ID   AT1B1_TETCF             Reviewed;         305 AA.
AC   P05029;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN   Name=atp1b1;
OS   Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX   NCBI_TaxID=7787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3005037; DOI=10.1016/0014-5793(86)80270-8;
RA   Noguchi S., Noda M., Takahashi H., Kawakami K., Ohta T., Nagano K.,
RA   Hirose T., Inayama S., Kawamura M., Numa S.;
RT   "Primary structure of the beta-subunit of Torpedo californica (Na+ + K+)-
RT   ATPase deduced from the cDNA sequence.";
RL   FEBS Lett. 196:315-320(1986).
RN   [2]
RP   DISULFIDE BOND 215-CYS--CYS-278.
RX   PubMed=2546555; DOI=10.1016/0006-291x(89)91962-1;
RA   Kellaris K.V.;
RT   "Identification of a disulfide between cysteine 214 and cysteine 277 in the
RT   beta subunit of native (Na+ + K+)ATPase.";
RL   Biochem. Biophys. Res. Commun. 162:64-70(1989).
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.
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   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; X03471; CAA27188.1; -; mRNA.
DR   PIR; A23625; PWRYNB.
DR   PIR; A33291; A33291.
DR   AlphaFoldDB; P05029; -.
DR   SMR; P05029; -.
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   1: Evidence at protein 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..305
FT                   /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT                   /id="PRO_0000219116"
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..305
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        127..150
FT                   /evidence="ECO:0000250"
FT   DISULFID        160..176
FT                   /evidence="ECO:0000250"
FT   DISULFID        215..278
FT                   /evidence="ECO:0000269|PubMed:2546555"
SQ   SEQUENCE   305 AA;  34673 MW;  BC13191F8D597563 CRC64;
     MAREKSTDDG GGWKKFLWDS EKKQVLGRTG TSWFKIFVFY LIFYGCLAGI FIGTIQVMLL
     TISDFEPKYQ DRVAPPGLSH SPYAVKTEIS FSVSNPNSYE NHVNGLKELL KNYNESKQDG
     NTPFEDCGVI PADYITRGPI EESQGQKRVC RFLLQWLKNC SGIDDPSYGY SEGKPCIIAK
     LNRILGFYPK PPKNGTDLPE ALQANYNQYV LPIHCQAKKE EDKVRIGTIE YFGMGGVGGF
     PLQYYPYYGK RLQKNYLQPL VGIQFTNLTH NVELRVECKV FGDNIAYSEK DRSLGRFEVK
     IEVKS