[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3755548 [NCBI, ExPASy, EBI, Israel, Japan] Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., Waterfield M.D., Francke U., Ullrich A.; "Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways."; Science 233:859-866(1986).
[2]	REVIEW. DOI=10.1038/334661a0; PubMed=3045562 [NCBI, ExPASy, EBI, Israel, Japan] Nishizuka Y.; "The molecular heterogeneity of protein kinase C and its implications for cellular regulation."; Nature 334:661-665(1988).

Comments

FUNCTION: This is a calcium-activated, 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.
COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to the C2 domain (By similarity).
SUBUNIT: Interacts with CDCP1 (By similarity).
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

M13976; AAA30704.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C24664; KIBOGC.

UniGene

Bt.12762

3D structure databases

HSSP

P05697; 1TBN. [HSSP ENTRY / PDB]

SMR

P05128; 78-143, 333-668.

ModBase

P05128.

Ontologies

GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
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 EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000008; C2_Ca-dep.
IPR002219; DAG_PE_bd.
IPR015745; PKC.
IPR000961; Pkinase_C.
IPR014375; Prot_kin_PKC_alpha.
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

PIRSF000550; PKC_alpha; 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

ENSBTAG00000013550; Bos taurus. [Contig view]

Phylogenomic databases

HOVERGEN

P05128; -.

Other

UniRef

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

Keywords

ATP-binding; Calcium; 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`	`<1 682`	`>682`	`Protein kinase C gamma type.`	`PRO_0000055688`
`DOMAIN`	`155 245`	`91`	`C2.`
`DOMAIN`	`336 599`	`264`	`Protein kinase.`
`DOMAIN`	`600 670`	`71`	`AGC-kinase C-terminal.`
`ZN_FING`	`20 70`	`51`	`Phorbol-ester/DAG-type 1.`
`ZN_FING`	`85 135`	`51`	`Phorbol-ester/DAG-type 2.`
`NP_BIND`	`342 350`	`9`	`ATP (By similarity).`
`ACT_SITE`	`465 465`		`Proton acceptor (By similarity).`
`METAL`	`171 171`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`172 172`		`Calcium 1 (By similarity).`
`METAL`	`172 172`		`Calcium 2 (By similarity).`
`METAL`	`178 178`		`Calcium 2 (By similarity).`
`METAL`	`231 231`		`Calcium 1 (By similarity).`
`METAL`	`231 231`		`Calcium 2 (By similarity).`
`METAL`	`232 232`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`233 233`		`Calcium 1 (By similarity).`
`METAL`	`233 233`		`Calcium 2 (By similarity).`
`METAL`	`233 233`		`Calcium 3 (By similarity).`
`METAL`	`236 236`		`Calcium 3 (By similarity).`
`METAL`	`237 237`		`Calcium 3; via carbonyl oxygen (By similarity).`
`METAL`	`239 239`		`Calcium 1 (By similarity).`
`METAL`	`239 239`		`Calcium 3 (By similarity).`
`BINDING`	`365 365`		`ATP (By similarity).`
`MOD_RES`	`180 180`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`297 297`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`307 307`		`Phosphoserine (By similarity).`
`MOD_RES`	`315 315`		`Phosphoserine (By similarity).`
`MOD_RES`	`499 499`		`Phosphothreonine (By similarity).`
`MOD_RES`	`503 503`		`Phosphothreonine (By similarity).`
`MOD_RES`	`633 633`		`Phosphothreonine; by autocatalysis (Potential).`
`MOD_RES`	`640 640`		`Phosphothreonine; by autocatalysis (Potential).`
`MOD_RES`	`672 672`		`Phosphoserine (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 682 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 77156 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 20392D11188C731C [This is a checksum on the sequence]

        10         20         30         40         50         60 
RPLFCRKGAL RQKVVHEVKS HKFTARFFKQ PTFCSHCTDF IWGIGKQGLQ CQVCSFVVHR 

        70         80         90        100        110        120 
RCHEFVTFEC PGAGKGPQTD DPRNKHKFRL HSYSSPTFCD HCGSLLYGLV HQGMKCSCCE 

       130        140        150        160        170        180 
MNVHRRCVRS VPSLCGVDHT ERRGRLQLEI RAPTSDEIHV TVGEARNLIP MDPNGLSDPY 

       190        200        210        220        230        240 
VKLKLIPDPR NLTKQKTRTV KATLNPVWNE TFVFNLKPGD VERRLSVEVW DWDRTSRNDF 

       250        260        270        280        290        300 
MGAMSFGVSE LLKAPVDGWY KLLNQEEGEY YNVPVADADN CNLLQKFEAC NYPLELYERV 

       310        320        330        340        350        360 
RTGPSSSPIP SPSPSPTDSK RCFFGASPGR LHISDFSFLM VLGKGSFGKV MLAERRGSDE 

       370        380        390        400        410        420 
LYAIKILKKD VIVQDDDVDC TLVEKRVLAL GGRGPGGRPH FLTQLHSTFQ TPDRLYFVME 

       430        440        450        460        470        480 
YVTGGDLMYH IQQLGKFKEP HAAFYAAEIA IGLFFLHNQG IIYRDLKLDN VMLDAEGHIK 

       490        500        510        520        530        540 
ITDFGMCKEN VFPGSTTRTF CGTPDYIAPE IIAYQPYGKS VDWWSFGVLL YEMLAGQPPF 

       550        560        570        580        590        600 
DGEDEEELFQ AIMEQTVTYP KSLSREAVAI CKGFLTKHPA KRLGSGPDGE PTIRAHGFFR 

       610        620        630        640        650        660 
WIDWDRLERL EIAPPFRPRP CGRSGENFDK FFTRAAPALT PPDRLVLASI DQAEFQGFTY 

       670        680 
VNPDFVHPDA RSPISPTPVP VM

P05128 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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