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Q64617 (KPCL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein kinase C eta type

EC=2.7.11.13
Alternative name(s):
PKC-L
nPKC-eta
Gene names
Name:Prkch
Synonyms:Pkch
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length683 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 By similarity.

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 structure

Interacts with DGKQ, FYN and RALA By similarity.

Subcellular location

Cytoplasm By similarity.

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.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 C2 domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 683683Protein kinase C eta type
PRO_0000055707

Regions

Domain12 – 10291C2
Domain355 – 614260Protein kinase
Domain615 – 68369AGC-kinase C-terminal
Zinc finger171 – 22252Phorbol-ester/DAG-type 1
Zinc finger245 – 29551Phorbol-ester/DAG-type 2
Nucleotide binding361 – 3699ATP By similarity

Sites

Active site4791Proton acceptor By similarity
Binding site3841ATP By similarity

Amino acid modifications

Modified residue571Phosphothreonine By similarity
Modified residue3171Phosphoserine By similarity
Modified residue3201Phosphoserine By similarity
Modified residue5131Phosphothreonine; by PDPK1 Probable
Modified residue6561Phosphothreonine Probable
Modified residue6751Phosphoserine Probable

Sequences

Sequence LengthMass (Da)Tools
Q64617 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 2F5B7078D1206510

FASTA68377,947
        10         20         30         40         50         60 
MSSGTMKFNG YLRVRIGEAV GLQPTRWSLR HSLFKKGHQL LDPYLTVSVD QVRVGQTSTK 

        70         80         90        100        110        120 
QKTNKPTYNE EFCTNVSDGG HLELAVFHET PLGYDHFVAN CTLQFQELLR TAGTSDTFEG 

       130        140        150        160        170        180 
WVDLEPEGKV FVVITLTGSF TEATLQRDRI FKHFTRKRQR AMRRRVHQVN GHKFMATYLR 

       190        200        210        220        230        240 
QPTYCSHCRE FIWGVFGKQG YQCQVCTCVV HKRCHHLIVT ACTCQNNINK VDAKIAEQRF 

       250        260        270        280        290        300 
GINIPHKFNV HNYKVPTFCD HCGSLLWGIM RQGLQCKICK MNVHIRCQAN VAPNCGVNAV 

       310        320        330        340        350        360 
ELAKTLAGMG LQPGNISPTS KLISRSTLRR QGKEGSKEGN GIGVNSSSRF GIDNFEFIRV 

       370        380        390        400        410        420 
LGKGSFGKVM LARIKETGEL YAVKVLKKDV ILQDDDVECT MTEKRILSLA RNHPFLTQLF 

       430        440        450        460        470        480 
CCFQTPDRLF FVMEFVNGGD LMFHIQKSRR FDEARARFYA AEIISALMFL HEKGIIYRDL 

       490        500        510        520        530        540 
KLDNVLLDHE GHCKLADFGM CKEGICNGVT TATFCGTPDY IAPEILQEML YGPAVDWWAM 

       550        560        570        580        590        600 
GVLLYEMLCG HAPFEAENED DLFEAILNDE VVYPTWLHED ATGILKSFMT KNPTMRLGSL 

       610        620        630        640        650        660 
TQGGEHEILR HPFFKEIDWV QLNHRQLEPP FRPRIKSRED VSNFDPDFIK EEPVLTPIDE 

       670        680 
GHLPMINQDE FRNFSYVSPE LQP 

« Hide

References

« Hide 'large scale' references
[1]"Biochemical properties of rat protein kinase C-eta expressed in COS cells."
Dekker L.V., Parker P.J., McIntyre P.
FEBS Lett. 312:195-199(1992) [PubMed: 1426252] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Lung.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68400 mRNA. Translation: CAA48466.1.
BC081782 mRNA. Translation: AAH81782.1.
IPIIPI00214397.
PIRS29478. I60246.
RefSeqNP_112347.1. NM_031085.2.
UniGeneRn.10398.

3D structure databases

ProteinModelPortalQ64617.
SMRQ64617. Positions 352-683.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ64617.

PTM databases

PhosphoSiteQ64617.

Proteomic databases

PRIDEQ64617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000006729; ENSRNOP00000006729; ENSRNOG00000004873.
GeneID81749.
KEGGrno:81749.
UCSCNM_031085. rat.

Organism-specific databases

CTD5583.
RGD621888. Prkch.

Phylogenomic databases

eggNOGroNOG06998.
GeneTreeENSGT00590000082973.
HOVERGENHBG108317.
InParanoidQ64617.
OMAREFIWGV.
OrthoDBEOG4P2Q1P.
PhylomeDBQ64617.

Enzyme and pathway databases

BRENDA2.7.11.13. 5301.

Gene expression databases

ArrayExpressQ64617.
GenevestigatorQ64617.
GermOnlineENSRNOG00000004873. Rattus norvegicus.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]
KOK06068.
PfamPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000551. PKC_delta. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
SSF56112. Kinase_like. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio615498.

Entry information

Entry nameKPCL_RAT
AccessionPrimary (citable) accession number: Q64617
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families