A0A8C0PJV6 · A0A8C0PJV6_CANLF

Function

function

Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis.

Catalytic activity

Activity regulation

Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are calcium-insensitive, but activated by diacylglycerol (DAG) and phosphatidylserine. Three specific sites; Thr-513 (activation loop of the kinase domain), Thr-656 (turn motif) and Ser-675 (hydrophobic region), need to be phosphorylated for its full activation.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site361-369ATP (UniProtKB | ChEBI)
Binding site384ATP (UniProtKB | ChEBI)
Active site479Proton acceptor

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functiondiacylglycerol-dependent serine/threonine kinase activity
Molecular Functionmetal ion binding
Biological Processcell differentiation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein kinase C eta type
  • EC number
  • Alternative names
    • PKC-L
    • nPKC-eta

Gene names

    • Name
      PRKCH

Organism names

Accessions

  • Primary accession
    A0A8C0PJV6
  • Secondary accessions
    • A0A8P0NH77

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-118C2
Domain171-222Phorbol-ester/DAG-type
Domain245-295Phorbol-ester/DAG-type
Region320-343Disordered
Domain355-614Protein kinase
Domain615-683AGC-kinase C-terminal

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    683
  • Mass (Da)
    77,883
  • Last updated
    2022-01-19 v1
  • Checksum
    555698F6655DF73F
MTSGSMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGYQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTAGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKMDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGRENTKEGNGVGVNSSSRLGIDNFEFIRVLGKGSFGKVMLARIKETGELYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHEKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHDDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQVEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSFVSPELQP

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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