ATNA_DROME
ID ATNA_DROME Reviewed; 1041 AA.
AC P13607; A4V366; A4V367; O61494; Q0KI37; Q7KS94; Q7KS95; Q86MY6; Q86MY7;
AC Q86MY8; Q86MY9; Q86MZ0; Q8IN40; Q8T0L8; Q9VDG6; Q9VDG7; Q9VDG8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 3.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha;
DE Short=Na(+)/K(+) ATPase alpha subunit;
DE EC=7.2.2.13 {ECO:0000305|PubMed:9648860};
DE AltName: Full=Sodium pump subunit alpha;
GN Name=Atpalpha; Synonyms=Na-p; ORFNames=CG5670;
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 1), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo, Head, and Pupae;
RX PubMed=2540956; DOI=10.1002/j.1460-2075.1989.tb03364.x;
RA Lebovitz R.M., Takeyasu K., Fambrough D.M.;
RT "Molecular characterization and expression of the (Na+ + K+)-ATPase alpha-
RT subunit in Drosophila melanogaster.";
RL EMBO J. 8:193-202(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Head;
RX PubMed=9648860; DOI=10.1046/j.1471-4159.1998.71010142.x;
RA Sun B., Wang W., Salvaterra P.M.;
RT "Functional analysis and tissue-specific expression of Drosophila Na+,K+-
RT ATPase subunits.";
RL J. Neurochem. 71:142-151(1998).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND RNA EDITING OF
RP POSITION 429.
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35 (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 835-865 (ISOFORMS 1; 5; 6 AND 7), FUNCTION, AND
RP MUTAGENESIS OF ASP-1020 AND GLU-1021.
RX PubMed=12598616; DOI=10.1523/jneurosci.23-04-01276.2003;
RA Palladino M.J., Bower J.E., Kreber R., Ganetzky B.;
RT "Neural dysfunction and neurodegeneration in Drosophila Na+/K+ ATPase alpha
RT subunit mutants.";
RL J. Neurosci. 23:1276-1286(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RX PubMed=9680312; DOI=10.1046/j.1365-4624.1997.00006.x;
RA Feng Y., Huynh L., Takeyasu K., Fambrough D.M.;
RT "The Drosophila Na,K-ATPase alpha-subunit gene: gene structure, promoter
RT function and analysis of a cold-sensitive recessive-lethal mutation.";
RL Genes Funct. 1:99-117(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 400-524.
RX PubMed=2557235; DOI=10.1016/0014-5793(89)81653-9;
RA Varadi A., Gilmore-Heber M., Benz E.J. Jr.;
RT "Amplification of the phosphorylation site-ATP-binding site cDNA fragment
RT of the Na+,K(+)-ATPase and the Ca2(+)-ATPase of Drosophila melanogaster by
RT polymerase chain reaction.";
RL FEBS Lett. 258:203-207(1989).
RN [9]
RP RNA EDITING OF POSITION 429.
RX PubMed=17018572; DOI=10.1261/rna.254306;
RA Stapleton M., Carlson J.W., Celniker S.E.;
RT "RNA editing in Drosophila melanogaster: new targets and functional
RT consequences.";
RL RNA 12:1922-1932(2006).
CC -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC potassium ions across the plasma membrane. This action creates the
CC electrochemical gradient of sodium and potassium ions, providing the
CC energy for active transport of various nutrients.
CC {ECO:0000269|PubMed:12598616, ECO:0000269|PubMed:2540956,
CC ECO:0000269|PubMed:9648860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
CC Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC EC=7.2.2.13; Evidence={ECO:0000305|PubMed:9648860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18354;
CC Evidence={ECO:0000305|PubMed:9648860};
CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Exon 6 has 4 mutually exclusive forms (6a, 6b, 6c and 6d).
CC Additional isoforms may exist.;
CC Name=1; Synonyms=A;
CC IsoId=P13607-1; Sequence=Displayed;
CC Name=2; Synonyms=B, C, E;
CC IsoId=P13607-2; Sequence=VSP_000417;
CC Name=3; Synonyms=D;
CC IsoId=P13607-3; Sequence=VSP_000417, VSP_008077, VSP_008078;
CC Name=4;
CC IsoId=P13607-4; Sequence=VSP_008074;
CC Name=5;
CC IsoId=P13607-5; Sequence=VSP_008075;
CC Name=6; Synonyms=F, H;
CC IsoId=P13607-6; Sequence=VSP_000417, VSP_000418;
CC Name=7; Synonyms=G;
CC IsoId=P13607-7; Sequence=VSP_000417, VSP_008076;
CC -!- TISSUE SPECIFICITY: High levels are found in some adult tissues:
CC Malpighian tubules, indirect flight muscles, tubular leg muscles and
CC throughout the nervous system (brain, optic lobes, retina and ventral
CC thoracic neuromere). Lower levels are detected at the posterior end
CC where the reproductive organs and rectum are located.
CC {ECO:0000269|PubMed:2540956, ECO:0000269|PubMed:9648860}.
CC -!- RNA EDITING: Modified_positions=429 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}; Note=Partially edited. Target of Adar.;
CC -!- MISCELLANEOUS: Ouabain-sensitive electrogenic ion pump.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
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DR EMBL; X14476; CAA32638.1; -; mRNA.
DR EMBL; AF044974; AAC05260.1; -; mRNA.
DR EMBL; AE014297; AAF55825.3; -; Genomic_DNA.
DR EMBL; AE014297; AAF55826.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF55828.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65183.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65184.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65185.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65186.1; -; Genomic_DNA.
DR EMBL; AY069184; AAL39329.1; -; mRNA.
DR EMBL; AY174097; AAO33930.1; -; Genomic_DNA.
DR EMBL; AY174097; AAO33931.1; -; Genomic_DNA.
DR EMBL; AY174097; AAO33932.1; -; Genomic_DNA.
DR EMBL; AY174097; AAO33933.1; -; Genomic_DNA.
DR EMBL; AY174098; AAO33929.1; -; Genomic_DNA.
DR EMBL; U55767; AAB01189.1; -; Genomic_DNA.
DR EMBL; X17471; CAA35504.1; -; mRNA.
DR PIR; S03632; S03632.
DR RefSeq; NP_001262790.1; NM_001275861.1. [P13607-2]
DR RefSeq; NP_001262791.1; NM_001275862.2. [P13607-2]
DR RefSeq; NP_732572.1; NM_169936.3. [P13607-1]
DR RefSeq; NP_732573.1; NM_169937.3. [P13607-2]
DR RefSeq; NP_732574.1; NM_169938.3. [P13607-2]
DR RefSeq; NP_732575.1; NM_169939.2. [P13607-3]
DR RefSeq; NP_996247.1; NM_206525.3. [P13607-6]
DR RefSeq; NP_996248.1; NM_206526.3. [P13607-7]
DR RefSeq; NP_996249.1; NM_206527.3. [P13607-6]
DR RefSeq; NP_996250.1; NM_206528.3. [P13607-2]
DR AlphaFoldDB; P13607; -.
DR SMR; P13607; -.
DR BioGRID; 71866; 59.
DR DIP; DIP-19649N; -.
DR IntAct; P13607; 36.
DR STRING; 7227.FBpp0088502; -.
DR PaxDb; P13607; -.
DR PRIDE; P13607; -.
DR DNASU; 48971; -.
DR EnsemblMetazoa; FBtr0089509; FBpp0088501; FBgn0002921. [P13607-2]
DR EnsemblMetazoa; FBtr0089510; FBpp0088502; FBgn0002921. [P13607-1]
DR EnsemblMetazoa; FBtr0089511; FBpp0088503; FBgn0002921. [P13607-2]
DR EnsemblMetazoa; FBtr0089512; FBpp0088504; FBgn0002921. [P13607-3]
DR EnsemblMetazoa; FBtr0089513; FBpp0088984; FBgn0002921. [P13607-2]
DR EnsemblMetazoa; FBtr0089514; FBpp0088983; FBgn0002921. [P13607-6]
DR EnsemblMetazoa; FBtr0089515; FBpp0088982; FBgn0002921. [P13607-7]
DR EnsemblMetazoa; FBtr0089516; FBpp0088981; FBgn0002921. [P13607-6]
DR EnsemblMetazoa; FBtr0333324; FBpp0305516; FBgn0002921. [P13607-2]
DR EnsemblMetazoa; FBtr0333325; FBpp0305517; FBgn0002921. [P13607-2]
DR GeneID; 48971; -.
DR KEGG; dme:Dmel_CG5670; -.
DR UCSC; CG5670-RE; d. melanogaster.
DR UCSC; CG5670-RH; d. melanogaster.
DR CTD; 48971; -.
DR FlyBase; FBgn0002921; Atpalpha.
DR VEuPathDB; VectorBase:FBgn0002921; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; P13607; -.
DR OMA; CYIAYSV; -.
DR PhylomeDB; P13607; -.
DR Reactome; R-DME-936837; Ion transport by P-type ATPases.
DR SignaLink; P13607; -.
DR BioGRID-ORCS; 48971; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Atpalpha; fly.
DR GenomeRNAi; 48971; -.
DR PRO; PR:P13607; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002921; Expressed in adult Malpighian tubule (Drosophila) and 24 other tissues.
DR ExpressionAtlas; P13607; baseline and differential.
DR Genevisible; P13607; DM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005918; C:septate junction; IDA:FlyBase.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IDA:FlyBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0006812; P:cation transport; IDA:FlyBase.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IDA:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0007630; P:jump response; IMP:FlyBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:FlyBase.
DR GO; GO:0050905; P:neuromuscular process; IMP:FlyBase.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0035158; P:regulation of tube diameter, open tracheal system; IMP:FlyBase.
DR GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:FlyBase.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0001894; P:tissue homeostasis; IMP:FlyBase.
DR GO; GO:0060439; P:trachea morphogenesis; IMP:FlyBase.
DR CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Ion transport; Membrane;
KW Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; RNA editing; Sodium; Sodium transport;
KW Sodium/potassium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1041
FT /note="Sodium/potassium-transporting ATPase subunit alpha"
FT /id="PRO_0000046309"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 808..828
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 870..890
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 935..955
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 970..990
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 394
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 2, isoform 3, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:9648860"
FT /id="VSP_000417"
FT VAR_SEQ 1..8
FT /note="MALRSDYE -> MSAQ (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_008074"
FT VAR_SEQ 835..865
FT /note="VPAISLAYEHAEADIMKRPPRDPFNDKLVNS -> IPAISLAYEGPEADIMK
FT RRPRNPEIDNLVNE (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_008075"
FT VAR_SEQ 835..865
FT /note="VPAISLAYEHAEADIMKRPPRDPFNDKLVNS -> IPAISLAYEQAESDIMK
FT RQPRDPYRDNLVNR (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_008076"
FT VAR_SEQ 836..878
FT /note="PAISLAYEHAEADIMKRPPRDPFNDKLVNSRLISMAYGQIGMI -> SLDLC
FT PKPKLHRRLKLKLLLSQYHSSKLYSYTSCSPSQLIVKN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_008077"
FT VAR_SEQ 844..865
FT /note="HAEADIMKRPPRDPFNDKLVNS -> TAESDIMKRQPRNPFQDKLVNE (in
FT isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_000418"
FT VAR_SEQ 879..1041
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_008078"
FT VARIANT 429
FT /note="Y -> C (in RNA edited version)"
FT MUTAGEN 1020
FT /note="D->N: In allele ATP-alpha-dts2; homozygous lethal
FT and temperature dependent bang sensitive paralysis,
FT shortened life span and neurodegeneration when
FT heterozygous."
FT /evidence="ECO:0000269|PubMed:12598616"
FT MUTAGEN 1021
FT /note="E->K: In allele ATP-alpha-dts1; homozygous lethal
FT and temperature dependent bang sensitive paralysis,
FT shortened life span and neurodegeneration when
FT heterozygous."
FT /evidence="ECO:0000269|PubMed:12598616"
FT CONFLICT 69
FT /note="L -> M (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="K -> R (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="Missing (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..113
FT /note="KN -> ED (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..118
FT /note="GF -> V (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="I -> V (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="E -> G (in Ref. 2; AAC05260)"
FT /evidence="ECO:0000305"
FT CONFLICT 196..197
FT /note="LT -> PS (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 207..208
FT /note="DV -> VL (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 211..212
FT /note="VK -> LE (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..221
FT /note="RIPADI -> LIPLVY (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="N -> D (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 270..272
FT /note="GTA -> ALP (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="G -> A (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="Missing (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="N -> T (in Ref. 8; CAA35504)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="I -> N (in Ref. 8; CAA35504)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="F -> S (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
FT CONFLICT 843
FT /note="E -> D (in Ref. 1; CAA32638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1041 AA; 115605 MW; B2DD36B2E9029F43 CRC64;
MALRSDYEHG RADSYRVATV IATDDDNRTA DGQYKSRRKM PAKVNKKENL DDLKQELDID
FHKISPEELY QRFQTHPENG LSHAKAKENL ERDGPNALTP PKQTPEWVKF CKNLFGGFAM
LLWIGAILCF VAYSIQASTS EEPADDNLYL GIVLSAVVIV TGIFSYYQES KSSKIMESFK
NMVPQFATVI REGEKLTLRA EDLVLGDVVE VKFGDRIPAD IRIIEARNFK VDNSSLTGES
EPQSRGAEFT HENPLETKNL AFFSTNAVEG TAKGVVISCG DHTVMGRIAG LASGLDTGET
PIAKEIHHFI HLITGVAVFL GVTFFVIAFI LGYHWLDAVI FLIGIIVANV PEGLLATVTV
CLTLTAKRMA SKNCLVKNLE AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIIEADT
TEDQSGVQYD RTSPGFKALS RIATLCNRAE FKGGQDGVPI LKKEVSGDAS EAALLKCMEL
ALGDVMNIRK RNKKIAEVPF NSTNKYQVSI HETEDTNDPR YLLVMKGAPE RILERCSTIF
INGKEKVLDE EMKEAFNNAY MELGGLGERV LGFCDFMLPS DKYPNGFKFN TDDINFPIDN
LRFVGLMSMI DPPRAAVPDA VAKCRSAGIK VIMVTGDHPI TAKAIAKSVG IISEGNETVE
DIAQRLNIPV SEVNPREAKA AVVHGAELRD VSSDQLDEIL RYHTEIVFAR TSPQQKLIIV
EGCQRMGAIV AVTGDGVNDS PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV
EEGRLIFDNL KKSIAYTLTS NIPEISPFLA FILCDIPLPL GTVTILCIDL GTDMVPAISL
AYEHAEADIM KRPPRDPFND KLVNSRLISM AYGQIGMIQA AAGFFVYFVI MAENGFLPKK
LFGIRKMWDS KAVNDLTDSY GQEWTYRDRK TLEYTCHTAF FISIVVVQWA DLIICKTRRN
SIFQQGMRNW ALNFGLVFET VLAAFLSYCP GMEKGLRMYP LKLVWWFPAI PFALAIFIYD
ETRRFYLRRN PGGWLEQETY Y
