Reviewed, UniProtKB/Swiss-Prot P16054 (KPCE_MOUSE)

Names and origin

Protein names

Recommended name:
    Protein kinase C epsilon type
    EC=2.7.11.13
Alternative name(s):
    nPKC-epsilon

Gene names

Name:	Prkce
Synonyms:	Pkce, Pkcea

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	737 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Three specific sites; Thr-566 (activation loop of the kinase domain), Thr-710 (turn motif) and Ser-729 (hydrophobic region), need to be phosphorylated for its full activation.
Subunit structure	Forms a ternary complex with TRIM63 and GN2BL1 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.
Post-translational modification	Phosphorylation on Thr-566 triggers autophosphorylation on Ser-729 By similarity.
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.

Ontologies

Keywords
Domain	Phorbol-ester binding Repeat Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	chemosensory behavior Traceable author statement. Source: MGI regulation of peptidyl-tyrosine phosphorylation Inferred from mutant phenotype. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: MGI nucleus Inferred from direct assay. Source: MGI
Molecular function	calcium-independent protein kinase C activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 737	737	Protein kinase C epsilon type
Regions
	Domain	1 – 99	99	C2
	Domain	408 – 668	261	Protein kinase
	Domain	669 – 737	69	AGC-kinase C-terminal
	Zinc finger	169 – 220	52	Phorbol-ester/DAG-type 1
	Zinc finger	242 – 292	51	Phorbol-ester/DAG-type 2
	Nucleotide binding	414 – 422	9	ATP By similarity
Sites
	Active site	532	1	Proton acceptor By similarity
	Binding site	437	1	ATP By similarity
Amino acid modifications
	Modified residue	337	1	Phosphoserine
	Modified residue	349	1	Phosphothreonine
	Modified residue	566	1	Phosphothreonine; by PDPK1 By similarity
	Modified residue	703	1	Phosphothreonine; by autocatalysis Potential
	Modified residue	710	1	Phosphothreonine; by autocatalysis Potential
	Modified residue	729	1	Phosphoserine; by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P16054-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 7AEBB8CC10C99F57	FASTA	737	83,561
	10 20 30 40 50 60 MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR IGQTATKQKT 70 80 90 100 110 120 NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI QFEELLQNGS RHFEDWIDLE 130 140 150 160 170 180 PEGKVYVIID LSGSSGEAPK DNEERVFRER MRPRKRQGAV RRRVHQVNGH KFMATYLRQP 190 200 210 220 230 240 TYCSHCRDFI WGVIGKQGYQ CQVCTCVVHK RCHELIITKC AGLKKQETPD EVGSQRFSVN 250 260 270 280 290 300 MPHKFGIHNY KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA 310 320 330 340 350 360 KVLADLGVTP DKITNSGQRR KKLAAGAESP QPASGNSPSE DDRSKSAPTS PCDQELKELE 370 380 390 400 410 420 NNIRKALSFD NRGEEHRASS ATDGQLASPG ENGEVRPGQA KRLGLDEFNF IKVLGKGSFG 430 440 450 460 470 480 KVMLAELKGK DEVYAVKVLK KDVILQDDDV DCTMTEKRIL ALARKHPYLT QLYCCFQTKD 490 500 510 520 530 540 RLFFVMEYVN GGDLMFQIQR SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL 550 560 570 580 590 600 DAEGHCKLAD FGMCKEGIMN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM 610 620 630 640 650 660 MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL GCVAAQNGED 670 680 690 700 710 720 AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ DFTREEPILT LVDEAIIKQI 730 NQEEFKGFSY FGEDLMP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Unique substrate specificity and regulatory properties of PKC-epsilon: a rationale for diversity." Schaap D., Parker P.J., Bristol A., Kriz R., Knopf J. FEBS Lett. 243:351-357(1989) [PubMed: 2917656] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The catalytic domain of PKC-epsilon, in reciprocal PKC-delta and - epsilon chimeras, is responsible for conferring tumorgenicity to NIH3T3 cells, whereas both regulatory and catalytic domains of PKC-epsilon contribute to in vitro transformation." Wang Q.J., Acs P., Goodnight J., Blumberg P.M., Mischak H., Mushinski J.F. Oncogene 16:53-60(1998) [PubMed: 9467942] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	Wheeler D.L. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[4]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-349, MASS SPECTROMETRY. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF028009 mRNA. Translation: AAB84189.1. AF325507 mRNA. Translation: AAG53692.1.
PIR	KIMSCE. S02270.
RefSeq	NP_035234.1.
UniGene	Mm.24614
3D structure databases
HSSP	HSSP built from PDB template 1GMI based on UniProtKB P09216.
SMR	P16054. Positions 1-136.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16054.
PTM databases
PhosphoSite	P16054.
Genome annotation databases
Ensembl	ENSMUSG00000045038. Mus musculus. [Contig view]
GeneID	18754.
KEGG	mmu:18754.
Organism-specific databases
MGI	MGI:97599. Prkce.
Phylogenomic databases
HOGENOM	P16054.
HOVERGEN	P16054.
Gene expression databases
ArrayExpress	P16054.
CleanEx	MM_PRKCE.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR002219. DAG_PE_bd. IPR015745. PKC. IPR000961. Pkinase_C. IPR014376. Prot_kin_PKC_delta. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
PANTHER	PTHR22985:SF86. PKC. 1 hit.
Pfam	PF00130. C1_1. 2 hits. PF00168. C2. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
PIRSF	PIRSF000551. PKC_delta. 1 hit.
PRINTS	PR00360. C2DOMAIN. PR00008. DAGPEDOMAIN.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00109. C1. 2 hits. SM00239. C2. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS51285. 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]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

KPCE_MOUSE

Accession

Primary (citable) accession number: P16054

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	July 22, 2008
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)