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AT1B3_XENLA
ID   AT1B3_XENLA             Reviewed;         277 AA.
AC   P21188;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-3;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-3;
DE            Short=ATPB-3;
GN   Name=atp1b3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2174552; DOI=10.1073/pnas.87.23.9088;
RA   Good P.J., Richter K., Dawid I.B.;
RT   "A nervous system-specific isotype of the beta subunit of Na+,K(+)-ATPase
RT   expressed during early development of Xenopus laevis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9088-9092(1990).
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       the beta-3 subunit is not known.
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:0000250|UniProtKB:P54709};
CC       Single-pass type II membrane protein.
CC   -!- TISSUE SPECIFICITY: Nervous system specific.
CC   -!- DEVELOPMENTAL STAGE: During embryogenesis rapid accumulation of beta 3
CC       mRNA begins at stage 14 (early neurula).
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; M37788; AAA49650.1; -; mRNA.
DR   PIR; A38411; A38411.
DR   AlphaFoldDB; P21188; -.
DR   SMR; P21188; -.
DR   MaxQB; P21188; -.
DR   Proteomes; UP000186698; Genome assembly.
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; Reference proteome; Signal-anchor; Sodium;
KW   Sodium transport; Sodium/potassium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..277
FT                   /note="Sodium/potassium-transporting ATPase subunit beta-3"
FT                   /id="PRO_0000219112"
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..277
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        127..144
FT                   /evidence="ECO:0000250"
FT   DISULFID        154..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        191..248
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   277 AA;  31570 MW;  C4A541270555FE5A CRC64;
     MAKEENKGSE QSGSDWKQFI YNPQKGEFMG RTASSWALIL LFYLVFYGFL AGLFTLTMWV
     MLQTLDDSVP KYRDRVSSPG LMISPKSAGL EIKFSRSKTQ SYMEYVQTLN TFLAPYNDSI
     QAKNEFCPPG LYFDQDEEVE KKTCQFNRTS LGICSGIEDP MFGYGEGKPC VIVKINRIIG
     LKPEGNPKIN CTSKTEDVNL QYFPDNGKID LMYFPYYGKK THVNYVQPVV AVKISPSNFT
     SEEIAVECKI HGSRNLKNED ERDKFLGRVT FKVKITE
 
 
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