ATP4B_RAT
ID ATP4B_RAT Reviewed; 294 AA.
AC P18598;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Potassium-transporting ATPase subunit beta;
DE AltName: Full=Gastric H(+)/K(+) ATPase subunit beta;
DE AltName: Full=Proton pump beta chain;
GN Name=Atp4b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Stomach;
RX PubMed=2165052; DOI=10.1016/s0021-9258(19)38317-6;
RA Shull G.E.;
RT "cDNA cloning of the beta-subunit of the rat gastric H,K-ATPase.";
RL J. Biol. Chem. 265:12123-12126(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1663070; DOI=10.1016/0888-7543(91)90131-w;
RA Newman P.R., Shull G.E.;
RT "Rat gastric H,K-ATPase beta-subunit gene: intron/exon organization,
RT identification of multiple transcription initiation sites, and analysis of
RT the 5'-flanking region.";
RL Genomics 11:252-262(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gastric mucosa;
RX PubMed=1978834; DOI=10.1016/s0021-9258(17)45454-8;
RA Canfield V.A., Okamoto C.T., Chow D., Dorfman J., Gros P., Forte J.G.,
RA Levenson R.;
RT "Cloning of the H,K-ATPase beta subunit. Tissue-specific expression,
RT chromosomal assignment, and relationship to Na,K-ATPase beta subunits.";
RL J. Biol. Chem. 265:19878-19884(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1657972; DOI=10.1016/s0021-9258(18)54678-0;
RA Maeda M., Oshiman K.I., Tamura S., Kaya S., Mahmood S., Reuben M.A.,
RA Lasater L.S., Sachs G., Futai M.;
RT "The rat H+/K(+)-ATPase beta subunit gene and recognition of its control
RT region by gastric DNA binding protein.";
RL J. Biol. Chem. 266:21584-21588(1991).
CC -!- FUNCTION: The beta subunit of the gastric H(+)/K(+) ATPase pump which
CC transports H(+) ions in exchange for K(+) ions across the apical
CC membrane of parietal cells. Plays a structural and regulatory role in
CC the assembly and membrane targeting of a functionally active pump (By
CC similarity). Within a transport cycle, the transfer of a H(+) ion
CC across the membrane is coupled to ATP hydrolysis and is associated with
CC a transient phosphorylation of the alpha subunit that shifts the pump
CC conformation from inward-facing (E1) to outward-facing state (E2).
CC Interacts with the phosphorylation domain of the alpha subunit and
CC functions as a ratchet, stabilizing the lumenal-open E2 conformation
CC and preventing the reverse reaction of the transport cycle (By
CC similarity). {ECO:0000250|UniProtKB:P18597,
CC ECO:0000250|UniProtKB:P19156}.
CC -!- SUBUNIT: The ATPase pump is composed of two subunits: alpha (catalytic)
CC and beta (regulatory). Interacts with alpha subunit ATP12A; this
CC interaction is required for the formation of a functionally active pump
CC and targeting at the plasma membrane (By similarity). Interacts (via N-
CC terminus) with alpha subunit ATP4A (via the P-domain) (By similarity).
CC {ECO:0000250|UniProtKB:P18434, ECO:0000250|UniProtKB:P18597}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P20648}; Single-pass type II membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P18597}; Single-
CC pass type II membrane protein {ECO:0000255}. Note=Localized in the
CC apical canalicular membrane of parietal cells.
CC {ECO:0000250|UniProtKB:P20648}.
CC -!- TISSUE SPECIFICITY: Stomach. {ECO:0000269|PubMed:2165052}.
CC -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC and mediates cell adhesion properties. {ECO:0000250|UniProtKB:P51164}.
CC -!- PTM: N-glycosylation is necessary for assembly and functional
CC expression of the pump at the plasma membrane.
CC {ECO:0000250|UniProtKB:P18597}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; L34666; AAA41332.1; -; Genomic_DNA.
DR EMBL; L34661; AAA41332.1; JOINED; Genomic_DNA.
DR EMBL; L34662; AAA41332.1; JOINED; Genomic_DNA.
DR EMBL; L34663; AAA41332.1; JOINED; Genomic_DNA.
DR EMBL; L34664; AAA41332.1; JOINED; Genomic_DNA.
DR EMBL; L34665; AAA41332.1; JOINED; Genomic_DNA.
DR EMBL; S76404; AAB21120.1; -; Genomic_DNA.
DR EMBL; M55655; AAA41330.1; -; mRNA.
DR EMBL; M35535; AAA63482.1; -; mRNA.
DR PIR; A41199; A41199.
DR RefSeq; NP_036642.2; NM_012510.2.
DR AlphaFoldDB; P18598; -.
DR SMR; P18598; -.
DR ComplexPortal; CPX-2183; Hydrogen:potassium-exchanging ATPase complex.
DR STRING; 10116.ENSRNOP00000025957; -.
DR BindingDB; P18598; -.
DR ChEMBL; CHEMBL4771; -.
DR GlyGen; P18598; 7 sites.
DR iPTMnet; P18598; -.
DR PhosphoSitePlus; P18598; -.
DR PaxDb; P18598; -.
DR PRIDE; P18598; -.
DR Ensembl; ENSRNOT00000025958; ENSRNOP00000025957; ENSRNOG00000018543.
DR GeneID; 24217; -.
DR KEGG; rno:24217; -.
DR UCSC; RGD:2178; rat.
DR CTD; 496; -.
DR RGD; 2178; Atp4b.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_1_1_1; -.
DR InParanoid; P18598; -.
DR OMA; CKILADH; -.
DR OrthoDB; 998086at2759; -.
DR PhylomeDB; P18598; -.
DR TreeFam; TF314618; -.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR PRO; PR:P18598; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000018543; Expressed in stomach and 13 other tissues.
DR Genevisible; P18598; RN.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IBA:GO_Central.
DR GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:0045851; P:pH reduction; IMP:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
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 adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrogen ion transport; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..294
FT /note="Potassium-transporting ATPase subunit beta"
FT /id="PRO_0000219095"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 194..294
FT /note="immunoglobulin-like"
FT /evidence="ECO:0000250"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P18597"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P18597"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P18597"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P18597"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P18597"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P18597"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P18597"
FT DISULFID 131..152
FT /evidence="ECO:0000250|UniProtKB:P18434"
FT DISULFID 162..178
FT /evidence="ECO:0000250|UniProtKB:P18434"
FT DISULFID 201..266
FT /evidence="ECO:0000250|UniProtKB:P18434"
FT CONFLICT 136
FT /note="Y -> H (in Ref. 1; AAA41330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 33689 MW; EE640D88835AD8AF CRC64;
MAALQEKKSC SQRMAEFRQY CWNPDTGQML GRTPARWVWI SLYYAAFYVV MTGLFALCIY
VLMQTIDPYT PDYQDQLKSP GVTLRPDVYG ERGLQISYNI SENSSWAGLT HTLHSFLAGY
TPASQQDSIN CSSEKYFFQE TFSAPNHTKF SCKFTADMLQ NCSGLVDPSF GFEEGKPCFI
IKMNRIVKFL PSNNTAPRVD CTFQDDPQKP RKDIEPLQVQ YYPPNGTFSL HYFPYYGKKA
QPHYSNPLVA AKFLNVPKNT QVLIVCKIMA DHVTFDNPHD PYEGKVEFKL TIQK
