AT1B1_MOUSE
ID AT1B1_MOUSE Reviewed; 304 AA.
AC P14094;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN Name=Atp1b1; Synonyms=Atp4b;
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=C57BL/6J; TISSUE=Brain;
RX PubMed=2557580;
RA Gloor S.;
RT "Cloning and nucleotide sequence of the mouse Na,K-ATPase beta-subunit.";
RL Nucleic Acids Res. 17:10117-10117(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 15-21; 72-107; 171-179; 205-217; 225-249 AND 279-291,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-304.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA Kato K.;
RT "A collection of cDNA clones with specific expression patterns in mouse
RT brain.";
RL Eur. J. Neurosci. 2:704-711(1990).
RN [5]
RP INTERACTION WITH FXYD3.
RX PubMed=15743908; DOI=10.1091/mbc.e04-10-0878;
RA Crambert G., Li C., Claeys D., Geering K.;
RT "FXYD3 (Mat-8), a new regulator of Na,K-ATPase.";
RL Mol. Biol. Cell 16:2363-2371(2005).
RN [6]
RP INTERACTION WITH NKAIN1; NKAIN2 AND NKAIN4.
RC STRAIN=C57BL/6J;
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-101, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158 AND ASN-266.
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 [9]
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).
RN [10]
RP INTERACTION WITH OBSCN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23392350; DOI=10.1096/fj.12-221317;
RA Hu L.Y., Kontrogianni-Konstantopoulos A.;
RT "The kinase domains of obscurin interact with intercellular adhesion
RT proteins.";
RL FASEB J. 27:2001-2012(2013).
RN [11]
RP GLUTATHIONYLATION.
RX PubMed=21454534; DOI=10.1074/jbc.m110.184101;
RA Bibert S., Liu C.C., Figtree G.A., Garcia A., Hamilton E.J., Marassi F.M.,
RA Sweadner K.J., Cornelius F., Geering K., Rasmussen H.H.;
RT "FXYD proteins reverse inhibition of the Na+-K+ pump mediated by
RT glutathionylation of its beta1 subunit.";
RL J. Biol. Chem. 286:18562-18572(2011).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=30012868; DOI=10.1161/hypertensionaha.118.11075;
RA Nakashima A., Kawamoto T., Noshiro M., Ueno T., Doi S., Honda K.,
RA Maruhashi T., Noma K., Honma S., Masaki T., Higashi Y., Kato Y.;
RT "Dec1 and CLOCK regulate Na+/K+-ATPase beta1 subunit expression and blood
RT pressure.";
RL Hypertension 72:746-754(2018).
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 -!- FUNCTION: Involved in cell adhesion and establishing epithelial cell
CC polarity. {ECO:0000250}.
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 subunit ATP12A
CC (By similarity). Interacts with regulatory subunit FXYD1 (By
CC similarity). Interacts with regulatory subunit FXYD3 (PubMed:15743908).
CC Interacts with NKAIN1, NKAIN2 and NKAIN4 (PubMed:17606467). Interacts
CC with MLC1 (By similarity). Part of a complex containing MLC1, TRPV4,
CC AQP4 and HEPACAM (By similarity). Interacts with KIRREL3 (By
CC similarity). Interacts with OBSCN (via protein kinase domain 1)
CC (PubMed:23392350). {ECO:0000250|UniProtKB:P05026,
CC ECO:0000250|UniProtKB:P07340, ECO:0000269|PubMed:15743908,
CC ECO:0000269|PubMed:17606467, ECO:0000269|PubMed:23392350}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P07340}; Single-pass type II membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:23392350}.
CC Note=Colocalizes with OBSCN at the intercalated disk and sarcolemma in
CC cardiomyocytes. Localizes in long striations at the level of Z and M
CC lines. {ECO:0000269|PubMed:23392350}.
CC -!- TISSUE SPECIFICITY: Expressed in cardiac muscle and in flexor digitorum
CC brevis (FDB) muscle (at protein level) (PubMed:23392350). Expressed in
CC a circadian manner in the kidney and aorta (at protein level)
CC (PubMed:30012868). {ECO:0000269|PubMed:23392350,
CC ECO:0000269|PubMed:30012868}.
CC -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC and mediates cell adhesion properties. {ECO:0000250}.
CC -!- PTM: Glutathionylated (PubMed:21454534). N-glycosylated (By
CC similarity). {ECO:0000250|UniProtKB:P07340,
CC ECO:0000269|PubMed:21454534}.
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; X16646; CAA34639.1; -; mRNA.
DR EMBL; BC027319; AAH27319.1; -; mRNA.
DR EMBL; X61433; CAA43675.1; -; mRNA.
DR CCDS; CCDS35755.1; -.
DR PIR; S09601; S09601.
DR RefSeq; NP_033851.1; NM_009721.6.
DR AlphaFoldDB; P14094; -.
DR SMR; P14094; -.
DR BioGRID; 198244; 19.
DR ComplexPortal; CPX-126; Sodium:potassium-exchanging ATPase complex.
DR IntAct; P14094; 95.
DR STRING; 10090.ENSMUSP00000027863; -.
DR GlyConnect; 2727; 14 N-Linked glycans (3 sites).
DR GlyGen; P14094; 3 sites, 14 N-linked glycans (3 sites).
DR iPTMnet; P14094; -.
DR PhosphoSitePlus; P14094; -.
DR SwissPalm; P14094; -.
DR jPOST; P14094; -.
DR PaxDb; P14094; -.
DR PeptideAtlas; P14094; -.
DR PRIDE; P14094; -.
DR ProteomicsDB; 277120; -.
DR Antibodypedia; 2485; 333 antibodies from 37 providers.
DR DNASU; 11931; -.
DR Ensembl; ENSMUST00000027863; ENSMUSP00000027863; ENSMUSG00000026576.
DR GeneID; 11931; -.
DR KEGG; mmu:11931; -.
DR UCSC; uc007dip.2; mouse.
DR CTD; 481; -.
DR MGI; MGI:88108; Atp1b1.
DR VEuPathDB; HostDB:ENSMUSG00000026576; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_2_0_1; -.
DR InParanoid; P14094; -.
DR OMA; ECKAYGQ; -.
DR OrthoDB; 998086at2759; -.
DR PhylomeDB; P14094; -.
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; 11931; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Atp1b1; mouse.
DR PRO; PR:P14094; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P14094; protein.
DR Bgee; ENSMUSG00000026576; Expressed in olfactory tubercle and 367 other tissues.
DR ExpressionAtlas; P14094; baseline and differential.
DR Genevisible; P14094; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; IMP:BHF-UCL.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0031090; C:organelle membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; IMP:BHF-UCL.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IMP:BHF-UCL.
DR GO; GO:0036126; C:sperm flagellum; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0001671; F:ATPase activator activity; IMP:ARUK-UCL.
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:0008022; F:protein C-terminus binding; IPI:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0098655; P:cation transmembrane transport; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:BHF-UCL.
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:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IC:ComplexPortal.
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:1903281; P:positive regulation of calcium:sodium antiporter activity; IMP:BHF-UCL.
DR GO; GO:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; IMP:ARUK-UCL.
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; IMP:ARUK-UCL.
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; IMP:BHF-UCL.
DR GO; GO:1902600; P:proton transmembrane transport; IC:ComplexPortal.
DR GO; GO:1903169; P:regulation of calcium ion transmembrane transport; IMP:BHF-UCL.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:BHF-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IMP:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IMP:ARUK-UCL.
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; IPR015565; Na/K_ATPase_sub_beta_chordates.
DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR PANTHER; PTHR11523; PTHR11523; 1.
DR PANTHER; PTHR11523:SF10; PTHR11523:SF10; 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.
DR PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glutathionylation; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium transport; Reference proteome; Signal-anchor; Sodium;
KW Sodium transport; Sodium/potassium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..304
FT /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT /id="PRO_0000219098"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..62
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 191..304
FT /note="immunoglobulin-like"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07340"
FT MOD_RES 101
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 126..149
FT /evidence="ECO:0000250"
FT DISULFID 159..175
FT /evidence="ECO:0000250"
FT DISULFID 214..277
FT /evidence="ECO:0000250"
SQ SEQUENCE 304 AA; 35195 MW; 8E15D8F860932680 CRC64;
MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT
ISELKPTYQD RVAPPGLTQI PQIQKTEISF RPNDPKSYEA YVLNIIRFLE KYKDSAQKDD
MIFEDCGNVP SEPKERGDIN HERGERKVCR FKLDWLGNCS GLNDDSYGYR EGKPCIIIKL
NRVLGFKPKP PKNESLETYP LMMKYNPNVL PVQCTGKRDE DKDKVGNIEY FGMGGYYGFP
LQYYPYYGKL LQPKYLQPLL AVQFTNLTVD TEIRVECKAY GENIGYSEKD RFQGRFDVKI
EIKS
