HSP83_DROME
ID HSP83_DROME Reviewed; 717 AA.
AC P02828; P92174; P92202; Q9VZT3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Heat shock protein 83;
DE AltName: Full=HSP 82;
GN Name=Hsp83 {ECO:0000312|FlyBase:FBgn0001233};
GN Synonyms=Hsp82 {ECO:0000312|FlyBase:FBgn0001233},
GN Hsp90 {ECO:0000303|PubMed:23509070, ECO:0000312|FlyBase:FBgn0001233};
GN ORFNames=CG1242 {ECO:0000312|FlyBase:FBgn0001233};
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 [GENOMIC DNA].
RX PubMed=2426456; DOI=10.1016/s0022-2836(86)80001-8;
RA Blackman R.K., Meselson M.;
RT "Interspecific nucleotide sequence comparisons used to identify regulatory
RT and structural features of the Drosophila hsp82 gene.";
RL J. Mol. Biol. 188:499-515(1986).
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.
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].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 1-375.
RX PubMed=6314271; DOI=10.1093/nar/11.20.7011;
RA Hackett R.W., Lis J.T.;
RT "Localization of the hsp83 transcript within a 3292 nucleotide sequence
RT from the 63B heat shock locus of D. melanogaster.";
RL Nucleic Acids Res. 11:7011-7030(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-371.
RC STRAIN=178.7, 709.6, DPF-13, DPF-2, DPF-30, DPF-46, DPF-62, DPF-77,
RC DPF-82.1, EM-10, MA-10.2, MA-4.2, MA-4.4, VC-805, and VC-815;
RX PubMed=8978045; DOI=10.1093/genetics/144.4.1565;
RA Hasson E., Eanes W.F.;
RT "Contrasting histories of three gene regions associated with In(3L)Payne of
RT Drosophila melanogaster.";
RL Genetics 144:1565-1575(1996).
RN [7]
RP INTERACTION WITH DPIT47 AND HSP70AA.
RX PubMed=11493638; DOI=10.1242/jcs.114.11.2015;
RA Crevel G., Bates H., Huikeshoven H., Cotterill S.;
RT "The Drosophila Dpit47 protein is a nuclear Hsp90 co-chaperone that
RT interacts with DNA polymerase alpha.";
RL J. Cell Sci. 114:2015-2025(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-294, AND IDENTIFICATION BY
RP 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).
RN [10]
RP FUNCTION, AND INTERACTION WITH HOP AND PIWI.
RX PubMed=21186352; DOI=10.1038/ng.743;
RA Gangaraju V.K., Yin H., Weiner M.M., Wang J., Huang X.A., Lin H.;
RT "Drosophila Piwi functions in Hsp90-mediated suppression of phenotypic
RT variation.";
RL Nat. Genet. 43:153-158(2011).
RN [11]
RP FUNCTION, AND INTERACTION WITH SHU.
RX PubMed=22902557; DOI=10.1016/j.molcel.2012.07.021;
RA Olivieri D., Senti K.A., Subramanian S., Sachidanandam R., Brennecke J.;
RT "The cochaperone shutdown defines a group of biogenesis factors essential
RT for all piRNA populations in Drosophila.";
RL Mol. Cell 47:954-969(2012).
RN [12]
RP IDENTIFICATION IN A COMPLEX WITH SICILY AND ND-42, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23509070; DOI=10.1083/jcb.201208033;
RA Zhang K., Li Z., Jaiswal M., Bayat V., Xiong B., Sandoval H., Charng W.L.,
RA David G., Haueter C., Yamamoto S., Graham B.H., Bellen H.J.;
RT "The C8ORF38 homologue Sicily is a cytosolic chaperone for a mitochondrial
RT complex I subunit.";
RL J. Cell Biol. 200:807-820(2013).
RN [13]
RP INTERACTION WITH NUP358.
RX PubMed=27979731; DOI=10.1016/j.ibmb.2016.12.005;
RA He Q., Zhang Y., Zhang X., Xu D., Dong W., Li S., Wu R.;
RT "Nucleoporin Nup358 facilitates nuclear import of Methoprene-tolerant (Met)
RT in an importin beta- and Hsp83-dependent manner.";
RL Insect Biochem. Mol. Biol. 81:10-18(2017).
RN [14]
RP INTERACTION WITH MORA.
RX PubMed=31907206; DOI=10.1242/jcs.236786;
RA Palumbo V., Tariq A., Borgal L., Metz J., Brancaccio M., Gatti M.,
RA Wakefield J.G., Bonaccorsi S.;
RT "Drosophila Morgana is an Hsp90-interacting protein with a direct role in
RT microtubule polymerisation.";
RL J. Cell Sci. 133:0-0(2020).
CC -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC for instance in cell cycle control and signal transduction. Undergoes a
CC functional cycle that is linked to its ATPase activity. This cycle
CC probably induces conformational changes in the client proteins, thereby
CC causing their activation. Interacts dynamically with various co-
CC chaperones that modulate its substrate recognition, ATPase cycle and
CC chaperone function. Together with Hop and piwi, mediates canalization,
CC also known as developmental robustness, likely via epigenetic silencing
CC of existing genetic variants and suppression of transposon-induced new
CC genetic variation. Required for piRNA biogenesis by facilitating
CC loading of piRNAs into PIWI proteins. {ECO:0000269|PubMed:21186352,
CC ECO:0000269|PubMed:22902557}.
CC -!- SUBUNIT: Homodimer (By similarity). Forms a complex with Hop and piwi;
CC probably Hop mediates the interaction between piwi and Hsp83
CC (PubMed:21186352). Forms a complex including sicily, ND-42 and Hsp83;
CC the complex is necessary to chaperone ND-42 in the cytoplasm before
CC mitochondrial import; the interaction with sicily is direct and is
CC dependent on its ATPase activity (PubMed:23509070). Interacts with shu
CC (PubMed:22902557). Interacts with Nup358 (via TPR repeats); the
CC interaction is required for the nuclear import of the sesquiterpenoid
CC juvenile hormone receptor Met (PubMed:27979731). Forms a complex with
CC Dpit47 and Hsp70aa (PubMed:11493638). Interacts with mora
CC (PubMed:31907206). {ECO:0000250|UniProtKB:P07900,
CC ECO:0000269|PubMed:11493638, ECO:0000269|PubMed:21186352,
CC ECO:0000269|PubMed:22902557, ECO:0000269|PubMed:23509070,
CC ECO:0000269|PubMed:27979731, ECO:0000269|PubMed:31907206}.
CC -!- INTERACTION:
CC P02828; P92204: Nelf-E; NbExp=2; IntAct=EBI-136814, EBI-194490;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: In contrast to other major heat shock proteins, this one is
CC also expressed at normal growth temperatures. It is also
CC developmentally expressed during oogenesis.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown is lethal at third instar
CC larva stage and shows decreased levels of sicily, ND-42, and ND-30.
CC {ECO:0000269|PubMed:23509070}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; X03810; CAA27435.1; -; Genomic_DNA.
DR EMBL; X00065; CAA24938.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47734.1; -; Genomic_DNA.
DR EMBL; AY122080; AAM52592.1; -; mRNA.
DR EMBL; U57459; AAB46677.1; -; Genomic_DNA.
DR EMBL; U57460; AAB46678.1; -; Genomic_DNA.
DR EMBL; U57461; AAB46679.1; -; Genomic_DNA.
DR EMBL; U57462; AAB46680.1; -; Genomic_DNA.
DR EMBL; U57463; AAB46681.1; -; Genomic_DNA.
DR EMBL; U57464; AAB46682.1; -; Genomic_DNA.
DR EMBL; U57465; AAB46683.1; -; Genomic_DNA.
DR EMBL; U57466; AAB46684.1; -; Genomic_DNA.
DR EMBL; U57467; AAB46685.1; -; Genomic_DNA.
DR EMBL; U57468; AAB46686.1; -; Genomic_DNA.
DR EMBL; U57469; AAB46687.1; -; Genomic_DNA.
DR EMBL; U57470; AAB46688.1; -; Genomic_DNA.
DR EMBL; U57471; AAB46689.1; -; Genomic_DNA.
DR EMBL; U57472; AAB46690.1; -; Genomic_DNA.
DR EMBL; U57473; AAB46691.1; -; Genomic_DNA.
DR PIR; A24827; HHFF83.
DR RefSeq; NP_001261362.1; NM_001274433.1.
DR RefSeq; NP_523899.1; NM_079175.4.
DR AlphaFoldDB; P02828; -.
DR SMR; P02828; -.
DR BioGRID; 63886; 88.
DR DIP; DIP-17366N; -.
DR IntAct; P02828; 5.
DR MINT; P02828; -.
DR STRING; 7227.FBpp0305095; -.
DR iPTMnet; P02828; -.
DR PaxDb; P02828; -.
DR PRIDE; P02828; -.
DR DNASU; 38389; -.
DR EnsemblMetazoa; FBtr0073040; FBpp0072904; FBgn0001233.
DR EnsemblMetazoa; FBtr0332873; FBpp0305095; FBgn0001233.
DR GeneID; 38389; -.
DR KEGG; dme:Dmel_CG1242; -.
DR CTD; 38389; -.
DR FlyBase; FBgn0001233; Hsp83.
DR VEuPathDB; VectorBase:FBgn0001233; -.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P02828; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; P02828; -.
DR Reactome; R-DME-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DME-203615; eNOS activation.
DR Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DME-3371511; HSF1 activation.
DR Reactome; R-DME-3371568; Attenuation phase.
DR Reactome; R-DME-3371571; HSF1-dependent transactivation.
DR Reactome; R-DME-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-DME-8937144; Aryl hydrocarbon receptor signalling.
DR Reactome; R-DME-8939211; ESR-mediated signaling.
DR Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DME-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR Reactome; R-DME-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR SignaLink; P02828; -.
DR BioGRID-ORCS; 38389; 2 hits in 3 CRISPR screens.
DR ChiTaRS; Hsp83; fly.
DR GenomeRNAi; 38389; -.
DR PRO; PR:P02828; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0001233; Expressed in wing disc and 66 other tissues.
DR ExpressionAtlas; P02828; baseline and differential.
DR Genevisible; P02828; DM.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0101031; C:chaperone complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IPI:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0005705; C:polytene chromosome interband; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:FlyBase.
DR GO; GO:0097718; F:disordered domain specific binding; IBA:GO_Central.
DR GO; GO:0005158; F:insulin receptor binding; IDA:FlyBase.
DR GO; GO:0030911; F:TPR domain binding; IPI:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IDA:FlyBase.
DR GO; GO:0034605; P:cellular response to heat; ISS:FlyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0009631; P:cold acclimation; IEP:FlyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IGI:FlyBase.
DR GO; GO:0019094; P:pole plasm mRNA localization; IMP:FlyBase.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0043248; P:proteasome assembly; IDA:FlyBase.
DR GO; GO:0006457; P:protein folding; ISS:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR GO; GO:0009408; P:response to heat; IEP:FlyBase.
DR GO; GO:0070922; P:RISC complex assembly; IGI:FlyBase.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..717
FT /note="Heat shock protein 83"
FT /id="PRO_0000062930"
FT REGION 213..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 713..717
FT /note="TPR repeat-binding"
FT COMPBIAS 213..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 294
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 234
FT /note="Missing (in strain: MA-10.2, DPF-13, DPF-82.1, EM-
FT 10, 178.7, 709.6 and MA-4.4)"
FT VARIANT 368
FT /note="N -> K (in strain: DPF-2, DPF-30, DPF-62, MA-10.2,
FT DPF-82.1, 178.7, DPF-13, MA-4.4, EM-10, VC-805, MA-4.2,
FT DPF-46, DPF-77, VC-815 and 709.6)"
SQ SEQUENCE 717 AA; 81865 MW; A71B96B2FE1684E6 CRC64;
MPEEAETFAF QAEIAQLMSL IINTFYSNKE IFLRELISNA SDALDKIRYE SLTDPSKLDS
GKELYIKLIP NKTAGTLTII DTGIGMTKSD LVNNLGTIAK SGTKAFMEAL QAGADISMIG
QFGVGFYSAY LVADKVTVTS KNNDDEQYVW ESSAGGSFTV RADNSEPLGR GTKIVLYIKE
DQTDYLEESK IKEIVNKHSQ FIGYPIKLLV EKEREKEVSD DEADDEKKEG DEKKEMETDE
PKIEDVGEDE DADKKDKDAK KKKTIKEKYT EDEELNKTKP IWTRNPDDIS QEEYGEFYKS
LTNDWEDHLA VKHFSVEGQL EFRALLFIPR RTPFDLFENQ KKRNNIKLYV RRVFIMDNCE
DLIPEYLNFM KGVVDSEDLP LNISREMLQQ NKVLKVIRKN LVKKTMELIE ELTEDKENYK
KFYDQFSKNL KLGVHEDSNN RAKLADFLRF HTSASGDDFC SLADYVSRMK DNQKHVYFIT
GESKDQVSNS AFVERVKARG FEVVYMTEPI DEYVIQHLKE YKGKQLVSVT KEGLELPEDE
SEKKKREEDK AKFESLCKLM KSILDNKVEK VVVSNRLVDS PCCIVTSQFG WSANMERIMK
AQALRDTATM GYMAGKKQLE INPDHPIVET LRQKADADKN DKAVKDLVIL LFETSLLSSG
FSLDSPQVHA SRIYRMIKLG LGIDEDEPMT TDDAQSAGDA PSLVEDTEDA SHMEEVD
