ID   AT1B4_XENLA             Reviewed;         314 AA.
AC   Q202B1;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Protein ATP1B4;
DE   AltName: Full=X,K-ATPase subunit beta-m;
DE   AltName: Full=X/potassium-transporting ATPase subunit beta-m;
GN   Name=atp1b4;
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], FUNCTION, SUBUNIT, GLYCOSYLATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=17592128; DOI=10.1073/pnas.0704809104;
RA   Pestov N.B., Ahmad N., Korneenko T.V., Zhao H., Radkov R., Schaer D.,
RA   Roy S., Bibert S., Geering K., Modyanov N.N.;
RT   "Evolution of Na,K-ATPase betam-subunit into a coregulator of transcription
RT   in placental mammals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:11215-11220(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000269|PubMed:17592128}.
CC   -!- SUBUNIT: Composed of two subunits: alpha (catalytic) and beta
CC       (accessory). {ECO:0000269|PubMed:17592128}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, liver, lung, kidney,
CC       heart, brain and skin. {ECO:0000269|PubMed:17592128}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:17592128}.
CC   -!- MISCELLANEOUS: Its function as a Na,K-ATPase beta-subunit will be lost
CC       in placental mammals.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; DQ413025; ABD72588.1; -; mRNA.
DR   EMBL; BC170017; AAI70017.1; -; mRNA.
DR   EMBL; BC170019; AAI70019.1; -; mRNA.
DR   RefSeq; NP_001089970.1; NM_001096501.1.
DR   RefSeq; XP_018084746.1; XM_018229257.1.
DR   AlphaFoldDB; Q202B1; -.
DR   SMR; Q202B1; -.
DR   GeneID; 735041; -.
DR   KEGG; xla:735041; -.
DR   CTD; 735041; -.
DR   Xenbase; XB-GENE-975980; atp1b4.L.
DR   OMA; GVQYDTH; -.
DR   OrthoDB; 998086at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 735041; Expressed in muscle tissue and 4 other tissues.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:InterPro.
DR   GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
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; PS00391; ATPASE_NA_K_BETA_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..314
FT                   /note="Protein ATP1B4"
FT                   /id="PRO_0000393965"
FT   TOPO_DOM        1..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..314
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        188
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        160..179
FT                   /evidence="ECO:0000250"
FT   DISULFID        189..205
FT                   /evidence="ECO:0000250"
FT   DISULFID        228..287
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  36129 MW;  A9BACD444F63B319 CRC64;
     MATTAGEQAN YLQSADSMSD GRQHHPEEAG EKKQEEQKKS WGEWLQDLKI FIWNPEKKEV
     LGRDKKSWAL ILLFYFILYC FLAGLFALCI YGLLATISPY VPTYRDRVFP PGLTIRPQFN
     ALYFSFNPSD RSTWSSHAES LNTFLEDYND EIQQEKNLEC TPGKYFFQPG EDHEERKACQ
     FRRSLLKNCS GIEDPTFGFA QGKPCILLKM NRIVGYQAGS GIPIYVTCEI LKADASYLGP
     VNFYPSDKFD LMYYPYYGKL THVNYTSPLI AMQFTEVKNN QDINIQCKIN GKDIISDHDK
     DRFLGRVAFT LHIG