F1LM10 (F1LM10_RAT) Unreviewed, UniProtKB/TrEMBL
Last modified April 16, 2014. Version 28. History...
Names and origin
|Protein names||Recommended name:|
Protein kinase C theta type PIRNR PIRNR000551
EC=18.104.22.168 PIRNR PIRNR000551
nPKC-theta PIRNR PIRNR000551
|Organism||Rattus norvegicus (Rat) [Reference proteome] Ensembl ENSRNOP00000025902|
|Taxonomic identifier||10116 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus|
|Sequence length||707 AA.|
|Protein existence||Inferred from homology|
General annotation (Comments)
Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates to the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1 By similarity. PIRNR PIRNR000551
Magnesium By similarity. PIRNR PIRNR000551
Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are calcium-insensitive, but activated by diacylglycerol (DAG) and phosphatidylserine. 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 By similarity. PIRNR PIRNR000551
Interacts with GLRX3 (via N-terminus). Interacts with ECT2 By similarity. PIRNR PIRNR000551
Cytoplasm. Cell membrane; Peripheral membrane protein. Note: In resting T-cells, mostly localized in cytoplasm. In response to TCR stimulation, associates with lipid rafts and then localizes in the immunological synapse By similarity. PIRNR PIRNR000551
Contains 1 protein kinase domain.
Contains AGC-kinase C-terminal domain. SAAS SAAS017892
Contains protein kinase domain. SAAS SAAS017892
The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSRNOP00000025902
|||"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."|
Rat Genome Sequencing Project Consortium
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway Ensembl ENSRNOP00000025902.
Submitted (JUL-2011) to UniProtKB
Cited for: IDENTIFICATION.
Strain: Brown Norway Ensembl ENSRNOP00000025902.
|+||Additional computationally mapped references.|
|AABR06092751 Genomic DNA. No translation available.|
AABR06092752 Genomic DNA. No translation available.
AABR06092753 Genomic DNA. No translation available.
AABR06092754 Genomic DNA. No translation available.
AABR06092755 Genomic DNA. No translation available.
AABR06092756 Genomic DNA. No translation available.
AABR06092757 Genomic DNA. No translation available.
AABR06092758 Genomic DNA. No translation available.
AABR06092759 Genomic DNA. No translation available.
|RefSeq||NP_001263650.1. NM_001276721.1. |
3D structure databases
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSRNOT00000025901; ENSRNOP00000025902; ENSRNOG00000019057. |
|RGD||620968. Prkcq. |
Family and domain databases
|Gene3D||22.214.171.124. 1 hit. |
|InterPro||IPR000961. AGC-kinase_C. |
|Pfam||PF00130. C1_1. 2 hits. |
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
|PIRSF||PIRSF000551. PKC_delta. 1 hit. |
PIRSF501105. Protein_kin_C_theta. 1 hit.
|PRINTS||PR00008. DAGPEDOMAIN. |
|SMART||SM00109. C1. 2 hits. |
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
|SUPFAM||SSF49562. SSF49562. 1 hit. |
SSF56112. SSF56112. 1 hit.
|PROSITE||PS51285. AGC_KINASE_CTER. 1 hit. |
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
|Accession||Primary (citable) accession number: F1LM10|
|Entry status||Unreviewed (UniProtKB/TrEMBL)|