AT1B1_SHEEP
ID AT1B1_SHEEP Reviewed; 303 AA.
AC P05028;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN Name=ATP1B1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3012356; DOI=10.1038/321429a0;
RA Shull G.E., Lane L.K., Lingrel J.B.;
RT "Amino-acid sequence of the beta-subunit of the (Na+ + K+)ATPase deduced
RT from a cDNA.";
RL Nature 321:429-431(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7521214; DOI=10.1016/0167-4838(94)00074-3;
RA Sun Y., Ball W.J. Jr.;
RT "Identification of antigenic sites on the Na+/K(+)-ATPase beta-subunit:
RT their sequences and the effects of thiol reduction upon their structure.";
RL Biochim. Biophys. Acta 1207:236-248(1994).
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. Plays a role in innate
CC immunity by enhancing virus-triggered induction of interferons (IFNs)
CC and interferon stimulated genes (ISGs). Mechanistically, enhances the
CC ubiquitination of TRAF3 and TRAF6 as well as the phosphorylation of
CC TAK1 and TBK1. {ECO:0000250|UniProtKB:P05026}.
CC -!- FUNCTION: Involved in cell adhesion and establishing epithelial cell
CC polarity. {ECO:0000250|UniProtKB:P05026}.
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 (By similarity).
CC Interacts with NKAIN1, NKAIN2 and NKAIN4 (By similarity). Interacts
CC with MLC1. Part of a complex containing MLC1, TRPV4, AQP4 and HEPACAM.
CC Interacts with KIRREL3 (By similarity). Interacts with OBSCN (via
CC protein kinase domain 1) (By similarity). Interacts with TRAF3 and
CC TRAF6 (By similarity). {ECO:0000250|UniProtKB:P05026,
CC ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}.
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
CC {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the
CC intercalated disk and sarcolemma in cardiomyocytes. Localizes in long
CC striations at the level of Z and M lines.
CC {ECO:0000250|UniProtKB:P14094}.
CC -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC and mediates cell adhesion properties. {ECO:0000250}.
CC -!- PTM: Glutathionylated (By similarity). N-glycosylated (By similarity).
CC {ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; X03883; CAA27515.1; -; mRNA.
DR PIR; A25768; A25768.
DR RefSeq; NP_001009796.1; NM_001009796.1.
DR AlphaFoldDB; P05028; -.
DR SMR; P05028; -.
DR STRING; 9940.ENSOARP00000010054; -.
DR PRIDE; P05028; -.
DR Ensembl; ENSOART00000010200; ENSOARP00000010054; ENSOARG00000009371.
DR Ensembl; ENSOART00020011846; ENSOARP00020009750; ENSOARG00020007736.
DR GeneID; 443384; -.
DR KEGG; oas:443384; -.
DR CTD; 481; -.
DR eggNOG; KOG3927; Eukaryota.
DR HOGENOM; CLU_057702_2_0_1; -.
DR OMA; ECKAYGQ; -.
DR OrthoDB; 998086at2759; -.
DR Proteomes; UP000002356; Chromosome 12.
DR Bgee; ENSOARG00000009371; Expressed in adult mammalian kidney and 54 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0031090; C:organelle membrane; IEA:Ensembl.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:Ensembl.
DR GO; GO:0036126; C:sperm flagellum; IEA:Ensembl.
DR GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR GO; GO:0001671; F:ATPase activator activity; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
DR GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IEA:Ensembl.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0086009; P:membrane repolarization; IEA:Ensembl.
DR GO; GO:1903281; P:positive regulation of calcium:sodium antiporter activity; IEA:Ensembl.
DR GO; GO:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; IEA:Ensembl.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; IEA:Ensembl.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glutathionylation;
KW Glycoprotein; Immunity; Innate immunity; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium transport; Reference proteome;
KW Signal-anchor; Sodium; Sodium transport; Sodium/potassium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..303
FT /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT /id="PRO_0000219101"
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..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 191..303
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:0000250|UniProtKB:P14094"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 126..149
FT /evidence="ECO:0000250"
FT DISULFID 159..175
FT /evidence="ECO:0000250"
FT DISULFID 213..276
FT /evidence="ECO:0000250"
SQ SEQUENCE 303 AA; 35071 MW; 0038B8EA355A3540 CRC64;
MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT
ISEFKPTYQD RVAPPGLTQI PQIQKTEIAF RPNDPKSYMT YVDNIDNFLK KYRDSAQKDD
MIFEDCGNVP SELKDRGEFN NEQGERKVCR FKLEWLGNCS GINDETYGYK EGKPCVIIKL
NRVLGFKPKP PKNESLETYP VMKYNPYVLP VQCTGKRDED KEKVGSIEYF GLGGYPGFPL
QYYPYYGKLL QPKYLQPLLA VQFTNLTMDT EIRIECKAYG ENIGYSEKDR FQGRFDVKIE
VKS
