ID   AT1B2_RHIMB             Reviewed;         299 AA.
AC   P43002;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-2;
DE   AltName: Full=Beta-B1 chain;
DE   AltName: Full=Sodium/potassium-dependent ATPase beta-2 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=8134260; DOI=10.1007/bf00374871;
RA   Jaisser F., Horisberger J., Rossier B.C.;
RT   "Primary sequence and functional expression of a novel beta subunit of the
RT   P-ATPase gene family.";
RL   Pflugers Arch. 425:446-452(1993).
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: Expressed at a high level in bladder epithelial
CC       cells and eye and at a trace level in kidney; it is not detectable in
CC       significant amounts in the stomach, colon and small intestine.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; Z25812; CAA81060.1; -; mRNA.
DR   PIR; S39267; S39267.
DR   AlphaFoldDB; P43002; -.
DR   SMR; P43002; -.
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..299
FT                   /note="Sodium/potassium-transporting ATPase subunit beta-2"
FT                   /id="PRO_0000219118"
FT   TOPO_DOM        1..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..299
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        130..152
FT                   /evidence="ECO:0000250"
FT   DISULFID        162..178
FT                   /evidence="ECO:0000250"
FT   DISULFID        206..270
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   299 AA;  34288 MW;  9578295B790C879B CRC64;
     MAALTQKKTC SQMMEEWKEF MWNPRTREFM GRTGSSWALI LLFYVVFYAF LTAVFSLSLW
     VMLQTIDEYT PKYADRLANP GLMIRPKMDT TEVVYSTNGM NGTWQAYVDN LNSLLKDYNK
     TVQMERGVNC TPGVYNMQED TGDVRNNPKK ACWFFRDVLG DCSGVSDTTY GYQDGKPCVL
     IKMNRVINFL PVPIKELSNT SITIKCTAQN NDDLLGSIQY FPSVNNQSLG AIDLMYFPYY
     GNRAQQNYTQ PFVAVKFLNA TKGVDHMVEC RVNAANINNQ DPRDLYQGRV IFTMKIDRL