AT1B1_ARTSF
ID AT1B1_ARTSF Reviewed; 315 AA.
AC P25169;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta;
DE AltName: Full=Sodium/potassium-dependent ATPase beta subunit;
OS Artemia franciscana (Brine shrimp) (Artemia sanfranciscana).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Anostraca; Artemiidae; Artemia.
OX NCBI_TaxID=6661;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2167242; DOI=10.1016/0014-5793(90)81162-h;
RA Bhattacharyya K.K., Bergstroem E.E., Hokin L.E.;
RT "Molecular cloning of the beta-subunit of the Na,K-ATPase in the brine
RT shrimp, Artemia. The cDNA-derived amino acid sequence shows low homology
RT with the beta-subunits of vertebrates except in the single transmembrane
RT and the carboxy-terminal domains.";
RL FEBS Lett. 269:233-238(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 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 -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; X55780; CAA39301.1; -; mRNA.
DR AlphaFoldDB; P25169; -.
DR SMR; P25169; -.
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 PROSITE; PS00390; ATPASE_NA_K_BETA_1; 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..315
FT /note="Sodium/potassium-transporting ATPase subunit beta"
FT /id="PRO_0000219113"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 145..157
FT /evidence="ECO:0000250"
FT DISULFID 168..182
FT /evidence="ECO:0000250"
FT DISULFID 233..290
FT /evidence="ECO:0000250"
SQ SEQUENCE 315 AA; 35955 MW; 787BAA38F99566E8 CRC64;
MADKKPDEQF VGSGPKETKW QSFKGFVWNS ETSQFMGRTA GSWAKITIFY VIFYTLLAGF
FAGMLMIFYQ TLDFKIPKWQ NKDSLIGANP GLGFRPMPPE AQVDSTLIQF KHGIKGDWQY
WVHSLTEFLE PYETLTSSGQ EFTNCDFDKP PQEGKACNFN VELLGDHCTK ENNFGYELGK
PCVLIKLTDF GWRPEVYNSS AEVPEDMPAD LKSYIKDIET GNKTHMNMVW LSCEGETAND
KEKIGTITYT PFRGFPAYYY PYLNVPGYLT PVVALQFGSL QNGQAVNVEC KAWANNISRD
RQRRLGSVHF EIRMD