EAS_DROME
ID EAS_DROME Reviewed; 518 AA.
AC P54352; C8VV66; M9NEJ9; M9NGH8; Q1RL01; Q540Y9; Q86B51; Q8IR20; Q9VXI7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ethanolamine kinase;
DE Short=EK;
DE EC=2.7.1.82 {ECO:0000269|PubMed:7923374};
DE AltName: Full=Protein easily shocked;
GN Name=eas; ORFNames=CG3525;
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] (ISOFORMS A AND E), FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=7923374; DOI=10.1016/0092-8674(94)90397-2;
RA Pavlidis P., Ramaswami M., Tanouye M.A.;
RT "The Drosophila easily shocked gene: a mutation in a phospholipid synthetic
RT pathway causes seizure, neuronal failure, and paralysis.";
RL Cell 79:23-33(1994).
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] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
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 [LARGE SCALE MRNA] OF 22-518 (ISOFORM E).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Booth B., Carlson J.W., Chavez C., Frise E., George R.A.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190 AND SER-194, 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: Highly specific for ethanolamine phosphorylation. May be a
CC rate-controlling step in phosphatidylethanolamine biosynthesis.
CC {ECO:0000269|PubMed:7923374}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine;
CC Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216;
CC EC=2.7.1.82; Evidence={ECO:0000269|PubMed:7923374};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070;
CC Evidence={ECO:0000269|PubMed:7923374};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC {ECO:0000269|PubMed:7923374}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=E;
CC IsoId=P54352-1; Sequence=Displayed;
CC Name=A; Synonyms=B, C, H, I;
CC IsoId=P54352-2; Sequence=VSP_001068;
CC Name=G;
CC IsoId=P54352-4; Sequence=VSP_053946, VSP_053947, VSP_053948;
CC Name=F;
CC IsoId=P54352-5; Sequence=VSP_053947, VSP_053948;
CC -!- DISRUPTION PHENOTYPE: 'Bang sensitive' phenotype; induction of
CC paralysis with electrical stimulation results in a brief seizure,
CC followed by a failure of the muscles to respond to giant fiber
CC stimulation. This is due to an excitability defect caused by altered
CC membrane phospholipid composition. {ECO:0000269|PubMed:7923374}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABE73230.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ABE73230.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=ACV91649.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L35603; AAC37209.1; -; mRNA.
DR EMBL; L35604; AAC37210.1; -; mRNA.
DR EMBL; AE014298; AAF48574.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48575.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09387.1; -; Genomic_DNA.
DR EMBL; AE014298; AAO41661.2; -; Genomic_DNA.
DR EMBL; AE014298; AFH07419.1; -; Genomic_DNA.
DR EMBL; AE014298; AFH07420.1; -; Genomic_DNA.
DR EMBL; AY118437; AAM48466.1; -; mRNA.
DR EMBL; BT025059; ABE73230.1; ALT_SEQ; mRNA.
DR EMBL; BT099812; ACV91649.1; ALT_FRAME; mRNA.
DR PIR; A54980; A54980.
DR RefSeq; NP_001245706.1; NM_001258777.1. [P54352-5]
DR RefSeq; NP_001245707.1; NM_001258778.2. [P54352-4]
DR RefSeq; NP_001285319.1; NM_001298390.1. [P54352-5]
DR RefSeq; NP_523364.2; NM_078640.4. [P54352-2]
DR RefSeq; NP_727941.2; NM_167489.2. [P54352-2]
DR RefSeq; NP_727942.1; NM_167490.3. [P54352-2]
DR RefSeq; NP_727943.1; NM_167491.2. [P54352-2]
DR RefSeq; NP_788914.2; NM_176741.3. [P54352-2]
DR AlphaFoldDB; P54352; -.
DR SMR; P54352; -.
DR BioGRID; 58926; 23.
DR IntAct; P54352; 2.
DR STRING; 7227.FBpp0073990; -.
DR iPTMnet; P54352; -.
DR PaxDb; P54352; -.
DR PRIDE; P54352; -.
DR DNASU; 32585; -.
DR EnsemblMetazoa; FBtr0074211; FBpp0073990; FBgn0000536. [P54352-2]
DR EnsemblMetazoa; FBtr0074212; FBpp0073991; FBgn0000536. [P54352-2]
DR EnsemblMetazoa; FBtr0074214; FBpp0073993; FBgn0000536. [P54352-2]
DR EnsemblMetazoa; FBtr0308617; FBpp0300841; FBgn0000536. [P54352-5]
DR EnsemblMetazoa; FBtr0308618; FBpp0300842; FBgn0000536. [P54352-4]
DR EnsemblMetazoa; FBtr0308619; FBpp0300843; FBgn0000536. [P54352-2]
DR EnsemblMetazoa; FBtr0343519; FBpp0310123; FBgn0000536. [P54352-2]
DR EnsemblMetazoa; FBtr0343520; FBpp0310124; FBgn0000536. [P54352-5]
DR GeneID; 32585; -.
DR KEGG; dme:Dmel_CG3525; -.
DR UCSC; CG3525-RB; d. melanogaster.
DR UCSC; CG3525-RD; d. melanogaster.
DR UCSC; CG3525-RE; d. melanogaster.
DR CTD; 32585; -.
DR FlyBase; FBgn0000536; eas.
DR VEuPathDB; VectorBase:FBgn0000536; -.
DR eggNOG; KOG4720; Eukaryota.
DR GeneTree; ENSGT00950000182939; -.
DR InParanoid; P54352; -.
DR OMA; FKMKPEA; -.
DR PhylomeDB; P54352; -.
DR Reactome; R-DME-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00741.
DR BioGRID-ORCS; 32585; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32585; -.
DR PRO; PR:P54352; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000536; Expressed in oviduct (Drosophila) and 25 other tissues.
DR ExpressionAtlas; P54352; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004103; F:choline kinase activity; TAS:FlyBase.
DR GO; GO:0004305; F:ethanolamine kinase activity; IDA:FlyBase.
DR GO; GO:0008306; P:associative learning; TAS:FlyBase.
DR GO; GO:0055059; P:asymmetric neuroblast division; IMP:FlyBase.
DR GO; GO:0007420; P:brain development; IMP:FlyBase.
DR GO; GO:0046959; P:habituation; TAS:FlyBase.
DR GO; GO:0007616; P:long-term memory; TAS:FlyBase.
DR GO; GO:0007638; P:mechanosensory behavior; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; IDA:FlyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0001666; P:response to hypoxia; IDA:FlyBase.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:FlyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..518
FT /note="Ethanolamine kinase"
FT /id="PRO_0000206231"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 2..30
FT /note="GTETKSNSYTGQISTSGGNPKVMKDSLSL -> STIRSKKN (in
FT isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_053946"
FT VAR_SEQ 130..152
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:7923374"
FT /id="VSP_001068"
FT VAR_SEQ 152..171
FT /note="YSFTDGITNKLVGCFHKEIS -> VLPMASQTNWSDVFIRRSPN (in
FT isoform F and isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_053947"
FT VAR_SEQ 172..518
FT /note="Missing (in isoform F and isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_053948"
FT CONFLICT 140..152
FT /note="YPAQNAMVMMTLY -> VSGPKCDGDDDA (in Ref. 1; AAC37209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 59563 MW; 90768FF07A119436 CRC64;
MGTETKSNSY TGQISTSGGN PKVMKDSLSL VRQTVNQQTL SLSQSNQVQN QLNSHSNSNS
YPNPSGSENK NENEQNSRDI RAKPEDKSRK EAIVPFVPIF VEEADVIQGA KELLKVIRPT
WDLSHVEFKI RVVPQIEDRY PAQNAMVMMT LYSFTDGITN KLVGCFHKEI SKLNDENGGS
YLPIKTQGLS PVQSEDPVII EKEDDDEFTD DRAADDGSPV QYSDNVVLVR IYGNKTDLLI
DRKAETQNFL LLHTYGLAPS LYATFKNGLV YEYVPGTTLN TDSVLCPEIW PLVARRMAEM
HRKVRKHGDS SATKPMPMIW KKTQSFLDLV PERFSDAEKH KRVKETFLPI GRLREEFNKL
YEYLEALDSP IVFSHNDLLL GNVIYTQSLN TVNFIDYEYA DYNFQAFDIG NHFAEMCGVD
EVDYSRYPKR EFQLQWLRVY LEEYLQRSNI QNDEVELLYV QVNQFALASH IFWTVWSLLQ
AEHSTIDFDY VGYAFLRYNE YLARKVEFLS LTAAKNNK
