KPCT_RAT
ID KPCT_RAT Reviewed; 707 AA.
AC Q9WTQ0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein kinase C theta type;
DE EC=2.7.11.13 {ECO:0000250|UniProtKB:Q04759};
DE AltName: Full=nPKC-theta;
GN Name=Prkcq; Synonyms=Pkcq;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 524-667.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=11220785; DOI=10.1385/jmn:15:2:121;
RA Minami H., Owada Y., Suzuki R., Handa Y., Kondo H.;
RT "Localization of mRNAs for novel, atypical as well as conventional protein
RT kinase C (PKC) isoforms in the brain of developing and mature rats.";
RL J. Mol. Neurosci. 15:121-135(2000).
RN [3]
RP FUNCTION IN PHOSPHORYLATION OF MSN.
RX PubMed=9516463; DOI=10.1074/jbc.273.13.7594;
RA Pietromonaco S.F., Simons P.C., Altman A., Elias L.;
RT "Protein kinase C-theta phosphorylation of moesin in the actin-binding
RT sequence.";
RL J. Biol. Chem. 273:7594-7603(1998).
RN [4]
RP INTERACTION WITH GLRX3.
RX PubMed=18479680; DOI=10.1016/j.cellimm.2008.04.005;
RA Kato N., Motohashi S., Okada T., Ozawa T., Mashima K.;
RT "PICOT, protein kinase C theta-interacting protein, is a novel regulator of
RT FcepsilonRI-mediated mast cell activation.";
RL Cell. Immunol. 251:62-67(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-
CC dependent serine/threonine-protein kinase that mediates non-redundant
CC functions in T-cell receptor (TCR) signaling, including T-cells
CC activation, proliferation, differentiation and survival, by mediating
CC activation of multiple transcription factors such as NF-kappa-B, JUN,
CC NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required
CC for the activation of NF-kappa-B and JUN, which in turn are essential
CC for IL2 production, and participates in the calcium-dependent NFATC1
CC and NFATC2 transactivation. Mediates the activation of the canonical
CC NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on
CC several serine residues, inducing CARD11 association with lipid rafts
CC and recruitment of the BCL10-MALT1 complex, which then activates IKK
CC complex, resulting in nuclear translocation and activation of NFKB1.
CC May also play an indirect role in activation of the non-canonical NF-
CC kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN
CC activation, acts by phosphorylating the mediator STK39/SPAK and may not
CC act through MAP kinases signaling. Plays a critical role in TCR/CD28-
CC induced NFATC1 and NFATC2 transactivation by participating in the
CC regulation of reduced inositol 1,4,5-trisphosphate generation and
CC intracellular calcium mobilization. After costimulation of T-cells
CC through CD28 can phosphorylate CBLB and is required for the
CC ubiquitination and subsequent degradation of CBLB, which is a
CC prerequisite for the activation of TCR. During T-cells differentiation,
CC plays an important role in the development of T-helper 2 (Th2) cells
CC following immune and inflammatory responses, and, in the development of
CC inflammatory autoimmune diseases, is necessary for the activation of
CC IL17-producing Th17 cells. May play a minor role in Th1 response. Upon
CC TCR stimulation, mediates T-cell protective survival signal by
CC phosphorylating BAD, thus protecting T-cells from BAD-induced
CC apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-
CC kappa-B and JUN pathways. In platelets, regulates signal transduction
CC downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors,
CC playing a positive role in 'outside-in' signaling and granule secretion
CC signal transduction. May relay signals from the activated ITGA2B
CC receptor by regulating the uncoupling of WASP and WIPF1, thereby
CC permitting the regulation of actin filament nucleation and branching
CC activity of the Arp2/3 complex. May mediate inhibitory effects of free
CC fatty acids on insulin signaling by phosphorylating IRS1, which in turn
CC blocks IRS1 tyrosine phosphorylation and downstream activation of the
CC PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of
CC phosphatidylglycerol or phosphatidylinositol (By similarity).
CC Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively
CC regulates its ability to phosphorylate PKB/AKT1 (By similarity).
CC Phosphorylates CCDC88A/GIV and inhibits its guanine nucleotide exchange
CC factor activity (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q04759, ECO:0000269|PubMed:9516463}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC Evidence={ECO:0000250|UniProtKB:Q04759};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
CC calcium-insensitive, but activated by diacylglycerol (DAG) and
CC phosphatidylserine. Three specific sites; Thr-538 (activation loop of
CC the kinase domain), Ser-676 (turn motif) and Ser-695 (hydrophobic
CC region), need to be phosphorylated for its full activation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of a membrane raft complex composed at least of BCL10,
CC CARD11, MALT1 and IKBKB (By similarity). Interacts with GLRX3 (via N-
CC terminus) (PubMed:18479680). Interacts with ECT2 (By similarity).
CC Interacts with CCDC88A/GIV; the interaction leads to phosphorylation of
CC CCDC88A and inhibition of its guanine nucleotide exchange factor
CC activity (By similarity). {ECO:0000250|UniProtKB:Q04759,
CC ECO:0000269|PubMed:18479680}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein. Note=In resting T-cells,
CC mostly localized in cytoplasm. In response to TCR stimulation,
CC associates with lipid rafts and then localizes in the immunological
CC synapse (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type region 1
CC (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a
CC non-calcium binding domain.
CC -!- PTM: Autophosphorylation at Thr-219 is required for targeting to the
CC TCR and cellular function of PRKCQ upon antigen receptor ligation.
CC Following TCR stimulation, phosphorylated at Tyr-90 and Ser-685 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; AABR03106275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03107517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03106934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03106283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03107733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03106804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03108584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03106764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB020614; BAA78371.1; -; mRNA.
DR AlphaFoldDB; Q9WTQ0; -.
DR SMR; Q9WTQ0; -.
DR IntAct; Q9WTQ0; 2.
DR STRING; 10116.ENSRNOP00000025902; -.
DR BindingDB; Q9WTQ0; -.
DR ChEMBL; CHEMBL2094266; -.
DR DrugCentral; Q9WTQ0; -.
DR iPTMnet; Q9WTQ0; -.
DR PhosphoSitePlus; Q9WTQ0; -.
DR PaxDb; Q9WTQ0; -.
DR PRIDE; Q9WTQ0; -.
DR UCSC; RGD:620968; rat.
DR RGD; 620968; Prkcq.
DR eggNOG; KOG0694; Eukaryota.
DR InParanoid; Q9WTQ0; -.
DR PhylomeDB; Q9WTQ0; -.
DR Reactome; R-RNO-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-RNO-202424; Downstream TCR signaling.
DR Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-RNO-373752; Netrin-1 signaling.
DR Reactome; R-RNO-9648002; RAS processing.
DR PRO; PR:Q9WTQ0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0004697; F:protein kinase C activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0060326; P:cell chemotaxis; ISO:RGD.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISO:RGD.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0070233; P:negative regulation of T cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:RGD.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:RGD.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; ISS:UniProtKB.
DR GO; GO:2000570; P:positive regulation of T-helper 2 cell activation; ISS:UniProtKB.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:RGD.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:RGD.
DR GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEP:RGD.
DR GO; GO:0045730; P:respiratory burst; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0042246; P:tissue regeneration; IEP:RGD.
DR CDD; cd00029; C1; 2.
DR CDD; cd05619; STKc_nPKC_theta; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR034668; nPKC_theta.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR027264; PKC_theta.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR014376; Prot_kin_PKC_delta.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000551; PKC_delta; 1.
DR PIRSF; PIRSF501105; Protein_kin_C_theta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Immunity; Inflammatory response;
KW Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..707
FT /note="Protein kinase C theta type"
FT /id="PRO_0000270836"
FT DOMAIN 1..107
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 380..634
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 635..706
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 159..209
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 231..281
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ACT_SITE 504
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 386..394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 90
FT /note="Phosphotyrosine; by LCK"
FT /evidence="ECO:0000250|UniProtKB:Q04759"
FT MOD_RES 219
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q04759"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04759"
FT MOD_RES 538
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:Q04759"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04759"
FT MOD_RES 695
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q04759, ECO:0000255"
SQ SEQUENCE 707 AA; 81750 MW; 7F82E35DE0C09DB9 CRC64;
MSPFLRIGLS NFDCGTCQAC QGEAVNPYCA VLVKEYVESE NGQMYIQKKP TMYPPWDSTF
DAHINKGRVM QIIVKGKNVD LISETTVELY SLAERCRKNN GRTEIWLELK PQGRMLMNAR
YFLEMSDTKD MSEFENEGFF ALHHRRGAIK QAKVHHVKCH EFTATFFPQP TFCSVCHEFV
WGLNKQGYQC RRCNAAIHKK CIDKVIAKCT GSAINSRETM FHKERFKIDM PHRFKVYNYK
SPTFCEHCGT LLWGLARQGL KCDACGMNVH HRCQTKVANL CGINQKLMAE ALAMIESTQQ
ARTLRDSEHI FREGPIEISF PRSIKSETRP PCVPTPGKSE PQGICWESPL DGADKTAQPP
EPEVNLQRAS LQLKLKIDDF ILHKMLGKGS FGKVFLAEFK RTKQFFAIKA LKKDVVLMDD
DVECTMVEKR VLSLAWEHPF LTHMFCTFQT KENLFFVMEY LNGGDLMYHI QSCHKFDLSR
ATFYAAEVIL GLQFLHSKGI VYRDLKLDNI LLDRDGHIKI ADFGMCKENM LGDAKTNTFC
GTPDYIAPEI LLGQKYNHSV DWWSFGVLLY EMLIGQSPFH GQDEEELFHS IRMDNPFYPR
WLEREAKDLL VKLFVREPEK RLGVRGDIRQ HPLFREINWE ELERKEIDPP FRPKVKSPYD
CSNFDKEFLS EKPRLSFADR ALINSMDQNM FSNFSFINPG METLICS
