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F1LM10

- F1LM10_RAT

UniProt

F1LM10 - F1LM10_RAT

Protein

Protein kinase C theta type

Gene

Prkcq

Organism
Rattus norvegicus (Rat)
Status
Unreviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 30 (01 Oct 2014)
      Sequence version 1 (03 May 2011)
      Previous versions | rss
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    Functioni

    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.UniRule annotation

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.UniRule annotationSAAS annotation

    Cofactori

    Magnesium.UniRule annotation

    Enzyme regulationi

    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.UniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein kinase C activity Source: UniProtKB-EC

    GO - Biological processi

    1. inflammatory response Source: UniProtKB-KW
    2. intracellular signal transduction Source: Ensembl
    3. membrane protein ectodomain proteolysis Source: Ensembl
    4. negative regulation of insulin receptor signaling pathway Source: Ensembl
    5. negative regulation of T cell apoptotic process Source: Ensembl
    6. positive regulation of interleukin-17 production Source: Ensembl
    7. positive regulation of interleukin-2 biosynthetic process Source: Ensembl
    8. positive regulation of interleukin-4 production Source: Ensembl
    9. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    10. positive regulation of T cell proliferation Source: Ensembl
    11. positive regulation of T-helper 17 type immune response Source: Ensembl
    12. positive regulation of T-helper 2 cell activation Source: Ensembl
    13. regulation of platelet aggregation Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinaseUniRule annotationSAAS annotation, Transferase

    Keywords - Biological processi

    Inflammatory responseUniRule annotation

    Keywords - Ligandi

    ATP-bindingUniRule annotationSAAS annotation, MagnesiumUniRule annotation, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_197513. FCERI mediated NF-kB activation.
    REACT_227662. Inactivation, recovery and regulation of the phototransduction cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C theta typeUniRule annotation (EC:2.7.11.13UniRule annotation)
    Alternative name(s):
    nPKC-thetaUniRule annotation
    Gene namesi
    Name:PrkcqImported
    OrganismiRattus norvegicus (Rat)Imported
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 17

    Organism-specific databases

    RGDi620968. Prkcq.

    Subcellular locationi

    Cytoplasm UniRule annotation. Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation
    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.UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. immunological synapse Source: Ensembl

    Keywords - Cellular componenti

    Cell membraneUniRule annotation, CytoplasmUniRule annotation, Membrane

    Interactioni

    Subunit structurei

    Interacts with GLRX3 (via N-terminus). Interacts with ECT2.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliF1LM10.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.UniRule annotation
    Contains AGC-kinase C-terminal domain.SAAS annotation
    Contains protein kinase domain.SAAS annotation

    Keywords - Domaini

    Zinc-fingerSAAS annotation

    Phylogenomic databases

    GeneTreeiENSGT00750000117339.
    KOiK18052.
    OMAiREPQGIS.
    OrthoDBiEOG77M8QM.
    TreeFamiTF102004.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR000008. C2_dom.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR027264. PKC_theta.
    IPR017892. Pkinase_C.
    IPR014376. Prot_kin_PKC_delta.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00130. C1_1. 2 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000551. PKC_delta. 1 hit.
    PIRSF501105. Protein_kin_C_theta. 1 hit.
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 2 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. 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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    F1LM10-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPFLRIGLS NFDCGTCQAC QGEAVNPYCA VLVKEYVESE NGQMYIQKKP    50
    TMYPPWDSTF DAHINKGRVM QIIVKGKNVD LISETTVELY SLAERCRKNN 100
    GRTEIWLELK PQGRMLMNAR YFLEMSDTKD MSEFENEGFF ALHHRRGAIK 150
    QAKVHHVKCH EFTATFFPQP TFCSVCHEFV WGLNKQGYQC RQCNAAIHKK 200
    CIDKVIAKCT GSAINSRETM FHKERFKIDM PHRFKVYNYK SPTFCEHCGT 250
    LLWGLARQGL KCDACGMNVH HRCQTKVANL CGINQKLMAE ALAMIESTQQ 300
    ARTLRDSEHI FREGPIEISF PRSIKSETRP PCVPTPGKKE PQGICWESPL 350
    DGADKTAQPP EPEVNLQRAS LQLKLKIDDF ILHKMLGKGS FGKVFLAEFK 400
    RTKQFFAIKA LKKDVVLMDD DVECTMVEKR VLSLAWEHPF LTHMFCTFQT 450
    KENLFFVMEY LNGGDLMYHI QSCHKFDLSR ATFYAAEIIL GLQFLHSKGI 500
    VYRDLKLDNI LLDRDGHIKI ADFGMCKENM LGDAKTNTFC GTPDYIAPEI 550
    LLGQKYNHSV DWWSFGVLLY EMLIGQSPFH GQDEEELFHS IRMDNPFYPR 600
    WLEREAKDLL VKLFVREPEK RLGVRGDIRQ HPLFREINWE ELERKEIDPP 650
    FRPKVKSPYD CSNFDKEFLS EKPRLSFADR ALINSMDQNM FSNFSFINPG 700
    METLICS 707
    Length:707
    Mass (Da):81,777
    Last modified:May 3, 2011 - v1
    Checksum:i7F81E6A3371B99A7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_001263650.1. NM_001276721.1.
    UniGeneiRn.8227.

    Genome annotation databases

    EnsembliENSRNOT00000025901; ENSRNOP00000025902; ENSRNOG00000019057.
    GeneIDi85420.
    KEGGirno:85420.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqi NP_001263650.1. NM_001276721.1.
    UniGenei Rn.8227.

    3D structure databases

    ProteinModelPortali F1LM10.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000025901 ; ENSRNOP00000025902 ; ENSRNOG00000019057 .
    GeneIDi 85420.
    KEGGi rno:85420.

    Organism-specific databases

    CTDi 5588.
    RGDi 620968. Prkcq.

    Phylogenomic databases

    GeneTreei ENSGT00750000117339.
    KOi K18052.
    OMAi REPQGIS.
    OrthoDBi EOG77M8QM.
    TreeFami TF102004.

    Enzyme and pathway databases

    Reactomei REACT_197513. FCERI mediated NF-kB activation.
    REACT_227662. Inactivation, recovery and regulation of the phototransduction cascade.

    Miscellaneous databases

    NextBioi 617498.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000961. AGC-kinase_C.
    IPR000008. C2_dom.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR027264. PKC_theta.
    IPR017892. Pkinase_C.
    IPR014376. Prot_kin_PKC_delta.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00130. C1_1. 2 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000551. PKC_delta. 1 hit.
    PIRSF501105. Protein_kin_C_theta. 1 hit.
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 2 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown NorwayImported.
    2. Ensembl
      Submitted (JUL-2011) to UniProtKB
      Cited for: IDENTIFICATION.
      Strain: Brown NorwayImported.

    Entry informationi

    Entry nameiF1LM10_RAT
    AccessioniPrimary (citable) accession number: F1LM10
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 3, 2011
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 30 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Caution

    The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3