ID   AT1B3_MOUSE             Reviewed;         278 AA.
AC   P97370;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 182.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-3;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-3;
DE            Short=ATPB-3;
DE   AltName: CD_antigen=CD298;
GN   Name=Atp1b3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Retina;
RX   PubMed=9003452; DOI=10.1016/s0167-4781(96)00192-3;
RA   Besirli C.G., Gong T.-W.L., Lomax M.I.;
RT   "Novel beta 3 isoform of the Na,K-ATPase beta subunit from mouse retina.";
RL   Biochim. Biophys. Acta 1350:21-26(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 18-31, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-124 AND ASN-197.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 exact function of
CC       the beta-3 subunit is not known.
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 catalytic alpha subunit
CC       ATP12A. {ECO:0000250|UniProtKB:Q63377}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q63377}; Single-pass type II membrane protein
CC       {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q63377}; Single-pass type II membrane protein
CC       {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P54709}.
CC       Note=Identified by mass spectrometry in melanosome fractions from stage
CC       I to stage IV. {ECO:0000250|UniProtKB:P54709}.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC       and may mediate cell adhesion properties. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U59761; AAC00019.1; -; mRNA.
DR   CCDS; CCDS23414.1; -.
DR   RefSeq; NP_031528.1; NM_007502.6.
DR   AlphaFoldDB; P97370; -.
DR   SMR; P97370; -.
DR   BioGRID; 198246; 1.
DR   FunCoup; P97370; 1555.
DR   IntAct; P97370; 2.
DR   STRING; 10090.ENSMUSP00000034983; -.
DR   GlyConnect; P97370; 7 N-Linked glycans (2 sites).
DR   GlyCosmos; P97370; 2 sites, 7 glycans.
DR   GlyGen; P97370; 3 sites, 9 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P97370; -.
DR   PhosphoSitePlus; P97370; -.
DR   SwissPalm; P97370; -.
DR   jPOST; P97370; -.
DR   PaxDb; 10090-ENSMUSP00000034983; -.
DR   PeptideAtlas; P97370; -.
DR   ProteomicsDB; 265121; -.
DR   Pumba; P97370; -.
DR   Antibodypedia; 33485; 416 antibodies from 35 providers.
DR   DNASU; 11933; -.
DR   Ensembl; ENSMUST00000034983.7; ENSMUSP00000034983.6; ENSMUSG00000032412.9.
DR   GeneID; 11933; -.
DR   KEGG; mmu:11933; -.
DR   UCSC; uc009rck.2; mouse.
DR   AGR; MGI:107788; -.
DR   CTD; 483; -.
DR   MGI; MGI:107788; Atp1b3.
DR   VEuPathDB; HostDB:ENSMUSG00000032412; -.
DR   eggNOG; KOG3927; Eukaryota.
DR   GeneTree; ENSGT01030000234579; -.
DR   HOGENOM; CLU_057702_1_1_1; -.
DR   InParanoid; P97370; -.
DR   OMA; NRNSGEF; -.
DR   OrthoDB; 5912413at2759; -.
DR   PhylomeDB; P97370; -.
DR   Reactome; R-MMU-210991; Basigin interactions.
DR   Reactome; R-MMU-5578775; Ion homeostasis.
DR   Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR   BioGRID-ORCS; 11933; 19 hits in 79 CRISPR screens.
DR   PRO; PR:P97370; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P97370; protein.
DR   Bgee; ENSMUSG00000032412; Expressed in sciatic nerve and 261 other cell types or tissues.
DR   ExpressionAtlas; P97370; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005901; C:caveola; ISO:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:GO_Central.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; ISO:GO_Central.
DR   GO; GO:0036126; C:sperm flagellum; ISO:GO_Central.
DR   GO; GO:0001671; F:ATPase activator activity; ISO:GO_Central.
DR   GO; GO:0051117; F:ATPase binding; ISO:GO_Central.
DR   GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; ISO:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:GO_Central.
DR   GO; GO:0141109; F:transporter activator activity; ISO:GO_Central.
DR   GO; GO:0030007; P:intracellular potassium ion homeostasis; ISO:GO_Central.
DR   GO; GO:0006883; P:intracellular sodium ion homeostasis; ISO:GO_Central.
DR   GO; GO:0086009; P:membrane repolarization; ISO:GO_Central.
DR   GO; GO:0030001; P:metal ion transport; ISO:GO_Central.
DR   GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; ISO:GO_Central.
DR   GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; ISO:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; ISO:GO_Central.
DR   GO; GO:0006813; P:potassium ion transport; ISO:GO_Central.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISO:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; ISO:GO_Central.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; ISO:GO_Central.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; ISO:GO_Central.
DR   GO; GO:0006814; P:sodium ion transport; ISO:GO_Central.
DR   FunFam; 2.60.40.1660:FF:000005; Sodium/potassium-transporting ATPase subunit beta; 1.
DR   Gene3D; 2.60.40.1660; Na, k-atpase alpha subunit; 1.
DR   InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR   InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR   NCBIfam; TIGR01107; Na_K_ATPase_bet; 1.
DR   PANTHER; PTHR11523; SODIUM/POTASSIUM-DEPENDENT ATPASE BETA SUBUNIT; 1.
DR   PANTHER; PTHR11523:SF47; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT BETA-3; 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; Direct protein sequencing; 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..278
FT                   /note="Sodium/potassium-transporting ATPase subunit beta-3"
FT                   /id="PRO_0000219109"
FT   TOPO_DOM        1..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..278
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          186..278
FT                   /note="immunoglobulin-like"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   DISULFID        128..144
FT                   /evidence="ECO:0000250"
FT   DISULFID        154..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        191..249
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   278 AA;  31776 MW;  98A46FF6EDA85AAC CRC64;
     MTKTEKKSFH QSLAEWKLFI YNPSSGEFLG RTSKSWGLIL LFYLVFYGFL AALFTFTMWA
     MLQTLNDEVP KYRDQIPSPG LMVFPKPQTA LEYTFSMSEP QTYKKLVEDL ESFLKPYSVE
     EQKNLTSCPD GAPFIQHGPD YRACQFPVSL LEECSGVTDA NFGYSKGQPC ILVKMNRIID
     LIPDGYPQIS CLPKEENATI ATYPEFGVLD LKYFPYYGKK RHVGYRQPLV AVQVKFDSGL
     NKKEVTVECH IAGTRNLKNK NERDKFLGRV SFKVTARA
//