PDPK1_DROME
ID PDPK1_DROME Reviewed; 836 AA.
AC Q9W0V1; O62534; Q0E8K9; Q53XF5; Q7KVE1; Q8IHG6; Q9W0V2; Q9W0V3;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 4.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=3-phosphoinositide-dependent protein kinase 1;
DE Short=dPDK-1;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase 61C;
DE AltName: Full=dSTPK61;
GN Name=Pdk1; Synonyms=Pk61C; ORFNames=CG1210;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RX PubMed=10336630; DOI=10.1046/j.1432-1327.1999.00404.x;
RA MacDougall C.N., Clyde D., Wood T., Todman M., Harbison D., Bownes M.;
RT "Sex-specific transcripts of the Dstpk61 serine/threonine kinase gene in
RT Drosophila melanogaster.";
RL Eur. J. Biochem. 262:456-466(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=Berkeley; TISSUE=Embryo, and Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=9368760; DOI=10.1016/s0960-9822(06)00336-8;
RA Alessi D.R., Deak M., Casamayor A., Caudwell F.B., Morrice N.A.,
RA Norman D.G., Gaffney P.R.J., Reese C.B., MacDougall C.N., Harbison D.,
RA Ashworth A., Bownes M.;
RT "3-phosphoinositide-dependent protein kinase-1 (PDK1): structural and
RT functional homology with the Drosophila DSTPK61 kinase.";
RL Curr. Biol. 7:776-789(1997).
RN [6]
RP ALTERNATIVE SPLICING.
RX PubMed=11115766; DOI=10.1677/joe.0.1670391;
RA Clyde D., Bownes M.;
RT "The Dstpk61 locus of Drosophila produces multiple transcripts and protein
RT isoforms, suggesting it is involved in multiple signalling pathways.";
RL J. Endocrinol. 167:391-401(2000).
RN [7]
RP FUNCTION IN SYNAPTOGENESIS, AND DEVELOPMENTAL STAGE.
RX PubMed=11301252; DOI=10.1016/s0960-9822(01)00124-5;
RA Kraut R., Menon K., Zinn K.;
RT "A gain-of-function screen for genes controlling motor axon guidance and
RT synaptogenesis in Drosophila.";
RL Curr. Biol. 11:417-430(2001).
RN [8]
RP FUNCTION.
RX PubMed=11344272; DOI=10.1073/pnas.101596998;
RA Cho K.S., Lee J.H., Kim S., Kim D., Koh H., Lee J., Kim C., Kim J.,
RA Chung J.;
RT "Drosophila phosphoinositide-dependent kinase-1 regulates apoptosis and
RT growth via the phosphoinositide 3-kinase-dependent signaling pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6144-6149(2001).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11752451; DOI=10.1073/pnas.011318098;
RA Rintelen F., Stocker H., Thomas G., Hafen E.;
RT "PDK1 regulates growth through Akt and S6K in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:15020-15025(2001).
RN [10]
RP FUNCTION.
RX PubMed=11862217; DOI=10.1038/ncb763;
RA Radimerski T., Montagne J., Rintelen F., Stocker H., van der Kaay J.,
RA Downes C.P., Hafen E., Thomas G.;
RT "dS6K-regulated cell growth is dPKB/dPI(3)K-independent, but requires
RT dPDK1.";
RL Nat. Cell Biol. 4:251-255(2002).
RN [11]
RP FUNCTION IN SPERMATOGENESIS.
RX PubMed=15238523; DOI=10.1534/genetics.103.023184;
RA Schulz C., Kiger A.A., Tazuke S.I., Yamashita Y.M., Pantalena-Filho L.C.,
RA Jones D.L., Wood C.G., Fuller M.T.;
RT "A misexpression screen reveals effects of bag-of-marbles and TGF beta
RT class signaling on the Drosophila male germ-line stem cell lineage.";
RL Genetics 167:707-723(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641; SER-645 AND SER-804, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Serine/threonine kinase required for embryonic development.
CC Inhibits apoptosis. Acts in the insulin receptor transduction pathway
CC which regulates cell growth and organ size, by phosphorylating and
CC activating Akt1 and S6k. May be involved in axonal pathfinding and
CC synaptogenesis, and in spermatogenesis. {ECO:0000269|PubMed:10336630,
CC ECO:0000269|PubMed:11301252, ECO:0000269|PubMed:11344272,
CC ECO:0000269|PubMed:11752451, ECO:0000269|PubMed:11862217,
CC ECO:0000269|PubMed:15238523, ECO:0000269|PubMed:9368760}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4; Synonyms=D;
CC IsoId=Q9W0V1-4; Sequence=Displayed;
CC Name=1; Synonyms=C;
CC IsoId=Q9W0V1-1; Sequence=VSP_017083;
CC Name=2; Synonyms=A, F;
CC IsoId=Q9W0V1-2; Sequence=VSP_004896;
CC Name=3; Synonyms=B, E;
CC IsoId=Q9W0V1-3; Sequence=VSP_004897;
CC -!- DEVELOPMENTAL STAGE: Highly expressed in Malpighian tubule primordia
CC from stage late 11 to 13. Expressed in hindgut at stage 13. After stage
CC 14, ubiquitously expressed at low levels.
CC {ECO:0000269|PubMed:11301252}.
CC -!- DOMAIN: The PIF-pocket is a small lobe in the catalytic domain required
CC by the enzyme for the binding to the hydrophobic motif of its
CC substrates. It is an allosteric regulatory site that can accommodate
CC small compounds acting as allosteric inhibitors.
CC {ECO:0000250|UniProtKB:O15530}.
CC -!- DISRUPTION PHENOTYPE: Death during the second instar stage.
CC {ECO:0000269|PubMed:11752451}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PDPK1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN71019.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA69216.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y07908; CAA69216.1; ALT_INIT; mRNA.
DR EMBL; AE014296; AAF47327.3; -; Genomic_DNA.
DR EMBL; AE014296; AAF47329.2; -; Genomic_DNA.
DR EMBL; AE014296; AAF47330.3; -; Genomic_DNA.
DR EMBL; AE014296; AAF47332.1; -; Genomic_DNA.
DR EMBL; BT004489; AAO42653.1; -; mRNA.
DR EMBL; BT001263; AAN71019.1; ALT_FRAME; mRNA.
DR EMBL; BT011471; AAR99129.1; -; mRNA.
DR RefSeq; NP_001261183.1; NM_001274254.1. [Q9W0V1-4]
DR RefSeq; NP_525121.2; NM_080382.4. [Q9W0V1-2]
DR RefSeq; NP_728470.1; NM_167789.2. [Q9W0V1-1]
DR RefSeq; NP_728471.2; NM_167790.3. [Q9W0V1-4]
DR RefSeq; NP_728472.1; NM_167791.3. [Q9W0V1-2]
DR RefSeq; NP_728473.1; NM_167792.3. [Q9W0V1-2]
DR RefSeq; NP_728474.1; NM_167793.3. [Q9W0V1-3]
DR RefSeq; NP_728475.1; NM_167794.3. [Q9W0V1-3]
DR RefSeq; NP_728476.1; NM_167795.3. [Q9W0V1-3]
DR AlphaFoldDB; Q9W0V1; -.
DR SMR; Q9W0V1; -.
DR BioGRID; 63582; 126.
DR DIP; DIP-20399N; -.
DR IntAct; Q9W0V1; 3.
DR STRING; 7227.FBpp0305420; -.
DR iPTMnet; Q9W0V1; -.
DR PaxDb; Q9W0V1; -.
DR DNASU; 38017; -.
DR EnsemblMetazoa; FBtr0072464; FBpp0072366; FBgn0020386. [Q9W0V1-4]
DR EnsemblMetazoa; FBtr0072465; FBpp0072367; FBgn0020386. [Q9W0V1-2]
DR EnsemblMetazoa; FBtr0072466; FBpp0072368; FBgn0020386. [Q9W0V1-2]
DR EnsemblMetazoa; FBtr0072467; FBpp0072369; FBgn0020386. [Q9W0V1-2]
DR EnsemblMetazoa; FBtr0072468; FBpp0072370; FBgn0020386. [Q9W0V1-1]
DR EnsemblMetazoa; FBtr0072469; FBpp0072371; FBgn0020386. [Q9W0V1-3]
DR EnsemblMetazoa; FBtr0072470; FBpp0072372; FBgn0020386. [Q9W0V1-3]
DR EnsemblMetazoa; FBtr0072471; FBpp0072373; FBgn0020386. [Q9W0V1-3]
DR EnsemblMetazoa; FBtr0333218; FBpp0305420; FBgn0020386. [Q9W0V1-4]
DR GeneID; 38017; -.
DR KEGG; dme:Dmel_CG1210; -.
DR CTD; 5163; -.
DR FlyBase; FBgn0020386; Pdk1.
DR VEuPathDB; VectorBase:FBgn0020386; -.
DR eggNOG; KOG0592; Eukaryota.
DR GeneTree; ENSGT00940000155267; -.
DR InParanoid; Q9W0V1; -.
DR OMA; GHTENNN; -.
DR PhylomeDB; Q9W0V1; -.
DR BRENDA; 2.7.11.1; 1994.
DR Reactome; R-DME-110478; Insulin signaling pathway.
DR Reactome; R-DME-110523; TOR signaling pathway.
DR Reactome; R-DME-114604; GPVI-mediated activation cascade.
DR Reactome; R-DME-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DME-165158; Activation of AKT2.
DR Reactome; R-DME-202424; Downstream TCR signaling.
DR Reactome; R-DME-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-DME-354192; Integrin signaling.
DR Reactome; R-DME-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-DME-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DME-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-DME-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DME-9634635; Estrogen-stimulated signaling through PRKCZ.
DR SignaLink; Q9W0V1; -.
DR BioGRID-ORCS; 38017; 3 hits in 3 CRISPR screens.
DR ChiTaRS; Pdk1; fly.
DR GenomeRNAi; 38017; -.
DR PRO; PR:Q9W0V1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0020386; Expressed in spermathecum and 36 other tissues.
DR ExpressionAtlas; Q9W0V1; baseline and differential.
DR Genevisible; Q9W0V1; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004676; F:3-phosphoinositide-dependent protein kinase activity; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:FlyBase.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:FlyBase.
DR GO; GO:0045793; P:positive regulation of cell size; IGI:FlyBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:FlyBase.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR CDD; cd01262; PH_PDK1; 1.
DR CDD; cd05581; STKc_PDK1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033931; PDK1-typ_PH.
DR InterPro; IPR039046; PDPK1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF14593; PH_3; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; ATP-binding; Cytoplasm;
KW Developmental protein; Differentiation; Growth regulation; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Spermatogenesis; Transferase.
FT CHAIN 1..836
FT /note="3-phosphoinositide-dependent protein kinase 1"
FT /id="PRO_0000086504"
FT DOMAIN 246..571
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 206..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..322
FT /note="PIF-pocket"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT REGION 401..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 256..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 325..327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT MOD_RES 641
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..297
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_004897"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10336630, ECO:0000303|Ref.4"
FT /id="VSP_004896"
FT VAR_SEQ 1..22
FT /note="MKCKSWSNKINNYVVRKIKSIK -> MNIIQ (in isoform 1)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_017083"
FT CONFLICT 200..201
FT /note="QQ -> HE (in Ref. 1; CAA69216)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="G -> R (in Ref. 1; CAA69216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 836 AA; 94079 MW; CA274D2265D17AE2 CRC64;
MKCKSWSNKI NNYVVRKIKS IKINGTQQQL QLPGSGASGI AAAAVITVAS DCGENCSSNG
TEHQQHFNIA TTTATSATEA TMPAMAKEKA SATVSLGESN FRDINLKDLA VVVEAASRLH
HQQNVCGCGA VSSTENNNNS RYGSSKYLTN GHTSPLAAAV ASNSSSVATT PHCRMLHNCS
LQQYQNDIRQ QTEILDMLRQ QHQQGYQSQQ QQQQPQQQQE QQQQQEQSQQ QQQLQNPAPR
RSPNDFIFGR YIGEGSYSIV YLAVDIHSRR EYAIKVCEKR LILRERKQDY IKREREVMHQ
MTNVPGFVNL SCTFQDQRSL YFVMTYARKG DMLPYINRVG SFDVACTRHY AAELLLACEH
MHRRNVVHRD LKPENILLDE DMHTLIADFG SAKVMTAHER ALATEHCSEQ RRSNSDEDDE
DSDRLENEDE DFYDRDSEEL DDGDDEQQQE EMDSPRHRQR RYNRHRKASF VGTAQYVSPE
VLQNGPITPA ADLWALGCIV YQMIAGLPPF RGSNDYVIFK EILDCAVDFP QGFDKDAEDL
VRKLLRVDPR DRLGAQDEFG YYESIRAHPF FAGIDWQTLR QQTPPPIYPY LPGVSQDEDF
RSSYTVPGDL EPGLDERQIS RLLSAELGVG SSVAMPVKRS TAKNSFDLND AEKLQRLEQQ
KTDKWHVFAD GEVILKKGFV NKRKGLFARK RMLLLTTGPR LIYIDPVQMI KKGEIPWSPD
LRAEYKNFKI FFVHTPNRTY YLDDPEGYAI HWSEAIENMR KLAYGDPSST SAVSCSSGSS
NSLAVISNSS AASSSNSPTV KRSSPVNAPQ ASTASDNRTL GSTRTGTSPS KKTASK
