AT1B1_CANLF
ID AT1B1_CANLF Reviewed; 303 AA.
AC P06583;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN Name=ATP1B1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Kidney;
RX PubMed=3030434; DOI=10.1016/0167-4838(87)90095-1;
RA Brown T.A., Horowitz B., Miller R.P., McDonough A.A., Farley R.A.;
RT "Molecular cloning and sequence analysis of the (Na+ + K+)-ATPase beta
RT subunit from dog kidney.";
RL Biochim. Biophys. Acta 912:244-253(1987).
RN [2]
RP GLYCOSYLATION AT ASN-158; ASN-193 AND ASN-265.
RX PubMed=2833926; DOI=10.1016/0167-4838(88)90054-4;
RA Miller R.P., Farley R.A.;
RT "All three potential N-glycosylation sites of the dog kidney (Na+ + K+)-
RT ATPase beta-subunit contain oligosaccharide.";
RL Biochim. Biophys. Acta 954:50-57(1988).
RN [3]
RP INTERACTION WITH FXYD1.
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 [4]
RP FUNCTION IN ADHESION.
RX PubMed=22328500; DOI=10.1242/jcs.100149;
RA Tokhtaeva E., Sachs G., Sun H., Dada L.A., Sznajder J.I., Vagin O.;
RT "Identification of the amino acid region involved in the intercellular
RT interaction between the beta1 subunits of Na+/K+ -ATPase.";
RL J. Cell Sci. 125:1605-1616(2012).
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 (PubMed:22328500).
CC Plays a role in innate immunity by enhancing virus-triggered induction
CC of interferons (IFNs) and interferon stimulated genes (ISGs).
CC Mechanistically, enhances the ubiquitination of TRAF3 and TRAF6 as well
CC as the phosphorylation of TAK1 and TBK1 (By similarity).
CC {ECO:0000250|UniProtKB:P05026, ECO:0000269|PubMed:22328500}.
CC -!- FUNCTION: Involved in cell adhesion and establishing epithelial cell
CC polarity. {ECO:0000269|PubMed:22328500}.
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
CC (PubMed:21454534). Interacts with regulatory subunit FXYD3 (By
CC similarity). Interacts with NKAIN1, NKAIN2 and NKAIN4 (By similarity).
CC Interacts with MLC1. Part of a complex containing MLC1, TRPV4, AQP4 and
CC HEPACAM. Interacts with KIRREL3 (By similarity). Interacts with OBSCN
CC (via 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 ECO:0000269|PubMed:21454534}.
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; X05297; CAA28917.1; -; mRNA.
DR PIR; S07148; PWDGB.
DR AlphaFoldDB; P06583; -.
DR SMR; P06583; -.
DR STRING; 9615.ENSCAFP00000022476; -.
DR iPTMnet; P06583; -.
DR PaxDb; P06583; -.
DR eggNOG; KOG3927; Eukaryota.
DR InParanoid; P06583; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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 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; Immunity; Innate immunity; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Signal-anchor; Sodium; Sodium transport;
KW Sodium/potassium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..303
FT /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT /id="PRO_0000219096"
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:0000269|PubMed:2833926"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2833926"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2833926"
FT DISULFID 126..149
FT DISULFID 159..175
FT /evidence="ECO:0000269|PubMed:2833926"
FT DISULFID 213..276
SQ SEQUENCE 303 AA; 35240 MW; 7E956AA6D5015318 CRC64;
MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT
ISEFKPTYQD RVAPPGLTQI PQIQKTEISF RPNDPKSYEE YVRNIVRFLE KYKDSAQKDE
MIFEDCGNMP SEIKERGEFN NERGERKVCR FKLEWLGNCS GINDETYGYR DGKPCVLIKL
NRVLGFKPKP PKNESLEAYP VMKYSPYVLP VQCTGKRDED KDRIGNVEYF GLGGYPGFPL
QYYPYYGKLL QPKYLQPLLA VQFTNLTMDT EIRIECKAYG ENIGYSEKDR FQGRFDVKIE
VKS
