ID   AT1B3_RHIMB             Reviewed;         279 AA.
AC   P30716;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-3;
DE   AltName: Full=Sodium/potassium-dependent ATPase beta-3 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 brain, eye and testis, at a lower
CC       extent in spleen.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; Z11799; CAA77843.1; -; mRNA.
DR   EMBL; Z11800; CAA77844.1; -; mRNA.
DR   PIR; C43451; C43451.
DR   AlphaFoldDB; P30716; -.
DR   SMR; P30716; -.
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; IPR038702; Na/K_ATPase_sub_beta_sf.
DR   PANTHER; PTHR11523; PTHR11523; 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..279
FT                   /note="Sodium/potassium-transporting ATPase subunit beta-3"
FT                   /id="PRO_0000219119"
FT   TOPO_DOM        1..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..279
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        125..144
FT                   /evidence="ECO:0000250"
FT   DISULFID        154..171
FT                   /evidence="ECO:0000250"
FT   DISULFID        192..250
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   279 AA;  31678 MW;  A39CE765D644A009 CRC64;
     MAKEENKSGE QSSSEWKQFI YNPSSGEILG RTASSWALIL LFYLVFYGFL AGLFTLTMWV
     MLQTLDDSVP KYRDRVSFPG LMISPKSAGL EISFSKSDKS HMKSILKFFT HFYHHTMTPY
     KLQMCSARKA ITTEQEGVEE KKSCQFNRSS LGPCAGLEGN EYFGYNDGSP CVLVKMNRII
     GLKPDGNPHI NCTSKAENIS LQYYPEYGKI DLMYYPYYGK KTHVNYVQPL VAVKITPSNS
     TGTSEIVLEC KLYGSPNLKN NDDRDKFLGR VNFKLEIKD