PRKCI

Protein kinase C iota type is an enzyme that in humans is encoded by the PRKCI gene.

PRKCI
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1VD2, 1WMH, 1ZRZ, 3A8W, 3A8X, 3ZH8
Identifiers
Aliases	PRKCI, DXS1179E, PKCI, nPKC-iota, protein kinase C iota
External IDs	OMIM: 600539; MGI: 99260; HomoloGene: 37667; GeneCards: PRKCI; OMA:PRKCI - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3q26.2 Start 170,222,424 bp End 170,305,977 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3 A3|3 14.65 cM Start 31,049,896 bp End 31,107,108 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in buccal mucosa cell pylorus lower lobe of lung corpus epididymis cardia oral cavity renal medulla mucosa of pharynx nipple palpebral conjunctiva Top expressed in molar ciliary body urothelium hair follicle iris conjunctival fornix transitional epithelium of urinary bladder epithelium of lens primitive streak ureter More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity protein kinase activity nucleotide binding protein kinase C activity protein domain specific binding metal ion binding kinase activity protein serine/threonine kinase activity protein binding phospholipid binding ATP binding Cellular component cytosol endosome membrane bicellular tight junction microtubule cytoskeleton Golgi membrane plasma membrane apical part of cell Schmidt-Lanterman incisure apical plasma membrane cell leading edge intercellular bridge extracellular exosome nucleus cytoplasm nucleoplasm protein-containing complex Schaffer collateral - CA1 synapse glutamatergic synapse Biological process negative regulation of neuron apoptotic process positive regulation of glucose import establishment of apical/basal cell polarity intracellular signal transduction response to interleukin-1 phosphorylation Golgi vesicle budding actin filament organization protein targeting to membrane negative regulation of glial cell apoptotic process response to peptide hormone negative regulation of apoptotic process secretion protein phosphorylation positive regulation of endothelial cell apoptotic process positive regulation of NF-kappaB transcription factor activity cytoskeleton organization establishment or maintenance of epithelial cell apical/basal polarity bicellular tight junction assembly positive regulation of neuron projection development cellular response to insulin stimulus eye photoreceptor cell development membrane organization positive regulation of glial cell proliferation cell migration vesicle-mediated transport cell-cell junction organization peptidyl-serine phosphorylation positive regulation of protein localization to plasma membrane positive regulation of Notch signaling pathway regulation of postsynaptic membrane neurotransmitter receptor levels Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5584 18759 Ensembl ENSG00000163558 ENSMUSG00000037643 UniProt P41743 Q62074 RefSeq (mRNA) NM_002740 NM_008857 RefSeq (protein) NP_002731 NP_032883 Location (UCSC) Chr 3: 170.22 – 170.31 Mb Chr 3: 31.05 – 31.11 Mb PubMed search
Wikidata
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Function

This gene encodes a member of the protein kinase C (PKC) family of serine/threonine protein kinases. The PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. This protein kinase is calcium-independent and phospholipid-dependent. It is not activated by phorbol esters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by direct interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway. This kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X.

Interactions

PRKCI has been shown to interact with:

• Centaurin, alpha 1,
• FRS2,
• Glyceraldehyde 3-phosphate dehydrogenase,
• PARD3,
• Phosphoinositide-dependent kinase-1,
• SMG1 (gene),
• Sequestosome 1,
• KRAS.
• Vimentin

Further reading

• Suzuki A, Akimoto K, Ohno S (Jan 2003). "Protein kinase C lambda/iota (PKClambda/iota): a PKC isotype essential for the development of multicellular organisms". Journal of Biochemistry. 133 (1): 9–16. doi:10.1093/jb/mvg018. PMID 12761193.
• Fields AP, Regala RP (Jun 2007). "Protein kinase C iota: human oncogene, prognostic marker and therapeutic target". Pharmacological Research. 55 (6): 487–97. doi:10.1016/j.phrs.2007.04.015. PMC 2705893. PMID 17570678.
• Ruegg CL, Strand M (Oct 1991). "A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx". Cellular Immunology. 137 (1): 1–13. doi:10.1016/0008-8749(91)90051-C. PMID 1832084.
• Chowdhury IH, Koyanagi Y, Kobayashi S, Hamamoto Y, Yoshiyama H, Yoshida T, Yamamoto N (May 1990). "The phorbol ester TPA strongly inhibits HIV-1-induced syncytia formation but enhances virus production: possible involvement of protein kinase C pathway". Virology. 176 (1): 126–32. doi:10.1016/0042-6822(90)90237-L. PMID 1970444.
• Ruegg CL, Strand M (May 1990). "Inhibition of protein kinase C and anti-CD3-induced Ca2+ influx in Jurkat T cells by a synthetic peptide with sequence identity to HIV-1 gp41". Journal of Immunology. 144 (10): 3928–35. doi:10.4049/jimmunol.144.10.3928. PMID 2139676. S2CID 44688726.
• Jakobovits A, Rosenthal A, Capon DJ (Apr 1990). "Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C". The EMBO Journal. 9 (4): 1165–70. doi:10.1002/j.1460-2075.1990.tb08223.x. PMC 551792. PMID 2182321.
• Fields AP, Bednarik DP, Hess A, May WS (May 1988). "Human immunodeficiency virus induces phosphorylation of its cell surface receptor". Nature. 333 (6170): 278–80. Bibcode:1988Natur.333..278F. doi:10.1038/333278a0. PMID 3259291. S2CID 4254146.
• Chirmule N, Goonewardena H, Pahwa S, Pasieka R, Kalyanaraman VS, Pahwa S (Aug 1995). "HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells". The Journal of Biological Chemistry. 270 (33): 19364–9. doi:10.1074/jbc.270.33.19364. PMID 7642615.
• Ward NE, Gravitt KR, O'Brian CA (Jan 1995). "Inhibition of protein kinase C by a synthetic peptide corresponding to cytoplasmic domain residues 828-848 of the human immunodeficiency virus type 1 envelope glycoprotein". Cancer Letters. 88 (1): 37–40. doi:10.1016/0304-3835(94)03610-U. PMID 7850771.
• Gupta S, Aggarwal S, Kim C, Gollapudi S (Mar 1994). "Human immunodeficiency virus-1 recombinant gp120 induces changes in protein kinase C isozymes--a preliminary report". International Journal of Immunopharmacology. 16 (3): 197–204. doi:10.1016/0192-0561(94)90013-2. PMID 8206685.
• Selbie LA, Schmitz-Peiffer C, Sheng Y, Biden TJ (Nov 1993). "Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells". The Journal of Biological Chemistry. 268 (32): 24296–302. doi:10.1016/S0021-9258(20)80525-0. PMID 8226978.
• Diaz-Meco MT, Municio MM, Sanchez P, Lozano J, Moscat J (Jan 1996). "Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo". Molecular and Cellular Biology. 16 (1): 105–14. doi:10.1128/MCB.16.1.105. PMC 230983. PMID 8524286.
• Parada NA, Cruikshank WW, Danis HL, Ryan TC, Center DM (Feb 1996). "IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C". Cellular Immunology. 168 (1): 100–6. doi:10.1006/cimm.1996.0054. PMID 8599832.
• Conant K, Ma M, Nath A, Major EO (Mar 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". Journal of Virology. 70 (3): 1384–9. doi:10.1128/JVI.70.3.1384-1389.1996. PMC 189957. PMID 8627654.
• Díaz-Meco MT, Municio MM, Frutos S, Sanchez P, Lozano J, Sanz L, Moscat J (Sep 1996). "The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C". Cell. 86 (5): 777–86. doi:10.1016/S0092-8674(00)80152-X. PMID 8797824. S2CID 15675524.
• Holmes AM (Nov 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". Archives of Biochemistry and Biophysics. 335 (1): 8–12. doi:10.1006/abbi.1996.0476. PMID 8914829.
• Murray NR, Fields AP (Oct 1997). "Atypical protein kinase C iota protects human leukemia cells against drug-induced apoptosis". The Journal of Biological Chemistry. 272 (44): 27521–4. doi:10.1074/jbc.272.44.27521. PMID 9346882.
• Borgatti P, Zauli G, Cantley LC, Capitani S (Jan 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". Biochemical and Biophysical Research Communications. 242 (2): 332–7. doi:10.1006/bbrc.1997.7877. PMID 9446795.
• Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT (May 1998). "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62". Molecular and Cellular Biology. 18 (5): 3069–80. doi:10.1128/mcb.18.5.3069. PMC 110686. PMID 9566925.