Descriptions

PRKCA encodes for Protein kinase C (PKC) alpha type belonging to the PCKs family and is involved in various cellular processes, including cell growth, immune response, muscle contraction, and synaptic plasticity. A well-known autoinhibitory region of the PKC family is a pseudosubstrate sequence at residues 1-30 that directly interacts with and blocks the catalytic activity of the kinase domain. Subsequences of the pseudosubstrate region are the C1 domains (C1A and C1B that bind diacylglycerol (DAG)), and the C2 domain (which binds to anionic phospholipids in a Ca2+-dependent manner). The C1A (residues 31-100) domain coordinates a network of domain-domain intramolecular interactions, including direct C1A-C2 contacts. The pseudosubstrate and C1A domains function as a single functional unit and are required to maintain autoinhibition. Additionally, the absence of the C1A domain significantly increases basal activity.

Autoinhibitory domains (AIDs)

Target domain

339-679 (Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha)

Relief mechanism

Ligand binding

Assay

Target domain

339-679 (Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha)

Relief mechanism

Ligand binding

Assay

Target domain

352-594 (Protein kinase domain)

Relief mechanism

Ligand binding

Assay

Target domain

352-594 (Protein kinase domain)

Relief mechanism

Ligand binding

Assay

Accessory elements

491-514 (Activation loop from InterPro)

Target domain

350-608 (Protein kinase domain)

Relief mechanism

Assay

491-514 (Activation loop from InterPro)

Target domain

350-608 (Protein kinase domain)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for P05130

Entry ID Method Resolution Chain Position Source
AF-P05130-F1 Predicted AlphaFoldDB

1 variants for P05130

Variant ID(s) Position Change Description Diseaes Association Provenance
437 M>I No

No associated diseases with P05130

12 regional properties for P05130

Type Name Position InterPro Accession
domain C2 domain 176 - 295 IPR000008
domain Protein kinase domain 350 - 608 IPR000719
domain AGC-kinase, C-terminal 609 - 679 IPR000961
domain Protein kinase C-like, phorbol ester/diacylglycerol-binding domain 45 - 106 IPR002219-1
domain Protein kinase C-like, phorbol ester/diacylglycerol-binding domain 119 - 172 IPR002219-2
active_site Serine/threonine-protein kinase, active site 470 - 482 IPR008271
binding_site Protein kinase, ATP binding site 356 - 379 IPR017441
domain Protein kinase, C-terminal 629 - 670 IPR017892
domain Diacylglycerol/phorbol-ester binding 43 - 57 IPR020454-1
domain Diacylglycerol/phorbol-ester binding 59 - 68 IPR020454-2
domain Diacylglycerol/phorbol-ester binding 81 - 92 IPR020454-3
domain Diacylglycerol/phorbol-ester binding 158 - 170 IPR020454-4

Functions

Description
EC Number 2.7.11.13 Protein-serine/threonine kinases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
diacylglycerol-dependent serine/threonine kinase activity Catalysis of the reaction
protein serine kinase activity Catalysis of the reactions
protein serine/threonine kinase activity Catalysis of the reactions
zinc ion binding Binding to a zinc ion (Zn).

4 GO annotations of biological process

Name Definition
intracellular signal transduction The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
positive regulation of clathrin-dependent endocytosis Any process that activates or increases the frequency, rate or extent of clathrin-mediated endocytosis.
protein phosphorylation The process of introducing a phosphate group on to a protein.
regulation of hemocyte proliferation Any process that modulates the frequency, rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this is found in Drosophila melanogaster.

31 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P24583 PKC1 Protein kinase C-like 1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P04409 PRKCA Protein kinase C alpha type Bos taurus (Bovine) EV SS
P05128 PRKCG Protein kinase C gamma type Bos taurus (Bovine) SS
P05126 PRKCB Protein kinase C beta type Bos taurus (Bovine) SS
Q9W0V1 Pdk1 3-phosphoinositide-dependent protein kinase 1 Drosophila melanogaster (Fruit fly) SS
A1Z9X0 aPKC Atypical protein kinase C Drosophila melanogaster (Fruit fly) SS
A1Z7T0 Pkn Serine/threonine-protein kinase N Drosophila melanogaster (Fruit fly) SS
P83099 Pkcdelta Putative protein kinase C delta type homolog Drosophila melanogaster (Fruit fly) PR
Q8INB9 Akt RAC serine/threonine-protein kinase Drosophila melanogaster (Fruit fly) SS
Q9NBK5 trc Serine/threonine-protein kinase tricornered Drosophila melanogaster (Fruit fly) SS
P13677 inaC Protein kinase C, eye isozyme Drosophila melanogaster (Fruit fly) SS
P05129 PRKCG Protein kinase C gamma type Homo sapiens (Human) SS
P05771 PRKCB Protein kinase C beta type Homo sapiens (Human) SS
Q02156 PRKCE Protein kinase C epsilon type Homo sapiens (Human) SS
P24723 PRKCH Protein kinase C eta type Homo sapiens (Human) SS
P17252 PRKCA Protein kinase C alpha type Homo sapiens (Human) EV
P20444 Prkca Protein kinase C alpha type Mus musculus (Mouse) SS
P68404 Prkcb Protein kinase C beta type Mus musculus (Mouse) SS
P16054 Prkce Protein kinase C epsilon type Mus musculus (Mouse) PR
P23298 Prkch Protein kinase C eta type Mus musculus (Mouse) PR
P63318 Prkcg Protein kinase C gamma type Mus musculus (Mouse) SS
Q64617 Prkch Protein kinase C eta type Rattus norvegicus (Rat) PR
P63319 Prkcg Protein kinase C gamma type Rattus norvegicus (Rat) SS
P05696 Prkca Protein kinase C alpha type Rattus norvegicus (Rat) SS
P68403 Prkcb Protein kinase C beta type Rattus norvegicus (Rat) SS
P90980 pkc-2 Protein kinase C-like 2 Caenorhabditis elegans SS
Q9SUA3 D6PKL1 Serine/threonine-protein kinase D6PKL1 Arabidopsis thaliana (Mouse-ear cress) PR
O64682 PID Protein kinase PINOID Arabidopsis thaliana (Mouse-ear cress) PR
Q9LUL2 WAG2 Serine/threonine-protein kinase WAG2 Arabidopsis thaliana (Mouse-ear cress) PR
A8KBH6 prkcb Protein kinase C beta type Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) SS
Q7SY24 prkcbb Protein kinase C beta type Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MSEGSDNNGD PQQQGAEGEA VGENKMKSRL RKGALKKKNV FNVKDHCFIA RFFKQPTFCS
70 80 90 100 110 120
HCKDFICGYQ SGYAWMGFGK QGFQCQVCSY VVHKRCHEYV TFICPGKDKG IDSDSPKTQH
130 140 150 160 170 180
NFEPFTYAGP TFCDHCGSLL YGIYHQGLKC SACDMNVHAR CKENVPSLCG CDHTERRGRI
190 200 210 220 230 240
YLEINVKENL LTVQIKEGRN LIPMDPNGLS DPYVKVKLIP DDKDQSKKKT RTIKACLNPV
250 260 270 280 290 300
WNETLTYDLK PEDKDRRILI EVWDWDRTSR NDFMGALSFG ISEIIKNPTN GWFKLLTQDE
310 320 330 340 350 360
GEYYNVPCAD DEQDLLKLKQ KPSQKKPMVM RSDTNTHTSS KKDMIRATDF NFIKVLGKGS
370 380 390 400 410 420
FGKVLLAERK GSEELYAIKI LKKDVIIQDD DVECTMIEKR VLALGEKPPF LVQLHSCFQT
430 440 450 460 470 480
MDRLFFVMEY VNGGDLMFQI QQFGKFKEPV AVFYAAEIAA GLFFLHTKGI LYRDLKLDNV
490 500 510 520 530 540
LLDADGHVKI ADFGMCKENI VGDKTTKTFC GTPDYIAPEI ILYQPYGKSV DWWAYGVLLY
550 560 570 580 590 600
EMLVGQPPFD GEDEEELFAA ITDHNVSYPK SLSKEAKEAC KGFLTKQPNK RLGCGSSGEE
610 620 630 640 650 660
DVRLHPFFRR IDWEKIENRE VQPPFKPKIK HRKDVSNFDK QFTSEKTDLT PTDKVFMMNL
670
DQSEFVGFSY MNPEYVFSP