AT1B3_MOUSE
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 03-AUG-2022, entry version 163.
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, Pancreas,
RC 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}.
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DR EMBL; U59761; AAC00019.1; -; mRNA.
DR CCDS; CCDS23414.1; -.
DR RefSeq; NP_031528.1; NM_007502.4.
DR AlphaFoldDB; P97370; -.
DR SMR; P97370; -.
DR IntAct; P97370; 2.
DR STRING; 10090.ENSMUSP00000034983; -.
DR GlyConnect; 2729; 7 N-Linked glycans (2 sites).
DR GlyGen; P97370; 2 sites, 7 N-linked glycans (2 sites).
DR iPTMnet; P97370; -.
DR PhosphoSitePlus; P97370; -.
DR SwissPalm; P97370; -.
DR EPD; P97370; -.
DR jPOST; P97370; -.
DR PaxDb; P97370; -.
DR PeptideAtlas; P97370; -.
DR PRIDE; P97370; -.
DR ProteomicsDB; 265121; -.
DR Antibodypedia; 33485; 402 antibodies from 32 providers.
DR DNASU; 11933; -.
DR Ensembl; ENSMUST00000034983; ENSMUSP00000034983; ENSMUSG00000032412.
DR GeneID; 11933; -.
DR KEGG; mmu:11933; -.
DR UCSC; uc009rck.2; mouse.
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; NQSLAQW; -.
DR OrthoDB; 998086at2759; -.
DR PhylomeDB; P97370; -.
DR TreeFam; TF314618; -.
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 74 CRISPR screens.
DR ChiTaRS; Atp1b3; mouse.
DR PRO; PR:P97370; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P97370; protein.
DR Bgee; ENSMUSG00000032412; Expressed in sciatic nerve and 257 other tissues.
DR ExpressionAtlas; P97370; baseline and differential.
DR Genevisible; P97370; MM.
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:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; ISO:MGI.
DR GO; GO:0036126; C:sperm flagellum; ISO:MGI.
DR GO; GO:0001671; F:ATPase activator activity; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; ISO:MGI.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:MGI.
DR GO; GO:0086009; P:membrane repolarization; ISO:MGI.
DR GO; GO:0030001; P:metal ion transport; ISO:MGI.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; ISO:MGI.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; ISO:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; ISO:MGI.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006814; P:sodium ion transport; ISO:MGI.
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 TIGRFAMs; TIGR01107; Na_K_ATPase_bet; 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
