ATPB2_DROME
ID ATPB2_DROME Reviewed; 323 AA.
AC Q24048; Q24047; Q9VM84; Q9VM85;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-2;
DE AltName: Full=Protein nervana 2;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-2;
GN Name=nrv2; ORFNames=CG9261;
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 2.1 AND 2.2).
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, 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 2.2).
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 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-206, AND IDENTIFICATION BY MASS
RP 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).
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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2.2; Synonyms=C, F;
CC IsoId=Q24048-1; Sequence=Displayed;
CC Name=2.1; Synonyms=A, D;
CC IsoId=Q24048-2; Sequence=VSP_000350;
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
CC shows a nervous system specific distribution: optic lobes, brain,
CC thoracic ganglia and axonal pathways in the leg. Both isoforms
CC concentrate in the adult head, isoform 2.2 being predominant. Both
CC isoforms are weakly expressed in the thorax and very poorly expressed
CC in the abdomen. {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; U22439; AAC46609.1; -; mRNA.
DR EMBL; U22440; AAC46610.1; -; mRNA.
DR EMBL; AE014134; AAF52438.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10600.1; -; Genomic_DNA.
DR EMBL; AY060289; AAL25328.1; -; mRNA.
DR RefSeq; NP_001014475.1; NM_001014475.2. [Q24048-1]
DR RefSeq; NP_001014476.1; NM_001014476.2. [Q24048-2]
DR RefSeq; NP_001260164.1; NM_001273235.1. [Q24048-1]
DR RefSeq; NP_477168.1; NM_057820.4. [Q24048-1]
DR RefSeq; NP_477169.1; NM_057821.4. [Q24048-2]
DR RefSeq; NP_723216.1; NM_164711.2. [Q24048-2]
DR AlphaFoldDB; Q24048; -.
DR SMR; Q24048; -.
DR BioGRID; 60105; 5.
DR IntAct; Q24048; 23.
DR STRING; 7227.FBpp0079009; -.
DR GlyGen; Q24048; 2 sites.
DR iPTMnet; Q24048; -.
DR PaxDb; Q24048; -.
DR PRIDE; Q24048; -.
DR DNASU; 33953; -.
DR EnsemblMetazoa; FBtr0079381; FBpp0079009; FBgn0015777. [Q24048-1]
DR EnsemblMetazoa; FBtr0079382; FBpp0079010; FBgn0015777. [Q24048-2]
DR EnsemblMetazoa; FBtr0079383; FBpp0079011; FBgn0015777. [Q24048-2]
DR EnsemblMetazoa; FBtr0100381; FBpp0099793; FBgn0015777. [Q24048-2]
DR EnsemblMetazoa; FBtr0100382; FBpp0099794; FBgn0015777. [Q24048-1]
DR EnsemblMetazoa; FBtr0332369; FBpp0304645; FBgn0015777. [Q24048-1]
DR GeneID; 33953; -.
DR KEGG; dme:Dmel_CG9261; -.
DR CTD; 33953; -.
DR FlyBase; FBgn0015777; nrv2.
DR VEuPathDB; VectorBase:FBgn0015777; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_0_0_1; -.
DR InParanoid; Q24048; -.
DR OMA; VCRPGHY; -.
DR PhylomeDB; Q24048; -.
DR Reactome; R-DME-210991; Basigin interactions.
DR Reactome; R-DME-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 33953; 0 hits in 3 CRISPR screens.
DR ChiTaRS; nrv2; fly.
DR GenomeRNAi; 33953; -.
DR PRO; PR:Q24048; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0015777; Expressed in antenna and 52 other tissues.
DR ExpressionAtlas; Q24048; baseline and differential.
DR Genevisible; Q24048; DM.
DR GO; GO:0030424; C:axon; 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:0001671; F:ATPase activator activity; IDA:FlyBase.
DR GO; GO:0006812; P:cation transport; IDA:FlyBase.
DR GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP: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:0060857; P:establishment of glial blood-brain barrier; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
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: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:0035151; P:regulation of tube size, open tracheal system; 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 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Signal-anchor; Sodium; Sodium transport;
KW Sodium/potassium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..323
FT /note="Sodium/potassium-transporting ATPase subunit beta-2"
FT /id="PRO_0000219121"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT DISULFID 153..165
FT /evidence="ECO:0000250"
FT DISULFID 175..189
FT /evidence="ECO:0000250"
FT DISULFID 241..298
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..46
FT /note="MPTITEDCIDGFQQYYSRPPERPKKKSLKQMVYDSEDNSYFGRSMD -> MS
FT KPVPMSPSFVDEDLHNLRKPKPFKLGQFLYNTEDGTVMGRDRS (in isoform
FT 2.1)"
FT /evidence="ECO:0000303|PubMed:7777518"
FT /id="VSP_000350"
FT CONFLICT 162
FT /note="G -> A (in Ref. 1; AAC46609/AAC46610)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="H -> R (in Ref. 1; AAC46609/AAC46610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 37283 MW; 8926A9D1FC48D6EF CRC64;
MPTITEDCID GFQQYYSRPP ERPKKKSLKQ MVYDSEDNSY FGRSMDSWAK IGIFYVAFYG
VLAALVAICM WAFFQTLDPR IPKWTLDRSL IGTNPGLGFR PLPPVDNVES TLIWYKGTQH
ENYKHWTDSL DDFLAVYKVP GLTPGRGQNI YNCDYNQPPP KGQVCDVDIK TWSPCTKENN
YSYHKSAPCI FLKLNKIYGW IPEYYNRSND LPANMPASLK TYIAEVEKTQ PEKLNTIWVS
CEGENPADQE NIGAVNYLPI RGFPGYFYPY QNSEGYLSPL VAVHFQRPKR GIIINVECRA
WARNIIHDRK ERIGSVHYEL LID
