ID   AT1B1_CHICK             Reviewed;         305 AA.
AC   P08251;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   02-SEP-2026, entry version 148.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN   Name=ATP1B1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3038895; DOI=10.1016/s0021-9258(18)61025-7;
RA   Takeyasu K., Tamkun M.M., Siegel N.R., Fambrough D.M.;
RT   "Expression of hybrid (Na+ + K+)-ATPase molecules after transfection of
RT   mouse Ltk-cells with DNA encoding the beta-subunit of an avian brain sodium
RT   pump.";
RL   J. Biol. Chem. 262:10733-10740(1987).
CC   -!- FUNCTION: Non-catalytic subunit of the Na(+)/K(+)-ATPase pump that
CC       hydrolyzes ATP to exchange ions across the plasma membrane, exporting 3
CC       Na(+) and importing 2 K(+) per cycle against electrochemical gradients.
CC       The beta subunit is important for the folding, stability, and targeting
CC       of the Na(+)/K(+)-ATPase pump to the plasma membranes (By similarity).
CC       In addition, acts as a homotypic cell adhesion molecule in epithelia
CC       cells. Interactions between ATP1B1 on neighboring cells are critical
CC       for proper lateral polarization of the Na(+)/K(+)-ATPase pump and for
CC       stabilizing cell-cell adhesion (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P05026,
CC       ECO:0000250|UniProtKB:P06583, ECO:0000250|UniProtKB:Q91580}.
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, called FXYD. There are four, three and
CC       seven isoforms for the alpha, beta and regulatory subunits,
CC       respectively, among which the expression of the alpha isoforms is
CC       tissue-specific. {ECO:0000250|UniProtKB:P07340,
CC       ECO:0000250|UniProtKB:P14094}.
CC   -!- INTERACTION:
CC       P08251; Q8AYS8: KCNMA1; NbExp=3; IntAct=EBI-7206371, EBI-1635766;
CC       P08251; Q08460: Kcnma1; Xeno; NbExp=5; IntAct=EBI-7206371, EBI-1633915;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05026};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:P05027}.
CC       Apical cell membrane {ECO:0000250|UniProtKB:P07340}; Single-pass type
CC       II membrane protein {ECO:0000250|UniProtKB:P05027}. Cell membrane,
CC       sarcolemma {ECO:0000250|UniProtKB:P14094}.
CC   -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC       and mediates cell adhesion properties. {ECO:0000250|UniProtKB:P05026}.
CC   -!- PTM: Glutathionylated (By similarity). N-glycosylated; promotes the
CC       stability of ATP1B1 homotypic interactions (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}.
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; J02787; AAA48608.1; -; mRNA.
DR   PIR; A28491; A28491.
DR   RefSeq; NP_990851.2; NM_205520.5.
DR   AlphaFoldDB; P08251; -.
DR   SMR; P08251; -.
DR   DIP; DIP-29N; -.
DR   FunCoup; P08251; 1916.
DR   IntAct; P08251; 2.
DR   MINT; P08251; -.
DR   STRING; 9031.ENSGALP00000036140; -.
DR   GlyCosmos; P08251; 3 sites, No reported glycans.
DR   GlyGen; P08251; 3 sites.
DR   PaxDb; 9031-ENSGALP00000036140; -.
DR   GeneID; 396529; -.
DR   KEGG; gga:396529; -.
DR   CTD; 481; -.
DR   VEuPathDB; HostDB:geneid_396529; -.
DR   eggNOG; KOG3927; Eukaryota.
DR   InParanoid; P08251; -.
DR   OrthoDB; 5912413at2759; -.
DR   PhylomeDB; P08251; -.
DR   PRO; PR:P08251; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IBA:GO_Central.
DR   GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR   GO; GO:0030007; P:intracellular potassium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006883; P:intracellular sodium ion homeostasis; IBA:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR   FunFam; 1.20.5.170:FF:000062; Sodium/potassium-transporting ATPase subunit beta; 1.
DR   FunFam; 2.60.40.1660:FF:000002; 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:SF10; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT BETA-1; 1.
DR   Pfam; PF00287; Na_K-ATPase; 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 membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW   Potassium; Potassium transport; Reference proteome; Signal-anchor; Sodium;
KW   Sodium transport; Sodium/potassium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..305
FT                   /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT                   /id="PRO_0000219102"
FT   TOPO_DOM        1..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P05027"
FT   TRANSMEM        36..63
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000250|UniProtKB:P05027"
FT   TOPO_DOM        64..305
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P05027"
FT   REGION          192..304
FT                   /note="immunoglobulin-like"
FT                   /evidence="ECO:0000250|UniProtKB:P05026"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P05026"
FT   DISULFID        127..150
FT                   /evidence="ECO:0000250|UniProtKB:P05026"
FT   DISULFID        160..176
FT                   /evidence="ECO:0000250|UniProtKB:P05026"
FT   DISULFID        214..277
FT                   /evidence="ECO:0000250|UniProtKB:P05026"
SQ   SEQUENCE   305 AA;  34941 MW;  E56E47E920769252 CRC64;
     MARGKANDGD GNWKKFIWNS EKKELLGRTG GSWFKILLFY VIFYGCLAGI FIGTIQVMLL
     TVSEFEPKYQ DRVAPPGLTQ VPQVQKTEIS FTVNDPKSYD PYVKNLEGFL NKYSAGEQTD
     NIVFQDCGDI PTDYKERGPY NDAQGQKKVC KFKREWLENC SGLQDNTFGY KDGKPCILVK
     LNRIIGFKPK APENESLPSD LAGKYNPYLI PVHCVAKRDE DADKIGMVEY YGMGGYPGFA
     LQYYPYYGRL LQPQYLQPLV AVQFTNLTYD VEVRVECKEY GQNIQYSDKD RFQGRFDIKF
     DIKSS
//