed=11891849; DOI=10.1002/jcb.10101.abs;
White W.O., Seibenhener M.L., Wooten M.W.;
"Phosphorylation of tyrosine 256 facilitates nuclear import of
atypical protein kinase C.";
J. Cell. Biochem. 85:42-53(2002).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Calcium- and diacylglycerol-independent serine/
threonine-protein kinase that plays a general protective role
against apoptotic stimuli, is involved in NF-kappa-B activation,
cell survival, differentiation and polarity, and contributes to
the regulation of microtubule dynamics in the early secretory
pathway. Is necessary for BCR-ABL oncogene-mediated resistance to
apoptotic drug in leukemia cells, protecting leukemia cells
against drug-induced apoptosis. In cultured neurons, prevents
amyloid beta protein-induced apoptosis by interrupting cell death
process at a very early step. In glioblastoma cells, may function
downstream of phosphatidylinositol 3-kinase (PI3K) and PDPK1 in
the promotion of cell survival by phosphorylating and inhibiting
the pro-apoptotic factor BAD. Can form a protein complex in non-
small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and
regulate ECT2 oncogenic activity by phosphorylation, which in turn
promotes transformed growth and invasion. In response to nerve
growth factor (NGF), acts downstream of SRC to phosphorylate and
activate IRAK1, allowing the subsequent activation of NF-kappa-B
and neuronal cell survival. Functions in the organization of the
apical domain in epithelial cells by phosphorylating EZR. This
step is crucial for activation and normal distribution of EZR at
the early stages of intestinal epithelial cell differentiation.
Forms a protein complex with LLGL1 and PARD6B independently of
PARD3 to regulate epithelial cell polarity. Plays a role in
microtubule dynamics in the early secretory pathway through
interaction with RAB2A and GAPDH and recruitment to vesicular
tubular clusters (VTCs). In human coronary artery endothelial
cells (HCAEC), is activated by saturated fatty acids and mediates
lipid-induced apoptosis. Downstream of PI3K is required for
insulin-stimulated glucose transport. Activates RAB4A and promotes
its association with KIF3A which is required for the insulin-
induced SLC2A4/GLUT4 translocation in adipocytes. Is essential in
early embryogenesis and development of differentiating
photoreceptors by playing a role in the establishment of
epithelial and neuronal polarity (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Atypical PKCs (PRKCI and PRKCZ) exhibit an
elevated basal enzymatic activity (that may be due to the
interaction with SMG1 or SQSTM1) and are not regulated by
diacylglycerol, phosphatidylserine, phorbol esters or calcium
ions. Two specific sites, Thr-412 (activation loop of the kinase
domain) and Thr-564 (turn motif), need to be phosphorylated for
its full activation. Might also be a target for novel lipid
activators that are elevated during nutrient-stimulated insulin
secretion (By similarity). {ECO:0000250}.
-!- SUBUNIT: Forms a complex with SQSTM1 and MP2K5 (By similarity).
Interacts directly with SQSTM1 (Probable). Interacts with IKBKB.
Interacts with PARD6A, PARD6B and PARD6G. Part of a quaternary
complex containing aPKC, PARD3, a PARD6 protein (PARD6A, PARD6B or
PARD6G) and a GTPase protein (CDC42 or RAC1). Part of a complex
with LLGL1 and PARD6B. Interacts with ADAP1/CENTA1. Interaction
with SMG1, through the ZN-finger domain, activates the kinase
activity. Interacts with CDK7. Forms a complex with RAB2A and
GAPDH involved in recruitment onto the membrane of vesicular
tubular clusters (VTCs). Interacts with ECT2 ('Thr-359'
phosphorylated form). Interacts with VAMP2. Interacts with WDFY2
(via WD repeats 1-3) (By similarity).
{ECO:0000250|UniProtKB:P41743, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891849}.
Membrane {ECO:0000250|UniProtKB:P41743}. Endosome
{ECO:0000250|UniProtKB:P41743}. Nucleus
{ECO:0000269|PubMed:11891849}. Note=Transported into the endosome
through interaction with SQSTM1/p62. After phosphorylation by SRC,
transported into the nucleus through interaction with KPNB1.
Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to
vesicular tubular clusters (VTCs) through interaction with RAB2A.
{ECO:0000250|UniProtKB:P41743}.
-!- DOMAIN: The PB1 domain mediates interaction with SQSTM1.
{ECO:0000250}.
-!- DOMAIN: The C1 zinc finger does not bind diacylglycerol (DAG).
{ECO:0000250}.
-!- DOMAIN: The pseudosubstrate motif resembles the sequence around
sites phosphorylated on target proteins, except the presence of a
non-phosphorylatable residue in place of Ser, it modulates
activity by competing with substrates. {ECO:0000250}.
-!- PTM: Phosphorylation at Thr-412 in the activation loop is not
mandatory for activation (By similarity). Upon neuronal growth
factor (NGF) stimulation, phosphorylated by SRC at Tyr-265, Tyr-
280 and Tyr-334. Phosphorylation at Tyr-265 facilitates binding to
KPNB1/importin-beta regulating entry of PRKCI into the nucleus.
Phosphorylation on Tyr-334 is important for NF-kappa-B
stimulation. {ECO:0000250, ECO:0000269|PubMed:11891849}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; EU517502; ACA66272.1; -; mRNA.
RefSeq; NP_114448.1; NM_032059.1.
UniGene; Rn.1388; -.
SMR; F1M7Y5; -.
BioGrid; 249872; 3.
IntAct; F1M7Y5; 2.
STRING; 10116.ENSRNOP00000012924; -.
iPTMnet; F1M7Y5; -.
PhosphoSitePlus; F1M7Y5; -.
PaxDb; F1M7Y5; -.
PRIDE; F1M7Y5; -.
Ensembl; ENSRNOT00000012924; ENSRNOP00000012924; ENSRNOG00000009652.
GeneID; 84006; -.
KEGG; rno:84006; -.
UCSC; RGD:620961; rat.
CTD; 5584; -.
RGD; 620961; Prkci.
eggNOG; KOG0695; Eukaryota.
eggNOG; ENOG410ZMG2; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; F1M7Y5; -.
KO; K06069; -.
OMA; KGDIMIT; -.
OrthoDB; EOG091G03Q9; -.
TreeFam; TF102004; -.
Reactome; R-RNO-209543; p75NTR recruits signalling complexes.
Reactome; R-RNO-420029; Tight junction interactions.
PRO; PR:F1M7Y5; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000009652; -.
Genevisible; F1M7Y5; RN.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0031252; C:cell leading edge; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
GO; GO:0004697; F:protein kinase C activity; IDA:RGD.
GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
GO; GO:0016477; P:cell migration; IMP:RGD.
GO; GO:0045216; P:cell-cell junction organization; IEA:Ensembl.
GO; GO:0034613; P:cellular protein localization; IMP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:RGD.
GO; GO:0035089; P:establishment of apical/basal cell polarity; IEA:Ensembl.
GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
GO; GO:0048194; P:Golgi vesicle budding; IDA:RGD.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISS:UniProtKB.
GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0060252; P:positive regulation of glial cell proliferation; ISS:UniProtKB.
GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0070555; P:response to interleukin-1; IMP:RGD.
GO; GO:0043434; P:response to peptide hormone; IDA:RGD.
CDD; cd00029; C1; 1.
CDD; cd06404; PB1_aPKC; 1.
CDD; cd05618; STKc_aPKC_iota; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR034661; aPKC_iota.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR034877; PB1_aPKC.
InterPro; IPR000270; PB1_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR012233; PKC.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 1.
Pfam; PF00564; PB1; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000554; PKC_zeta; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 1.
SMART; SM00666; PB1; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS51745; PB1; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Developmental protein; Endosome; Kinase; Membrane; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Tumor suppressor; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P41743}.
CHAIN 2 596 Protein kinase C iota type.
/FTId=PRO_0000414090.
DOMAIN 25 108 PB1. {ECO:0000255|PROSITE-
ProRule:PRU01081}.
DOMAIN 254 522 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 523 594 AGC-kinase C-terminal.
ZN_FING 140 190 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 260 268 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 253 Regulatory domain. {ECO:0000250}.
REGION 2 28 Required for interaction with RAB2.
{ECO:0000250}.
REGION 72 91 Interaction with PARD6A. {ECO:0000250}.
MOTIF 125 134 Pseudosubstrate. {ECO:0000250}.
ACT_SITE 378 378 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 283 283 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylproline.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 3 3 Phosphothreonine.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 9 9 Phosphothreonine.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 265 265 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:11891849}.
MOD_RES 280 280 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 334 334 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 412 412 Phosphothreonine; by PDPK1.
{ECO:0000250|UniProtKB:Q62074}.
MOD_RES 564 564 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MUTAGEN 265 265 Y->F: Loss of phosphorylation and nuclear
import. {ECO:0000269|PubMed:11891849}.
CONFLICT 171 171 C -> R (in Ref. 2; ACA66272).
{ECO:0000305}.
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


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