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