ID   AT1B1_RHIMB             Reviewed;         303 AA.
AC   P30715;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE   AltName: Full=Sodium/potassium-dependent ATPase beta-1 subunit;
OS   Rhinella marina (Cane toad) (Bufo marinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Rhinella.
OX   NCBI_TaxID=8386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Urinary bladder urothelium;
RX   PubMed=1380956; DOI=10.1016/s0021-9258(18)41869-8;
RA   Jaisser F., Canessa C.M., Horisberger J.-D., Rossier B.C.;
RT   "Primary sequence and functional expression of a novel ouabain-resistant
RT   Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-
RT   pump.";
RL   J. Biol. Chem. 267:16895-16903(1992).
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 exact function of
CC       this glycoprotein is not known. Some specific sequence of the beta
CC       subunit can modulate the activation of the Na,K-pump by extracellular
CC       potassium ions.
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. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Abundantly in kidney, at a lower extent in bladder,
CC       colon, eye and testis. Low levels in brain, heart, spleen and liver.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; Z11797; CAA77841.1; -; mRNA.
DR   PIR; B43451; B43451.
DR   AlphaFoldDB; P30715; -.
DR   SMR; P30715; -.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW   Potassium; Potassium transport; 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_0000219117"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..303
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        127..150
FT                   /evidence="ECO:0000250"
FT   DISULFID        160..176
FT                   /evidence="ECO:0000250"
FT   DISULFID        212..275
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   303 AA;  34533 MW;  3A4493D00F25805D CRC64;
     MARDKNKEND GSWKKFLWDP EKKEFMGRTG SSWFKILLFY LVFYGCLAGI FIGTIQVLLL
     TLSIYEPKYQ DRVAPPGLTQ VPRAVKAEIS FTVGNPSTYE DYVTSLSNFL NQYNSSKQDN
     LALFEDCGDK PKGYIDRGAI SPDHGTKRSC QFKREWLGEC SGLNDTTFGF NEGKPCLIVK
     LNRIVGFKPR PTNVDVPAAV ANLTENIIPL HCKGKRPEDD NNLLDIQYYG MGGYPGFPLN
     YYPYYGRLLQ PNYLQPLIAV QFTNITLDTE VRIECRAYGE NLLLSEKDRF QGRFDIKIEM
     KSS