ATPB1_DROME
ID ATPB1_DROME Reviewed; 309 AA.
AC Q24046; Q8MR34; Q9VM86;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE AltName: Full=Protein nervana 1;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN Name=nrv1; ORFNames=CG9258;
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].
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=7777518; DOI=10.1073/pnas.92.12.5396;
RA Sun B., Salvaterra P.M.;
RT "Two Drosophila nervous system antigens, Nervana 1 and 2, are homologous to
RT the beta subunit of Na+,K(+)-ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5396-5400(1995).
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=Embryo;
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 DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=7540667; DOI=10.1046/j.1471-4159.1995.65010434.x;
RA Sun B., Salvaterra P.M.;
RT "Characterization of nervana, a Drosophila melanogaster neuron-specific
RT glycoprotein antigen recognized by anti-horseradish peroxidase
RT antibodies.";
RL J. Neurochem. 65:434-443(1995).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-133 AND ASN-211, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [8]
RP INTERACTION WITH NKAIN.
RX PubMed=17606467; DOI=10.1093/hmg/ddm167;
RA Gorokhova S., Bibert S., Geering K., Heintz N.;
RT "A novel family of transmembrane proteins interacting with beta subunits of
RT the Na,K-ATPase.";
RL Hum. Mol. Genet. 16:2394-2410(2007).
CC -!- FUNCTION: This is the non-catalytic component of the active enzyme,
CC which catalyzes the hydrolysis of ATP coupled with the exchange of
CC Na(+) and K(+) ions across the plasma membrane. The beta subunit
CC regulates, through assembly of alpha/beta heterodimers, the number of
CC sodium pumps transported to the plasma membrane.
CC {ECO:0000269|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. Interacts with nkain.
CC {ECO:0000269|PubMed:17606467, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In embryos, it is expressed in the neurons of the
CC CNS and PNS, in Garland cells and posterior spiracles. In adults, it is
CC concentrated in the thorax and abdomen (muscle tissue, digestive system
CC and Malpighian tubules) and weakly expressed in the head. Expression is
CC diffuse in the nervous system. {ECO:0000269|PubMed:7540667,
CC ECO:0000269|PubMed:9648860}.
CC -!- DEVELOPMENTAL STAGE: Expression in embryos is first seen 12 hours after
CC oviposition, peaks at 24 hours and decreases to a low level by 48
CC hours. Low levels are seen during larval and early pupal development.
CC Levels increase during late pupae to maximal at the adult stage.
CC {ECO:0000269|PubMed:7540667}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; U22438; AAC46608.1; -; mRNA.
DR EMBL; AE014134; AAF52437.1; -; Genomic_DNA.
DR EMBL; AY122147; AAM52659.1; -; mRNA.
DR RefSeq; NP_001260163.1; NM_001273234.1.
DR RefSeq; NP_477167.1; NM_057819.4.
DR AlphaFoldDB; Q24046; -.
DR SMR; Q24046; -.
DR BioGRID; 60104; 6.
DR DIP; DIP-20098N; -.
DR STRING; 7227.FBpp0079012; -.
DR GlyGen; Q24046; 2 sites.
DR iPTMnet; Q24046; -.
DR PaxDb; Q24046; -.
DR PRIDE; Q24046; -.
DR DNASU; 33952; -.
DR EnsemblMetazoa; FBtr0079384; FBpp0079012; FBgn0015776.
DR EnsemblMetazoa; FBtr0332370; FBpp0304646; FBgn0015776.
DR GeneID; 33952; -.
DR KEGG; dme:Dmel_CG9258; -.
DR CTD; 33952; -.
DR FlyBase; FBgn0015776; nrv1.
DR VEuPathDB; VectorBase:FBgn0015776; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_0_0_1; -.
DR InParanoid; Q24046; -.
DR OMA; ECKAYGQ; -.
DR OrthoDB; 998086at2759; -.
DR PhylomeDB; Q24046; -.
DR Reactome; R-DME-210991; Basigin interactions.
DR Reactome; R-DME-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 33952; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33952; -.
DR PRO; PR:Q24046; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0015776; Expressed in oviduct (Drosophila) and 34 other tissues.
DR ExpressionAtlas; Q24046; baseline and differential.
DR Genevisible; Q24046; DM.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:FlyBase.
DR GO; GO:0001671; F:ATPase activator activity; IDA: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:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; IDA:FlyBase.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR Gene3D; 2.60.40.1660; -; 1.
DR InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR PANTHER; PTHR11523; PTHR11523; 1.
DR Pfam; PF00287; Na_K-ATPase; 1.
DR PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW Potassium; Potassium transport; Reference proteome; Signal-anchor; Sodium;
KW Sodium transport; Sodium/potassium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..309
FT /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT /id="PRO_0000219120"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT DISULFID 143..155
FT /evidence="ECO:0000250"
FT DISULFID 165..179
FT /evidence="ECO:0000250"
FT DISULFID 225..282
FT /evidence="ECO:0000250"
FT CONFLICT 205
FT /note="D -> N (in Ref. 4; AAM52659)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..220
FT /note="QQ -> HE (in Ref. 1; AAC46608)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="N -> F (in Ref. 1; AAC46608)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="V -> A (in Ref. 1; AAC46608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 35309 MW; 35EA43910B86D84F CRC64;
MSKNNGKGAK GEFEFPQPAK KQTFSEMIYN PQEGTFFGRT GKSWSQLLLF YTIFYIVLAA
LFTICMQGLL STISDTEPKW KLQDSLIGTN PGLGFRPLSE QTERGSVIAF DGKKPAESDY
WIELIDDFLR DYNHTEGRDM KHCGFGQVLE PTDVCVVNTD LFGGCSKANN YGYKTNQPCI
FLKLNKIFGW IPEVYDKEEK DMPDDLKKVI NETKTEERQQ VWVSCNGHLG KDKENFQNIR
YFPSQGFPSY YYPFLNQPGY LSPLVAVQFN SPPKGQMLDV ECRAWAKNIQ YSGSVRDRKG
SVTFQILLD
