ID   AT1B1_ANGAN             Reviewed;         303 AA.
AC   P51165;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN   Name=atp1b1;
OS   Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7936;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gill;
RX   PubMed=8574922; DOI=10.1016/0305-0491(95)00037-9;
RA   Cutler C., Sanders I.L., Hazon N., Cramb G.;
RT   "Primary sequence, tissue specificity and expression of the Na+,K(+)-ATPase
RT   alpha 1 subunit in the European eel (Anguilla anguilla).";
RL   Comp. Biochem. Physiol. 111B:567-573(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Gill;
RA   Cutler C., Sanders I.L., Hazon N., Cramb G.;
RT   "Primary sequence, tissue specificity and expression of the Na+,K(+)-ATPase
RT   beta 1 subunit in the European eel (Anguilla anguilla).";
RL   Fish Physiol. Biochem. 14:423-429(1995).
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   -!- TISSUE SPECIFICITY: Detected in all tissues except liver and cardiac
CC       muscle. Highest levels found in intestine, ovary and kidney with
CC       marginally lower levels in brain, spleen, esophagus, eye and pancreas,
CC       intermediate levels in gill and low levels in white and red skeletal
CC       muscle. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; X76109; CAA53715.1; -; mRNA.
DR   PIR; S45093; S45093.
DR   AlphaFoldDB; P51165; -.
DR   SMR; P51165; -.
DR   OMA; RTGGSWX; -.
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_0000219114"
FT   TOPO_DOM        1..34
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..303
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
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        126..149
FT                   /evidence="ECO:0000250"
FT   DISULFID        159..175
FT                   /evidence="ECO:0000250"
FT   DISULFID        214..275
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   303 AA;  34901 MW;  3117CF841542321C CRC64;
     MPAATKDSDG GWKKFLWNSE KKEFLGRTGG SWAKILLFYV IFYGCLAGIF IGTIQALLLT
     INDFKPVYQD RVAPPGLSHT PRSEKSEMSF KVGDPSTYQK YVKAMHDFLQ AYNDSKQENM
     MKYEDCGDTP KSYINRGELD NNQGIKKACI FRRSWLDKCS GLEDPTFGFS EGKPCLIVKL
     NRIVNFRPRP PTSNDSIPEE AQSKVQPDVI PIYCTNKREE DAAKVREIKY YGIQEGFPLQ
     YYPYYGKQLH PQYLQPLVAV HFTNLTMATE LRIECRVYGQ NIAYSDKDRY RGRFDVKFTI
     NES