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| Primary source |
Uniprot : Q04759
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| Name |
Protein kinase C theta type
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| Alternative name(s) |
nPKC-theta
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| Synonym(s) |
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| Organism |
Homo sapiens
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| Length |
706 aa
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| Protein existence |
---
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General annotation (Comments)
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top
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Catalytic activity
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ATP + a protein = ADP + a phosphoprotein.
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Cofactor
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Magnesium.
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Domain
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The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain.
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Enzyme regulation
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Three specific sites; Thr-538 (activation loop of the kinase domain), Ser-676 (turn motif) and Ser-695 (hydrophobic region), need to be phosphorylated for its full activation.
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Function
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This is a calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. Essential for T-cell receptor (TCR)-mediated T-cell activation, but is dispensable during TCR-dependent thymocyte development. Links the TCR signaling complex to the activation of NF-kappa-B in mature T lymphocytes. Required for interleukin-2 (IL2) production.
PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters.
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Ptm
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Autophosphorylation at Thr-219 is required for targeting to the TCR and cellular function of PKC upon antigen receptor ligation.
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Similarity
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Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
Contains 1 AGC-kinase C-terminal domain.
Contains 1 C2 domain.
Contains 2 phorbol-ester/DAG-type zinc fingers.
Contains 1 protein kinase domain.
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Subunit
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Interacts with GLRX3 (via N-terminus).
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Tissue specificity
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Skeletal muscle, megakaryoblastic cells and platelets.
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Biological process
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regulation of cell growth [GO:0001558]
protein amino acid phosphorylation [GO:0006468]
membrane protein ectodomain proteolysis [GO:0006509]
intracellular signaling pathway [GO:0023034]
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Molecular function
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protein kinase C activity [GO:0004697]
protein binding [GO:0005515]
ATP binding [GO:0005524]
metal ion binding [GO:0046872]
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Alternative product(s)
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top
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Uniprot Identifier
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Difference(s) with the 'canonical' sequence
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Notes
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Sequences
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Isoform 1
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Q04759-1
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---
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'Canonical' sequence
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Get Fasta
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Isoform 2
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Q04759-2
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550-612 : Missing
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---
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Get Fasta
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Feature key |
Position
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Length
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Description
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Feature identifier
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Region
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Domain
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8 - 123
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116
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C2
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Q04759-DOMAIN-8
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Domain
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380 - 634
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255
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Protein kinase
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Q04759-DOMAIN-380
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Domain
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635 - 706
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72
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AGC-kinase C-terminal
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Q04759-DOMAIN-635
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Nucleotide binding
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386 - 394
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9
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ATP (By similarity)
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Q04759-NP_BIND-386
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Zinc finger
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159 - 209
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51
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Phorbol-ester/DAG-type 1
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Q04759-ZN_FING-159
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Zinc finger
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231 - 281
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51
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Phorbol-ester/DAG-type 2
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Q04759-ZN_FING-231
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Sites
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Active site
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504 - 504
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1
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Proton acceptor (By similarity)
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Q04759-ACT_SITE-504
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Binding site
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409 - 409
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1
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ATP
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Q04759-BINDING-409
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Natural variations
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Natural variant site
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240 - 240
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1
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K -> N (in a colorectal adenocarcinoma sample; somatic mutation)
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VAR_042319
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Natural variant site
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306 - 306
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1
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D -> V (in dbSNP:rs45590231)
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VAR_042320
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Natural variant site
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330 - 330
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1
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P -> L (in dbSNP:rs2236379)
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VAR_020401
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Natural variant site
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354 - 354
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1
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D -> N (in dbSNP:rs34524148)
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VAR_042321
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Alternative sequence
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550 - 612
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63
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Missing
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VSP_017294
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Amino acid modifications
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Modified residue
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219 - 219
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1
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Phosphothreonine; by autocatalysis
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Q04759-MOD_RES-219
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Modified residue
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348 - 348
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1
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Phosphoserine
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Q04759-MOD_RES-348
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Modified residue
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384 - 384
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1
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N6-acetyllysine
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Q04759-MOD_RES-384
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Modified residue
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536 - 536
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1
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Phosphothreonine
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Q04759-MOD_RES-536
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Modified residue
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538 - 538
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1
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Phosphothreonine
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Q04759-MOD_RES-538
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Modified residue
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657 - 657
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1
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Phosphoserine
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Q04759-MOD_RES-657
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Modified residue
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676 - 676
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1
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Phosphoserine
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Q04759-MOD_RES-676
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Modified residue
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685 - 685
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1
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Phosphoserine
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Q04759-MOD_RES-685
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Modified residue
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695 - 695
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1
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Phosphoserine
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Q04759-MOD_RES-695
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Experimental info
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Mutagenesis
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219 - 219
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1
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T->A: Loss of transactivation of the IL2 promoter and translocation to the plasma membrane. No effect on kinase activity
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Q04759-MUTAGEN-219
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Mutagenesis
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409 - 409
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1
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K->A: Loss of kinase activity
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Q04759-MUTAGEN-409
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Mutagenesis
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538 - 538
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1
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T->A: Loss of kinase activity
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Q04759-MUTAGEN-538
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Mutagenesis
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676 - 676
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1
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S->A: Reduction in kinase activity
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Q04759-MUTAGEN-676
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Mutagenesis
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695 - 695
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1
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S->A: Reduction in kinase activity
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Q04759-MUTAGEN-695
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| 1 |
MSPFLRIGLS |
NFDCGSCQSC |
QGEAVNPYCA |
VLVKEYVESE |
NGQMYIQKKP |
TMYPPWDSTF |
DAHINKGRVM |
QIIVKGKNVD |
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| 81 |
LISETTVELY |
SLAERCRKNN |
GKTEIWLELK |
PQGRMLMNAR |
YFLEMSDTKD |
MNEFETEGFF |
ALHQRRGAIK |
QAKVHHVKCH |
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| 161 |
EFTATFFPQP |
TFCSVCHEFV |
WGLNKQGYQC |
RQCNAAIHKK |
CIDKVIAKCT |
GSAINSRETM |
FHKERFKIDM |
PHRFKVYNYK |
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| 241 |
SPTFCEHCGT |
LLWGLARQGL |
KCDACGMNVH |
HRCQTKVANL |
CGINQKLMAE |
ALAMIESTQQ |
ARCLRDTEQI |
FREGPVEIGL |
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| 321 |
PCSIKNEARP |
PCLPTPGKRE |
PQGISWESPL |
DEVDKMCHLP |
EPELNKERPS |
LQIKLKIEDF |
ILHKMLGKGS |
FGKVFLAEFK |
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| 401 |
KTNQFFAIKA |
LKKDVVLMDD |
DVECTMVEKR |
VLSLAWEHPF |
LTHMFCTFQT |
KENLFFVMEY |
LNGGDLMYHI |
QSCHKFDLSR |
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| 481 |
ATFYAAEIIL |
GLQFLHSKGI |
VYRDLKLDNI |
LLDKDGHIKI |
ADFGMCKENM |
LGDAKTNTFC |
GTPDYIAPEI |
LLGQKYNHSV |
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DWWSFGVLLY |
EMLIGQSPFH |
GQDEEELFHS |
IRMDNPFYPR |
WLEKEAKDLL |
VKLFVREPEK |
RLGVRGDIRQ |
HPLFREINWE |
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| 641 |
ELERKEIDPP |
FRPKVKSPFD |
CSNFDKEFLN |
EKPRLSFADR |
ALINSMDQNM |
FRNFSFMNPG |
MERLIS |
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>sp|Q04759|KPCT_human Protein kinase C theta type
MSPFLRIGLSNFDCGSCQSCQGEAVNPYCAVLVKEYVESENGQMYIQKKPTMYPPWDSTFDAHINKGRVMQIIVKGKNVD
LISETTVELYSLAERCRKNNGKTEIWLELKPQGRMLMNARYFLEMSDTKDMNEFETEGFFALHQRRGAIKQAKVHHVKCH
EFTATFFPQPTFCSVCHEFVWGLNKQGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYK
SPTFCEHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQARCLRDTEQIFREGPVEIGL
PCSIKNEARPPCLPTPGKREPQGISWESPLDEVDKMCHLPEPELNKERPSLQIKLKIEDFILHKMLGKGSFGKVFLAEFK
KTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKFDLSR
ATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTNTFCGTPDYIAPEILLGQKYNHSV
DWWSFGVLLYEMLIGQSPFHGQDEEELFHSIRMDNPFYPRWLEKEAKDLLVKLFVREPEKRLGVRGDIRQHPLFREINWE
ELERKEIDPPFRPKVKSPFDCSNFDKEFLNEKPRLSFADRALINSMDQNMFRNFSFMNPGMERLIS
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