NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-I AND BETA-II).
TISSUE=Brain;
DOI=10.1038/325161a0; PubMed=3808073 [NCBI, ExPASy, EBI, Israel, Japan]
Ohno S., Kawasaki H., Imajoh S., Suzuki K., Inagaki M., Yokokura H., Sakoh T., Hidaka H.;
"Tissue-specific expression of three distinct types of rabbit protein kinase C.";
Nature 325:161-166(1987).

Comments

FUNCTION: This is a calcium-activated, 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. May be considered as a novel component of the NF-kappa-B signaling axis responsible for the survival and activation of B-cells after BCR cross-linking (By similarity).
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 PDK1 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; Peripheral membrane protein (By similarity).
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name Beta-I

Isoform ID P05772-1

This is the isoform sequence displayed in this entry.

Name Beta-II

Isoform ID P05772-2

Features which should be applied to build the isoform sequence: VSP_004740.
PTM: Phosphorylation on 'Thr-499' of isoform beta-I, within the activation loop, renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Similarly, isoform beta-II is autophosphorylated on 'Thr-640' and 'Ser-659', subsequent to phosphorylation on Thr-500. Autophosphorylated on other sites i.e. in the N-terminal and hinge regions have no effect on PKC activity (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

X04795; CAA28482.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04793; CAA28480.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A26037; KIRBC2.
B26037; KIRBC1.

RefSeq

NP_001095193.1; -.
NP_001095195.1; -.

UniGene

Ocu.3267

3D structure databases

HSSP

P04410; 1A25. [HSSP ENTRY / PDB]

SMR

P05772; 94-158, 95-159, 156-287, 157-288, 339-668.

ModBase

P05772.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
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.

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

GeneID

100037719; -.

Phylogenomic databases

HOVERGEN

P05772; -.

Other

UniRef

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

Keywords

Acetylation; Alternative splicing; ATP-binding; Calcium; Cytoplasm; Kinase; Membrane; 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`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 671`	`670`	`Protein kinase C beta type.`	`PRO_0000055686`
`DOMAIN`	`173 260`	`88`	`C2.`
`DOMAIN`	`342 600`	`259`	`Protein kinase.`
`DOMAIN`	`601 671`	`71`	`AGC-kinase C-terminal.`
`ZN_FING`	`36 86`	`51`	`Phorbol-ester/DAG-type 1.`
`ZN_FING`	`101 151`	`51`	`Phorbol-ester/DAG-type 2.`
`NP_BIND`	`348 356`	`9`	`ATP (By similarity).`
`ACT_SITE`	`466 466`		`Proton acceptor (By similarity).`
`METAL`	`186 186`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`187 187`		`Calcium 1 (By similarity).`
`METAL`	`187 187`		`Calcium 2 (By similarity).`
`METAL`	`193 193`		`Calcium 2 (By similarity).`
`METAL`	`246 246`		`Calcium 1 (By similarity).`
`METAL`	`246 246`		`Calcium 2 (By similarity).`
`METAL`	`247 247`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`248 248`		`Calcium 1 (By similarity).`
`METAL`	`248 248`		`Calcium 2 (By similarity).`
`METAL`	`248 248`		`Calcium 3 (By similarity).`
`METAL`	`251 251`		`Calcium 3 (By similarity).`
`METAL`	`252 252`		`Calcium 3; via carbonyl oxygen (By similarity).`
`METAL`	`254 254`		`Calcium 1 (By similarity).`
`METAL`	`254 254`		`Calcium 3 (By similarity).`
`BINDING`	`371 371`		`ATP (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`MOD_RES`	`16 16`		`Phosphoserine; by autocatalysis (Potential).`
`MOD_RES`	`17 17`		`Phosphothreonine; by autocatalysis (Potential).`
`MOD_RES`	`195 195`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`314 314`		`Phosphothreonine; by autocatalysis (Potential).`
`MOD_RES`	`324 324`		`Phosphothreonine; by autocatalysis (Potential).`
`MOD_RES`	`500 500`		`Phosphothreonine (By similarity).`
`MOD_RES`	`504 504`		`Phosphothreonine (By similarity).`
`MOD_RES`	`635 635`		`Phosphothreonine; by autocatalysis (Potential).`
`MOD_RES`	`642 642`		`Phosphothreonine (Potential).`
`MOD_RES`	`661 661`		`Phosphoserine; by autocatalysis (By similarity).`
`VAR_SEQ`	`622 671`		`RDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFS` `YTNPEFVINV -> CGRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEFEGFSF` `VNSEFLKPEVKS (in isoform Beta-II).`	`VSP_004740`

Sequence information

Length: 671 AA [This is the length of the unprocessed precursor]

Molecular weight: 76828 Da [This is the MW of the unprocessed precursor]

CRC64: DFBF22EEB3D41861 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADPAAGQPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF 

        70         80         90        100        110        120 
GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS 

       130        140        150        160        170        180 
LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIDR EVLIVVVRDA 

       190        200        210        220        230        240 
KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL 

       250        260        270        280        290        300 
SVEIWDWDLT SRNDFMGSLS FGISELQKAG VDGWFKLLSQ EEGEYFNVPV PPEGSEGNEE 

       310        320        330        340        350        360 
LRQKFERAKI GQGTKTPEEK TTNTISKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE 

       370        380        390        400        410        420 
RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM 

       430        440        450        460        470        480 
EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI 

       490        500        510        520        530        540 
KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP 

       550        560        570        580        590        600 
FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKDHAFF 

       610        620        630        640        650        660 
RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM NLDQNEFAGF 

       670 
SYTNPEFVIN V

P05772 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