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Protein kinase C eta type (EC 2.7.11.13) (PKC-L) (nPKC-eta)

 KPCL_MOUSE              Reviewed;         683 AA.
P23298; Q8K2K8;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
23-MAY-2018, entry version 176.
RecName: Full=Protein kinase C eta type;
EC=2.7.11.13;
AltName: Full=PKC-L;
AltName: Full=nPKC-eta;
Name=Prkch; Synonyms=Pkch;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Epidermis;
PubMed=2266135;
Osada S., Mizuno K., Saido T.C., Akita Y., Suzuki K., Kuroki T.,
Ohno S.;
"A phorbol ester receptor/protein kinase, nPKC eta, a new member of
the protein kinase C family predominantly expressed in lung and
skin.";
J. Biol. Chem. 265:22434-22440(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N-3; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, INTERACTION WITH FYN, AND SUBCELLULAR LOCATION.
PubMed=11106751; DOI=10.1016/S1097-2765(00)00110-6;
Cabodi S., Calautti E., Talora C., Kuroki T., Stein P.L., Dotto G.P.;
"A PKC-eta/Fyn-dependent pathway leading to keratinocyte growth arrest
and differentiation.";
Mol. Cell 6:1121-1129(2000).
[5]
FUNCTION IN B-CELL SIGNALING.
PubMed=18780722; DOI=10.1093/intimm/dxn101;
Oda A., Ono T., Yamamoto M., Goitsuka R., Kitamura D.;
"PKC eta directs induction of IRF-4 expression and Ig kappa gene
rearrangement in pre-BCR signaling pathway.";
Int. Immunol. 20:1417-1426(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
FUNCTION, INTERACTION WITH RALA, AND SUBCELLULAR LOCATION.
PubMed=21346190; DOI=10.1091/mbc.E10-09-0754;
Shirai Y., Morioka S., Sakuma M., Yoshino K., Otsuji C., Sakai N.,
Kashiwagi K., Chida K., Shirakawa R., Horiuchi H., Nishigori C.,
Ueyama T., Saito N.;
"Direct binding of RalA to PKC? and its crucial role in morphological
change during keratinocyte differentiation.";
Mol. Biol. Cell 22:1340-1352(2011).
-!- FUNCTION: Calcium-independent, phospholipid- and diacylglycerol
(DAG)-dependent serine/threonine-protein kinase that is involved
in the regulation of cell differentiation in keratinocytes and
pre-B cell receptor, mediates regulation of epithelial tight
junction integrity and foam cell formation, and is required for
glioblastoma proliferation and apoptosis prevention in MCF-7
cells. In keratinocytes, binds and activates the tyrosine kinase
FYN, which in turn blocks epidermal growth factor receptor (EGFR)
signaling and leads to keratinocyte growth arrest and
differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B
complex and inhibits CDK2 kinase activity, leading to RB1
dephosphorylation and thereby G1 arrest in keratinocytes. In
association with RALA activates actin depolymerization, which is
necessary for keratinocyte differentiation. In the pre-B cell
receptor signaling, functions downstream of BLNK by up-regulating
IRF4, which in turn activates L chain gene rearrangement.
Regulates epithelial tight junctions (TJs) by phosphorylating
occludin (OCLN) on threonine residues, which is necessary for the
assembly and maintenance of TJs. In association with PLD2 and via
TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced
RGS2 down-regulation and foam cell formation. Upon PMA
stimulation, mediates glioblastoma cell proliferation by
activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-
dependent phosphorylation of ELK1. Involved in the protection of
glioblastoma cells from irradiation-induced apoptosis by
preventing caspase-9 activation. In camptothecin-treated MCF-7
cells, regulates NF-kappa-B upstream signaling by activating
IKBKB, and confers protection against DNA damage-induced
apoptosis. Promotes oncogenic functions of ATF2 in the nucleus
while blocking its apoptotic function at mitochondria.
Phosphorylates ATF2 which promotes its nuclear retention and
transcriptional activity and negatively regulates its
mitochondrial localization. {ECO:0000269|PubMed:11106751,
ECO:0000269|PubMed:18780722, ECO:0000269|PubMed:21346190}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
calcium-insensitive, but activated by diacylglycerol (DAG) and
phosphatidylserine. Three specific sites; Thr-513 (activation loop
of the kinase domain), Thr-656 (turn motif) and Ser-675
(hydrophobic region), need to be phosphorylated for its full
activation.
-!- SUBUNIT: Interacts with DGKQ (By similarity). Interacts with FYN
and RALA. {ECO:0000250, ECO:0000269|PubMed:11106751,
ECO:0000269|PubMed:21346190}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11106751,
ECO:0000269|PubMed:21346190}. Note=Associates with cell membrane
during keratinocytes differentiation.
-!- TISSUE SPECIFICITY: Predominantly expressed in lung and skin.
-!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type
region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the
C2 domain is a non-calcium binding domain.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D90242; BAA14288.1; -; mRNA.
EMBL; AK164044; BAE37603.1; -; mRNA.
EMBL; BC031121; AAH31121.1; -; mRNA.
CCDS; CCDS25976.1; -.
PIR; A23690; A23690.
RefSeq; NP_001300906.1; NM_001313977.1.
RefSeq; NP_032882.2; NM_008856.4.
UniGene; Mm.341677; -.
ProteinModelPortal; P23298; -.
SMR; P23298; -.
BioGrid; 202199; 1.
IntAct; P23298; 2.
MINT; P23298; -.
STRING; 10090.ENSMUSP00000021527; -.
BindingDB; P23298; -.
ChEMBL; CHEMBL4992; -.
iPTMnet; P23298; -.
PhosphoSitePlus; P23298; -.
EPD; P23298; -.
MaxQB; P23298; -.
PaxDb; P23298; -.
PRIDE; P23298; -.
Ensembl; ENSMUST00000021527; ENSMUSP00000021527; ENSMUSG00000021108.
GeneID; 18755; -.
KEGG; mmu:18755; -.
UCSC; uc007nwn.1; mouse.
CTD; 5583; -.
MGI; MGI:97600; Prkch.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; P23298; -.
KO; K18051; -.
OMA; NHRQLEP; -.
OrthoDB; EOG091G0QRS; -.
TreeFam; TF351133; -.
BRENDA; 2.7.11.13; 3474.
Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
PRO; PR:P23298; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000021108; -.
CleanEx; MM_PRKCH; -.
ExpressionAtlas; P23298; baseline and differential.
Genevisible; P23298; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004699; F:calcium-independent protein kinase C activity; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0017160; F:Ral GTPase binding; IPI:UniProtKB.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0060252; P:positive regulation of glial cell proliferation; ISS:UniProtKB.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0070528; P:protein kinase C signaling; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISS:UniProtKB.
CDD; cd00029; C1; 2.
CDD; cd05590; STKc_nPKC_eta; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR034665; nPKC_eta.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR027431; PKC_eta.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR014376; Prot_kin_PKC_delta.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 2.
Pfam; PF00168; C2; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000551; PKC_delta; 1.
PIRSF; PIRSF501107; Protein_kin_C_eta; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00239; C2; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50004; C2; 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; 2.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Differentiation; Kinase;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Repeat; Serine/threonine-protein kinase; Transferase; Zinc;
Zinc-finger.
CHAIN 1 683 Protein kinase C eta type.
/FTId=PRO_0000055706.
DOMAIN 12 102 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 355 614 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 615 683 AGC-kinase C-terminal.
ZN_FING 171 222 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 245 295 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 361 369 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 479 479 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 384 384 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000250|UniProtKB:P24723}.
MOD_RES 32 32 Phosphoserine.
{ECO:0000250|UniProtKB:P24723}.
MOD_RES 317 317 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 513 513 Phosphothreonine; by PDPK1.
{ECO:0000250}.
MOD_RES 656 656 Phosphothreonine.
{ECO:0000250|UniProtKB:P24723,
ECO:0000305}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000250|UniProtKB:Q64617,
ECO:0000305}.
CONFLICT 582 582 T -> R (in Ref. 1; BAA14288).
{ECO:0000305}.
SEQUENCE 683 AA; 77919 MW; 50454A6AE1900AD3 CRC64;
MSSGTMKFNG YLRVRIGEAV GLQPTRWSLR HSLFKKGHQL LDPYLTVSVD QVRVGQTSTK
QKTNKPTYNE EFCANVTDGG HLELAVFHET PLGYDHFVAN CTLQFQELLR TAGTSDTFEG
WVDLEPEGKV FVVITLTGSF TEATLQRDRI FKHFTRKRQR AMRRRVHQVN GHKFMATYLR
QPTYCSHCRE FIWGVFGKQG YQCQVCTCVV HKRCHHLIVT ACTCQNNINK VDAKIAEQRF
GINIPHKFNV HNYKVPTFCD HCGSLLWGIM RQGLQCKICK MNVHIRCQAN VAPNCGVNAV
ELAKTLAGMG LQPGNISPTS KLISRSTLRR QGKEGSKEGN GIGVNSSSRF GIDNFEFIRV
LGKGSFGKVM LARIKETGEL YAVKVLKKDV ILQDDDVECT MTEKRILSLA RNHPFLTQLF
CCFQTPDRLF FVMEFVNGGD LMFHIQKSRR FDEARARFYA AEIISALMFL HEKGIIYRDL
KLDNVLLDHE GHCKLADFGM CKEGICNGVT TATFCGTPDY IAPEILQEML YGPAVDWWAM
GVLLYEMLCG HAPFEAENED DLFEAILNDE VVYPTWLHED ATGILKSFMT KNPTMRLGSL
TQGGEHEILR HPFFKEIDWA QLNHRQLEPP FRPRIKSRED VSNFDPDFIK EEPVLTPIDE
GHLPMINQDE FRNFSYVSPE LQL


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