AT1B1_RABIT
ID AT1B1_RABIT Reviewed; 303 AA.
AC Q9TT37;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN Name=ATP1B1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white;
RX PubMed=10511383;
RA Caviston T.L., Campbell W.G., Wingo C.S., Cain B.D.;
RT "Molecular identification of the renal H+,K+-ATPases.";
RL Semin. Nephrol. 19:431-437(1999).
RN [2]
RP INTERACTION WITH FXYD3.
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).
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 (By similarity).
CC {ECO:0000250}.
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 Interacts with regulatory subunit FXYD1 (By similarity). Interacts with
CC regulatory subunit FXYD3 (PubMed:21454534). Interacts with NKAIN1,
CC NKAIN2 and NKAIN4 (By similarity). Interacts with MLC1 (By similarity).
CC Part of a complex containing MLC1, TRPV4, AQP4 and HEPACAM (By
CC similarity). Interacts with KIRREL3 (By similarity). Interacts with
CC OBSCN (via protein kinase domain 1) (By similarity).
CC {ECO:0000250|UniProtKB:P05026, ECO:0000250|UniProtKB:P07340,
CC ECO:0000250|UniProtKB:P14094, ECO:0000269|PubMed:21454534}.
CC -!- INTERACTION:
CC Q9TT37; Q9N0Z6: ATP1A1; NbExp=2; IntAct=EBI-9685670, EBI-9685690;
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; AF204927; AAF18134.1; -; mRNA.
DR RefSeq; NP_001075542.1; NM_001082073.1.
DR AlphaFoldDB; Q9TT37; -.
DR SMR; Q9TT37; -.
DR IntAct; Q9TT37; 3.
DR STRING; 9986.ENSOCUP00000020666; -.
DR GeneID; 100008749; -.
DR KEGG; ocu:100008749; -.
DR CTD; 481; -.
DR eggNOG; KOG3927; Eukaryota.
DR InParanoid; Q9TT37; -.
DR OrthoDB; 998086at2759; -.
DR Proteomes; UP000001811; 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; IEA:InterPro.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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; Disulfide bond; Glutathionylation;
KW Glycoprotein; Ion transport; Membrane; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Signal-anchor; Sodium;
KW Sodium transport; Sodium/potassium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..303
FT /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT /id="PRO_0000265958"
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:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 34940 MW; C1908DBE392E584F CRC64;
MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT
ISEFKPTYQD RVAPPGLTQV PQIQKTEIAF RPSDPKSYEE YVVNIVRFLE KYKDSAQKDD
MVFEDCGDVP SEPKERGEFN NERGQRKVCR FKLNWLGNCS GIDDETYGYK DGKPCIIIKL
NRVLGFKPKP PKNDSLEFSP GTKYNPNVLP VQCTGKRDED KEKVGSMEYF GMGDYAGFPL
QYYPYYGKLL QPKYLQPLLA VQFTNLTMDT EIRIECKAYG ENIGYSEKDR FQGRFDVKIE
VKS
