ID   AT233_ANGAN             Reviewed;         302 AA.
AC   Q9I9C3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-233;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-233;
GN   Name=atnb233 {ECO:0000312|EMBL:CAB85586.1};
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] {ECO:0000305, ECO:0000312|EMBL:CAB85586.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, AND
RP   GLYCOSYLATION.
RC   TISSUE=Gill {ECO:0000269|PubMed:10896885};
RX   PubMed=10896885; DOI=10.1152/ajpregu.2000.279.1.r222;
RA   Cutler C.P., Brezillon S., Bekir S., Sanders I.L., Hazon N., Cramb G.;
RT   "Expression of a duplicate Na,K-ATPase beta(1)-isoform in the European eel
RT   (Anguilla anguilla).";
RL   Am. J. Physiol. 279:R222-R229(2000).
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. {ECO:0000305}.
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 mainly in epithelial tissues.
CC       {ECO:0000269|PubMed:10896885}.
CC   -!- INDUCTION: By seawater acclimation in sexually maturing migratory
CC       silver eels but not in sexually immature non-migratory yellow eels.
CC       {ECO:0000269|PubMed:10896885}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:10896885}.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; AJ239317; CAB85586.1; -; mRNA.
DR   AlphaFoldDB; Q9I9C3; -.
DR   SMR; Q9I9C3; -.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; NAS:UniProtKB.
DR   GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; NAS:UniProtKB.
DR   GO; GO:0006813; P:potassium ion transport; NAS:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; NAS:UniProtKB.
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..302
FT                   /note="Sodium/potassium-transporting ATPase subunit beta-
FT                   233"
FT                   /id="PRO_0000219115"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        125..148
FT                   /evidence="ECO:0000250|UniProtKB:P33704"
FT   DISULFID        158..174
FT                   /evidence="ECO:0000250|UniProtKB:P33704"
FT   DISULFID        213..274
FT                   /evidence="ECO:0000250|UniProtKB:P33704"
SQ   SEQUENCE   302 AA;  34707 MW;  721E056F04274D0D CRC64;
     MSGNKDSDGG WKTFIWNSEK KELLGRTGCS WFKILLFYVI FYGCLAAVFV GTIQALLLTL
     SNYKPTHQDR VAPPGLSHTP CPEKAEITFN KHELETYMKY TKGMKEFLEL YDETAQLDQL
     KYEDCGENPG GYKNRGDLES DIGVRKACRF KRSWLKDCSG LEDRTFGFKD GKPCVIVKLN
     RIVNFRPKPP NSNESIPEDA KAKVRPNVIP IYCTNKKEED AGKLQEVKYF GIGDGFPLQY
     YPYYGKLLHP QYLQPLVAIQ FTNLTMNTEL RIECRIYGEN IGYSEKDRYQ GRFDIKITVN
     DS