NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Epidermis;
PubMed=2266135 [NCBI, ExPASy, EBI, Israel, Japan]
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).

Comments

FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme.
FUNCTION: 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-513 (activation loop of the kinase domain), Thr-656 (turn motif) and Ser-675 (hydrophobic region), need to be phosphorylated for its full activation.
TISSUE SPECIFICITY: Predominantly expressed in lunk 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.
SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
SIMILARITY: Contains 1 C2 domain.
SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D90242; BAA14288.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A23690; A23690.

UniGene

Mm.341677

3D structure databases

HSSP

P28867; 1PTQ. [HSSP ENTRY / PDB]

P23298; 2-137.

PTM databases

P23298; -.

Organism-specific databases

MGI

MGI:97600; Prkch.

Gene expression databases

ArrayExpress

P23298; -.

CleanEx

MM_PRKCH; -.

GermOnline

ENSMUSG00000021108; Mus musculus.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0019992;	Molecular function: diacylglycerol binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004697;	Molecular function: protein kinase C activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007242;	Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.

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 of domain structure.

PANTHER

PTHR22985:SF86; PKC; 1.

Pfam

PF00130; C1_1; 2.
PF00168; C2; 1.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000551; PKC_delta; 1.

PRINTS

PR00360; C2DOMAIN.
PR00008; DAGPEDOMAIN.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00109; C1; 2.
SM00239; C2; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS51285; AGC_KINASE_CTER; 1.
PS50004; C2; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS00479; ZF_DAG_PE_1; 2.
PS50081; ZF_DAG_PE_2; 2.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSMUSG00000021108; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

P23298; -.

HOVERGEN

P23298; -.

Other

LinkHub

P23298; -.

SOURCE

Prkch; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Kinase; Metal-binding; Nucleotide-binding; Phorbol-ester binding; Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 683`	`683`	`Protein kinase C eta type.`	`PRO_0000055706`
`DOMAIN`	`12 102`	`91`	`C2.`
`DOMAIN`	`355 614`	`260`	`Protein kinase.`
`DOMAIN`	`615 683`	`69`	`AGC-kinase C-terminal.`
`ZN_FING`	`171 222`	`52`	`Phorbol-ester/DAG-type 1.`
`ZN_FING`	`245 295`	`51`	`Phorbol-ester/DAG-type 2.`
`NP_BIND`	`361 369`	`9`	`ATP (By similarity).`
`ACT_SITE`	`479 479`		`Proton acceptor (By similarity).`
`BINDING`	`384 384`		`ATP (By similarity).`
`MOD_RES`	`513 513`		`Phosphothreonine (Potential).`
`MOD_RES`	`656 656`		`Phosphothreonine (Probable).`
`MOD_RES`	`675 675`		`Phosphoserine (Probable).`

Sequence information

Length: 683 AA [This is the length of the unprocessed precursor]

Molecular weight: 77974 Da [This is the MW of the unprocessed precursor]

CRC64: C7DB338A9F95F576 [This is a checksum on the sequence]

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

        70         80         90        100        110        120 
QKTNKPTYNE EFCANVTDGG 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 ARGILKSFMT KNPTMRLGSL 

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

       670        680 
GHLPMINQDE FRNFSYVSPE LQL

P23298 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools