PRKD3

PRKD3
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2D9Z
Identifiers
Aliases	PRKD3, EPK2, PKC-NU, PKD3, PRKCN, nPKC-NU, protein kinase D3
External IDs	OMIM: 607077; MGI: 1922542; HomoloGene: 2055; GeneCards: PRKD3; OMA:PRKD3 - orthologs
Gene location (Human)
Chr.	Chromosome 2 (human)
End	37,324,833 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	79,328,245 bp
RNA expression pattern
	Top expressed in
	Achilles tendon; ; buccal mucosa cell; ; sperm; ; corpus epididymis; ; tail of epididymis; ; skin of hip; ; parietal pleura; ; tibia; ; cartilage tissue; ; superficial temporal artery;
	Top expressed in
	Rostral migratory stream; ; internal carotid artery; ; saccule; ; external carotid artery; ; vas deferens; ; condyle; ; efferent ductule; ; fossa; ; otic placode; ; renal corpuscle;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity; nucleotide binding; protein kinase activity; protein kinase C activity; protein binding; ATP binding; metal ion binding; kinase activity; protein serine/threonine kinase activity;
Cellular component	membrane; nucleoplasm; cytosol; cytoplasm;
Biological process	protein phosphorylation; protein kinase C-activating G protein-coupled receptor signaling pathway; intracellular signal transduction; phosphorylation; sphingolipid biosynthetic process; protein kinase D signaling;
	Sources:Amigo / QuickGO
Orthologs
	23683
	75292
	ENSG00000115825
	ENSMUSG00000024070
	O94806
	Q8K1Y2
	NM_005813
	NM_001171004; NM_001171005; NM_029239
	NP_005804
	NP_001164475; NP_001164476; NP_083515
	Wikidata
View/Edit Human	View/Edit Mouse

Serine/threonine-protein kinase D3 (PKD3) or PKC-nu is an enzyme that in humans is encoded by the PRKD3 gene.^[5]^[6]

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role. The protein encoded by this gene is one of the PKC family members. This kinase can be activated rapidly by the agonists of G protein-coupled receptors. It resides in both cytoplasm and nucleus, and its nuclear accumulation is found to be dramatically enhanced in response to its activation. This kinase can also be activated after B-cell antigen receptor (BCR) engagement, which requires intact phospholipase C gamma and the involvement of other PKC family members.^[6]

References

Ali A, Hoeflich KP, Woodgett JR (2002). "Glycogen synthase kinase-3: properties, functions, and regulation". Chem. Rev. 101 (8): 2527–40. doi:10.1021/cr000110o. PMID 11749387.
Jakobovits A, Rosenthal A, Capon DJ (1990). "Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C". EMBO J. 9 (4): 1165–70. doi:10.1002/j.1460-2075.1990.tb08223.x. PMC 551792. PMID 2182321.
Schultz SJ, Nigg EA (1994). "Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans". Cell Growth Differ. 4 (10): 821–30. PMID 8274451.
Conant K, Ma M, Nath A, Major EO (1996). "Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes". J. Virol. 70 (3): 1384–9. doi:10.1128/JVI.70.3.1384-1389.1996. PMC 189957. PMID 8627654.
Holmes AM (1996). "In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46". Arch. Biochem. Biophys. 335 (1): 8–12. doi:10.1006/abbi.1996.0476. PMID 8914829.
Borgatti P, Zauli G, Cantley LC, Capitani S (1998). "Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells". Biochem. Biophys. Res. Commun. 242 (2): 332–7. doi:10.1006/bbrc.1997.7877. PMID 9446795.
Zidovetzki R, Wang JL, Chen P, et al. (1998). "Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways". AIDS Res. Hum. Retroviruses. 14 (10): 825–33. doi:10.1089/aid.1998.14.825. PMID 9671211.
Mayne M, Holden CP, Nath A, Geiger JD (2000). "Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages". J. Immunol. 164 (12): 6538–42. doi:10.4049/jimmunol.164.12.6538. PMID 10843712.
Fang X, Yu SX, Lu Y, et al. (2000). "Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A". Proc. Natl. Acad. Sci. U.S.A. 97 (22): 11960–5. Bibcode:2000PNAS...9711960F. doi:10.1073/pnas.220413597. PMC 17277. PMID 11035810.
Badou A, Bennasser Y, Moreau M, et al. (2000). "Tat Protein of Human Immunodeficiency Virus Type 1 Induces Interleukin-10 in Human Peripheral Blood Monocytes: Implication of Protein Kinase C-Dependent Pathway". J. Virol. 74 (22): 10551–62. doi:10.1128/JVI.74.22.10551-10562.2000. PMC 110929. PMID 11044099.
Park IW, Wang JF, Groopman JE (2001). "HIV-1 Tat promotes monocyte chemoattractant protein-1 secretion followed by transmigration of monocytes". Blood. 97 (2): 352–8. doi:10.1182/blood.V97.2.352. PMID 11154208.
Bennasser Y, Yamina B, Contreras X, et al. (2002). "[HIV-1 Tat protein induces IL-10 production by human monocytes: implications of the PKC and calcium pathway]". J. Soc. Biol. 195 (3): 319–26. PMID 11833470.
Fang X, Yu S, Tanyi JL, et al. (2002). "Convergence of Multiple Signaling Cascades at Glycogen Synthase Kinase 3: Edg Receptor-Mediated Phosphorylation and Inactivation by Lysophosphatidic Acid through a Protein Kinase C-Dependent Intracellular Pathway". Mol. Cell. Biol. 22 (7): 2099–110. doi:10.1128/MCB.22.7.2099-2110.2002. PMC 133668. PMID 11884598.
Bennasser Y, Bahraoui E (2002). "HIV-1 Tat protein induces interleukin-10 in human peripheral blood monocytes: involvement of protein kinase C-betaII and -delta". FASEB J. 16 (6): 546–54. doi:10.1096/fj.01-0775com. PMID 11919157. S2CID 84545613.
Dai F, Yu L, He H, et al. (2002). "Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction". Biochem. Biophys. Res. Commun. 293 (4): 1191–6. doi:10.1016/S0006-291X(02)00349-2. PMID 12054501.
Efimova T, Deucher A, Kuroki T, et al. (2002). "Novel protein kinase C isoforms regulate human keratinocyte differentiation by activating a p38 delta mitogen-activated protein kinase cascade that targets CCAAT/enhancer-binding protein alpha". J. Biol. Chem. 277 (35): 31753–60. doi:10.1074/jbc.M205098200. PMID 12080077.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Bennasser Y, Badou A, Tkaczuk J, Bahraoui E (2003). "Signaling pathways triggered by HIV-1 Tat in human monocytes to induce TNF-alpha". Virology. 303 (1): 174–80. doi:10.1006/viro.2002.1676. PMID 12482669.

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

PRKD3

References

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