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Reviewed, UniProtKB/Swiss-Prot Q02111 (KPCT_MOUSE)

Last modified February 9, 2010. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein kinase C theta type
    EC=2.7.11.13
Alternative name(s):
    nPKC-theta
Gene names
Name: Prkcq
Synonyms: Pkcq
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length707 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. Ref.1 Ref.2

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. Ref.1 Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

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.

Subunit structure

Interacts with TXNL2/PICOT By similarity.

Tissue specificity

T-lymphocytes and skeletal muscle. Ref.1 Ref.2

Domain

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.

Post-translational modification

Autophosphorylation at Thr-219 is required for targeting to the TCR and cellular function of PKC upon antigen receptor ligation.

Sequence similarities

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 707707Protein kinase C theta type
PRO_0000055709

Regions

Domain8 – 123116C2
Domain380 – 634255Protein kinase
Domain635 – 70672AGC-kinase C-terminal
Zinc finger159 – 20951Phorbol-ester/DAG-type 1
Zinc finger231 – 28151Phorbol-ester/DAG-type 2
Nucleotide binding386 – 3949ATP By similarity

Sites

Active site5041Proton acceptor By similarity
Binding site4091ATP By similarity

Amino acid modifications

Modified residue2191Phosphothreonine; by autocatalysis By similarity
Modified residue3481Phosphoserine By similarity
Modified residue3841N6-acetyllysine By similarity
Modified residue5361Phosphothreonine By similarity
Modified residue5381Phosphothreonine By similarity
Modified residue6571Phosphoserine By similarity
Modified residue6761Phosphoserine By similarity
Modified residue6851Phosphoserine By similarity
Modified residue6951Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02111-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 7A16492116CD2880

FASTA70781,573
        10         20         30         40         50         60 
MSPFLRIGLS NFDCGTCQAC QGEAVNPYCA VLVKEYVESE NGQMYIQKKP TMYPPWDSTF 

        70         80         90        100        110        120 
DAHINKGRVM QIIVKGKNVD LISETTVELY SLAERCRKNN GRTEIWLELK PQGRMLMNAR 

       130        140        150        160        170        180 
YFLEMSDTKD MSEFENEGFF ALHQRRGAIK QAKVHHVKCH EFTATFFPQP TFCSVCHEFV 

       190        200        210        220        230        240 
WGLNKQGYQC RQCNAAIHKK CIDKVIAKCT GSAINSRETM FHKERFKIDM PHRFKVYNYK 

       250        260        270        280        290        300 
SPTFCEHCGT LLWGLARQGL KCDACGMNVH HRCQTKVANL CGINQKLMAE ALAMIESTQQ 

       310        320        330        340        350        360 
ARSLRDSEHI FREGPVEIGL PCSTKNETRP PCVPTPGKRE PQGISWDSPL DGSNKSAGPP 

       370        380        390        400        410        420 
EPEVSMRRTS LQLKLKIDDF ILHKMLGKGS FGKVFLAEFK RTNQFFAIKA LKKDVVLMDD 

       430        440        450        460        470        480 
DVECTMVEKR VLSLAWEHPF LTHMFCTFQT KENLFFVMEY LNGGDLMYHI QSCHKFDLSR 

       490        500        510        520        530        540 
ATFYAAEVIL GLQFLHSKGI VYRDLKLDNI LLDRDGHIKI ADFGMCKENM LGDAKTNTFC 

       550        560        570        580        590        600 
GTPDYIAPEI LLGQKYNHSV DWWSFGVLVY EMLIGQSPFH GQDEEELFHS IRMDNPFYPR 

       610        620        630        640        650        660 
WLEREAKDLL VKLFVREPEK RLGVRGDIRQ HPLFREINWE ELERKEIDPP FRPKVKSPYD 

       670        680        690        700 
CSNFDKEFLS EKPRLSFADR ALINSMDQNM FSNFSFINPG METLICS 

« Hide

References

[1]"A new member of the protein kinase C family, nPKC theta, predominantly expressed in skeletal muscle."
Osada S., Mizuno K., Saido T.C., Suzuki K., Kuroki T., Ohno S.
Mol. Cell. Biol. 12:3930-3938(1992) [PubMed: 1508194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
[2]"PKC-theta is required for TCR-induced NF-kappaB activation in mature but not immature T lymphocytes."
Sun Z., Arendt C.W., Ellmeier W., Schaeffer E.M., Sunshine M.J., Gandhi L., Annes J., Petrzilka D., Kupfer A., Schwartzberg P.L., Littman D.R.
Nature 404:402-407(2000) [PubMed: 10746729] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D11091 mRNA. Translation: BAA01864.1.
IPIIPI00124496.
PIRA44500.
RefSeqNP_032885.1.
UniGeneMm.329993

3D structure databases

SMRQ02111. Positions 3-126, 144-213, 157-252, 227-284, 375-700.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ02111.

PTM databases

PhosphoSiteQ02111.

Proteomic databases

PRIDEQ02111.

Genome annotation databases

EnsemblENSMUST00000028118; ENSMUSP00000028118; ENSMUSG00000026778; Mus musculus. [Genome view]
GeneID18761.
KEGGmmu:18761.
UCSCuc008iic.1. mouse.

Organism-specific databases

CTD18761.
MGIMGI:97601. Prkcq.

Phylogenomic databases

eggNOGroNOG07577.
HOGENOMHBG755340.
HOVERGENQ02111.
InParanoidQ02111.
OMAAKTNTFC.
PhylomeDBQ02111.

Enzyme and pathway databases

BRENDA2.7.11.13. 244.

Gene expression databases

ArrayExpressQ02111.
BgeeQ02111.
CleanExMM_PRKCQ.
GenevestigatorQ02111.
GermOnlineENSMUSG00000026778. Mus musculus.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR020454. DAG/PE_bd.
IPR011009. Kinase-like_dom.
IPR015745. PKC.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR002219. Prot_Kinase_C-like_PE/DAG_bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PANTHERPTHR22985:SF86. PKC. 1 hit.
PfamPF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000551. PKC_delta. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. False negative.
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.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio294949.
SOURCESearch...

Entry information

Entry nameKPCT_MOUSE
AccessionPrimary (citable) accession number: Q02111
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 9, 2010
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents