Protein kinase C iota type

Details

Name
Protein kinase C iota type
Synonyms
  • 2.7.11.13
  • aPKC-lambda/iota
  • Atypical protein kinase C-lambda/iota
  • DXS1179E
  • nPKC-iota
  • PRKC-lambda/iota
Gene Name
PRKCI
Organism
Humans
Amino acid sequence
>lcl|BSEQ0007450|Protein kinase C iota type
MPTQRDSSTMSHTVAGGGSGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCNEVRDMCSF
DNEQLFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGE
DKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHK
KCHKLVTIECGRHSLPQEPVMPMDQSSMHSDHAQTVIPYNPSSHESLDQVGEEKEAMNTR
ESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQ
TEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSA
EISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYI
APEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIR
IPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFK
PNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV
Number of residues
596
Molecular Weight
68261.855
Theoretical pI
5.68
GO Classification
Functions
ATP binding / metal ion binding / phospholipid binding / protein kinase activity / protein kinase C activity / protein serine/threonine kinase activity
Processes
actin filament organization / bicellular tight junction assembly / cell junction assembly / cell migration / cell-cell junction organization / cellular response to insulin stimulus / cytoskeleton organization / establishment of apical/basal cell polarity / establishment or maintenance of epithelial cell apical/basal polarity / eye photoreceptor cell development / Golgi vesicle budding / intracellular signal transduction / membrane organization / negative regulation of apoptotic process / negative regulation of glial cell apoptotic process / negative regulation of neuron apoptotic process / neurotrophin TRK receptor signaling pathway / positive regulation of endothelial cell apoptotic process / positive regulation of establishment of protein localization to plasma membrane / positive regulation of glial cell proliferation / positive regulation of glucose import / positive regulation of neuron projection development / positive regulation of NF-kappaB transcription factor activity / protein phosphorylation / protein targeting to membrane / response to interleukin-1 / secretion / vesicle-mediated transport
Components
apical plasma membrane / bicellular tight junction / cell leading edge / cytoplasm / cytosol / endosome / extracellular exosome / Golgi membrane / intercellular bridge / microtubule cytoskeleton / nucleus / plasma membrane / protein complex / Schmidt-Lanterman incisure
General Function
Protein serine/threonine kinase activity
Specific Function
Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0017259|Protein kinase C iota type (PRKCI)
ATGCCGACCCAGAGGGACAGCAGCACCATGTCCCACACGGTCGCAGGCGGCGGCAGCGGG
GACCATTCCCACCAGGTCCGGGTGAAAGCCTACTACCGCGGGGATATCATGATAACACAT
TTTGAACCTTCCATCTCCTTTGAGGGCCTTTGCAATGAGGTTCGAGACATGTGTTCTTTT
GACAACGAACAGCTCTTCACCATGAAATGGATAGATGAGGAAGGAGACCCGTGTACAGTA
TCATCTCAGTTGGAGTTAGAAGAAGCCTTTAGACTTTATGAGCTAAACAAGGATTCTGAA
CTCTTGATTCATGTGTTCCCTTGTGTACCAGAACGTCCTGGGATGCCTTGTCCAGGAGAA
GATAAATCCATCTACCGTAGAGGTGCACGCCGCTGGAGAAAGCTTTATTGTGCCAATGGC
CACACTTTCCAAGCCAAGCGTTTCAACAGGCGTGCTCACTGTGCCATCTGCACAGACCGA
ATATGGGGACTTGGACGCCAAGGATATAAGTGCATCAACTGCAAACTCTTGGTTCATAAG
AAGTGCCATAAACTCGTCACAATTGAATGTGGGCGGCATTCTTTGCCACAGGAACCAGTG
ATGCCCATGGATCAGTCATCCATGCATTCTGACCATGCACAGACAGTAATTCCATATAAT
CCTTCAAGTCATGAGAGTTTGGATCAAGTTGGTGAAGAAAAAGAGGCAATGAACACCAGG
GAAAGTGGCAAAGCTTCATCCAGTCTAGGTCTTCAGGATTTTGATTTGCTCCGGGTAATA
GGAAGAGGAAGTTATGCCAAAGTACTGTTGGTTCGATTAAAAAAAACAGATCGTATTTAT
GCAATGAAAGTTGTGAAAAAAGAGCTTGTTAATGATGATGAGGATATTGATTGGGTACAG
ACAGAGAAGCATGTGTTTGAGCAGGCATCCAATCATCCTTTCCTTGTTGGGCTGCATTCT
TGCTTTCAGACAGAAAGCAGATTGTTCTTTGTTATAGAGTATGTAAATGGAGGAGACCTA
ATGTTTCATATGCAGCGACAAAGAAAACTTCCTGAAGAACATGCCAGATTTTACTCTGCA
GAAATCAGTCTAGCATTAAATTATCTTCATGAGCGAGGGATAATTTATAGAGATTTGAAA
CTGGACAATGTATTACTGGACTCTGAAGGCCACATTAAACTCACTGACTACGGCATGTGT
AAGGAAGGATTACGGCCAGGAGATACAACCAGCACTTTCTGTGGTACTCCTAATTACATT
GCTCCTGAAATTTTAAGAGGAGAAGATTATGGTTTCAGTGTTGACTGGTGGGCTCTTGGA
GTGCTCATGTTTGAGATGATGGCAGGAAGGTCTCCATTTGATATTGTTGGGAGCTCCGAT
AACCCTGACCAGAACACAGAGGATTATCTCTTCCAAGTTATTTTGGAAAAACAAATTCGC
ATACCACGTTCTCTGTCTGTAAAAGCTGCAAGTGTTCTGAAGAGTTTTCTTAATAAGGAC
CCTAAGGAACGATTGGGTTGTCATCCTCAAACAGGATTTGCTGATATTCAGGGACACCCG
TTCTTCCGAAATGTTGATTGGGATATGATGGAGCAAAAACAGGTGGTACCTCCCTTTAAA
CCAAATATTTCTGGGGAATTTGGTTTGGACAACTTTGATTCTCAGTTTACTAATGAACCT
GTCCAGCTCACTCCAGATGACGATGACATTGTGAGGAAGATTGATCAGTCTGAATTTGAA
GGTTTTGAGTATATCAATCCTCTTTTGATGTCTGCAGAAGAATGTGTCTGA
Chromosome Location
3
Locus
3q26.3
External Identifiers
ResourceLink
UniProtKB IDP41743
UniProtKB Entry NameKPCI_HUMAN
GenBank Protein ID432274
GenBank Gene IDL18964
HGNC IDHGNC:9404
General References
  1. Selbie LA, Schmitz-Peiffer C, Sheng Y, Biden TJ: Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells. J Biol Chem. 1993 Nov 15;268(32):24296-302. [PubMed:8226978]
  2. Mazzarella R, Ciccodicola A, Esposito T, Arcucci A, Migliaccio C, Jones C, Schlessinger D, D'Urso M, D'Esposito M: Human protein kinase C Iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3. Genomics. 1995 Apr 10;26(3):629-31. [PubMed:7607695]
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  4. Diaz-Meco MT, Municio MM, Sanchez P, Lozano J, Moscat J: 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. Mol Cell Biol. 1996 Jan;16(1):105-14. [PubMed:8524286]
  5. Murray NR, Fields AP: Atypical protein kinase C iota protects human leukemia cells against drug-induced apoptosis. J Biol Chem. 1997 Oct 31;272(44):27521-4. [PubMed:9346882]
  6. Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT: Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62. Mol Cell Biol. 1998 May;18(5):3069-80. [PubMed:9566925]
  7. Wooten MW, Seibenhener ML, Zhou G, Vandenplas ML, Tan TH: Overexpression of atypical PKC in PC12 cells enhances NGF-responsiveness and survival through an NF-kappaB dependent pathway. Cell Death Differ. 1999 Aug;6(8):753-64. [PubMed:10467349]
  8. Sanz L, Sanchez P, Lallena MJ, Diaz-Meco MT, Moscat J: The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. EMBO J. 1999 Jun 1;18(11):3044-53. [PubMed:10356400]
  9. Spitaler M, Villunger A, Grunicke H, Uberall F: Unique structural and functional properties of the ATP-binding domain of atypical protein kinase C-iota. J Biol Chem. 2000 Oct 27;275(43):33289-96. [PubMed:10906326]
  10. Xie J, Guo Q, Zhu H, Wooten MW, Mattson MP: Protein kinase C iota protects neural cells against apoptosis induced by amyloid beta-peptide. Brain Res Mol Brain Res. 2000 Oct 20;82(1-2):107-13. [PubMed:11042363]
  11. Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H: Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells. 2001 Feb;6(2):107-19. [PubMed:11260256]
  12. Suzuki A, Yamanaka T, Hirose T, Manabe N, Mizuno K, Shimizu M, Akimoto K, Izumi Y, Ohnishi T, Ohno S: Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures. J Cell Biol. 2001 Mar 19;152(6):1183-96. [PubMed:11257119]
  13. Tisdale EJ: Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway. J Biol Chem. 2002 Feb 1;277(5):3334-41. Epub 2001 Nov 27. [PubMed:11724794]
  14. Wooten MW, Vandenplas ML, Seibenhener ML, Geetha T, Diaz-Meco MT: Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase C's via a src kinase pathway. Mol Cell Biol. 2001 Dec;21(24):8414-27. [PubMed:11713277]
  15. White WO, Seibenhener ML, Wooten MW: Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C. J Cell Biochem. 2002;85(1):42-53. [PubMed:11891849]
  16. Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A: Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C. Biochem Biophys Res Commun. 2003 Aug 1;307(3):459-65. [PubMed:12893243]
  17. Yamanaka T, Horikoshi Y, Sugiyama Y, Ishiyama C, Suzuki A, Hirose T, Iwamatsu A, Shinohara A, Ohno S: Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity. Curr Biol. 2003 Apr 29;13(9):734-43. [PubMed:12725730]
  18. Tisdale EJ, Wang J, Silver RB, Artalejo CR: Atypical protein kinase C plays a critical role in protein transport from pre-Golgi intermediates. J Biol Chem. 2003 Sep 26;278(39):38015-21. Epub 2003 Jul 17. [PubMed:12871960]
  19. Tisdale EJ: Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation. J Biol Chem. 2003 Dec 26;278(52):52524-30. Epub 2003 Oct 21. [PubMed:14570876]
  20. Mamidipudi V, Lin C, Seibenhener ML, Wooten MW: Regulation of interleukin receptor-associated kinase (IRAK) phosphorylation and signaling by iota protein kinase C. J Biol Chem. 2004 Feb 6;279(6):4161-5. Epub 2003 Dec 18. [PubMed:14684752]
  21. Regala RP, Weems C, Jamieson L, Copland JA, Thompson EA, Fields AP: Atypical protein kinase Ciota plays a critical role in human lung cancer cell growth and tumorigenicity. J Biol Chem. 2005 Sep 2;280(35):31109-15. Epub 2005 Jul 1. [PubMed:15994303]
  22. Bicaku E, Patel R, Acevedo-Duncan M: Cyclin-dependent kinase activating kinase/Cdk7 co-localizes with PKC-iota in human glioma cells. Tissue Cell. 2005 Feb;37(1):53-8. Epub 2005 Jan 25. [PubMed:15695176]
  23. Fritzius T, Burkard G, Haas E, Heinrich J, Schweneker M, Bosse M, Zimmermann S, Frey AD, Caelers A, Bachmann AS, Moelling K: A WD-FYVE protein binds to the kinases Akt and PKCzeta/lambda. Biochem J. 2006 Oct 1;399(1):9-20. [PubMed:16792529]
  24. Tisdale EJ, Artalejo CR: Src-dependent aprotein kinase C iota/lambda (aPKCiota/lambda) tyrosine phosphorylation is required for aPKCiota/lambda association with Rab2 and glyceraldehyde-3-phosphate dehydrogenase on pre-golgi intermediates. J Biol Chem. 2006 Mar 31;281(13):8436-42. Epub 2006 Feb 1. [PubMed:16452474]
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  28. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976]
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  30. Staiger K, Schatz U, Staiger H, Weyrich P, Haas C, Guirguis A, Machicao F, Haring HU, Kellerer M: Protein kinase C iota mediates lipid-induced apoptosis of human coronary artery endothelial cells. Microvasc Res. 2009 Jun;78(1):40-4. doi: 10.1016/j.mvr.2009.01.014. Epub 2009 Mar 25. [PubMed:19327373]
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  39. Hirano Y, Yoshinaga S, Ogura K, Yokochi M, Noda Y, Sumimoto H, Inagaki F: Solution structure of atypical protein kinase C PB1 domain and its mode of interaction with ZIP/p62 and MEK5. J Biol Chem. 2004 Jul 23;279(30):31883-90. Epub 2004 May 13. [PubMed:15143057]
  40. Hirano Y, Yoshinaga S, Takeya R, Suzuki NN, Horiuchi M, Kohjima M, Sumimoto H, Inagaki F: Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains. J Biol Chem. 2005 Mar 11;280(10):9653-61. Epub 2004 Dec 7. [PubMed:15590654]
  41. Messerschmidt A, Macieira S, Velarde M, Badeker M, Benda C, Jestel A, Brandstetter H, Neuefeind T, Blaesse M: Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. J Mol Biol. 2005 Sep 30;352(4):918-31. [PubMed:16125198]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03777Rbt205 InhibitorexperimentalunknownDetails
DB12010Fostamatinibapproved, investigationalunknowninhibitorDetails
DB00675TamoxifenapprovedunknowninhibitorDetails