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XSB1247 : protein kinase C, alpha [Homo sapiens]

[ CaMP Format ]

This entry is computationally expanded from SB0055

* Basic Information

OrganismHomo sapiens (human)
Protein NamesProtein kinase C alpha type; PKC-alpha; PKC-A; 2.7.11.13; protein kinase C; alpha; aging-associated gene 6
Gene NamesPRKCA; PKCA, PRKACA; PKCA; PRKACA; protein kinase C, alpha
Gene Locus17q22-q23.2; chromosome 17
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_002728 NM_002737 5578 P17252 176960 9393 N/A hsa:5578

* Information From OMIM

Function: Ekinci and Shea (1999) stated that PKC-alpha is reversibly activated at the plasma membrane by transient generation of diacylglycerol (DAG), coupled with the release of Ca(2+) from intracellular stores, following receptor-mediated hydrolysis of inositol phospholipids. PKC-alpha is also irreversibly activated by calpain (see OMIM:114220)-mediated cleavage of its regulatory and catalytic subunits, resulting in a cofactor-independent, free PKC-alpha catalytic subunit termed PKM-alpha. Ekinci and Shea (1999) found that activation of PKC-alpha in human neuroblastoma cells by either the phorbol ester TPA or by ionophore-mediated calcium mobilization, which experimentally correspond to DAG-mediated and calpain-mediated activation, respectively, resulted in increased phosphorylation of the microtubule-associated protein tau (MAPT; OMIM:157140). Activation of PKC-alpha by calcium mobilization, but not TPA, generated PKM-alpha and resulted in calpain-dependent release of PKM-alpha from the plasma membrane. The TPA-mediated increase in tau phosphorylation was blocked by cotreatment with an MAP2K (see OMIM:176872) inhibitor, but ionophore-mediated tau phosphorylation was not.

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* Structure Information

1. Primary Information

Length: 672 aa

Average Mass: 76.764 kDa

Monoisotopic Mass: 76.714 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
C1_1 1. 378983.29.4e-22
C1_1 2. 10215492.51.5e-24
C2 1. 173260137.93.3e-38
--- cleavage 316 ---
--- cleavage 309 ---
--- cleavage 324 ---
Pkinase 1. 339597291.22.2e-84
Pkinase_C 1. 61766255.81.6e-13

3. Sequence Information

Fasta Sequence: XSB1247.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 2ELI (NMR; -; A=92-169)

* Cleavage Information

3 [sites]

Cleavage sites (±10aa)

[Site 1] KAKLGPAGNK316-VISPSEDRKQ

Lys316 Val

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Lys307Ala308Lys309Leu310Gly311Pro312Ala313Gly314Asn315Lys316
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Val317Ile318Ser319Pro320Ser321Glu322Asp323Arg324Lys325Gln326

Sequence conservation (by blast)

[Site 2] ELRQKFEKAK309-LGPAGNKVIS

Lys309 Leu

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Glu300Leu301Arg302Gln303Lys304Phe305Glu306Lys307Ala308Lys309
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Leu310Gly311Pro312Ala313Gly314Asn315Lys316Val317Ile318Ser319

Sequence conservation (by blast)

[Site 3] NKVISPSEDR324-KQPSNNLDRV

Arg324 Lys

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Asn315Lys316Val317Ile318Ser319Pro320Ser321Glu322Asp323Arg324
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Lys325Gln326Pro327Ser328Asn329Asn330Leu331Asp332Arg333Val334

Sequence conservation (by blast)

* References

[PubMed ID: 19235902] Haughian JM, Bradford AP, Protein kinase C alpha (PKCalpha) regulates growth and invasion of endometrial cancer cells. J Cell Physiol. 2009 Jul;220(1):112-8.

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