ATP4B_HUMAN
ID ATP4B_HUMAN Reviewed; 291 AA.
AC P51164; B1B0N8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
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 {ECO:0000312|HGNC:HGNC:820};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1656976; DOI=10.1016/s0006-291x(05)81251-3;
RA Ma J.-Y., Song Y.-H., Sjoestrand S.E., Rask L., Maardh S.;
RT "cDNA cloning of the beta-subunit of the human gastric H,K-ATPase.";
RL Biochem. Biophys. Res. Commun. 180:39-45(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RC TISSUE=Liver;
RX PubMed=9315713; DOI=10.1016/s0014-5793(97)01017-x;
RA Yoshida T., Sato R., Mahmood S., Kawasaki S., Futai M., Maeda M.;
RT "GATA-6 DNA binding protein expressed in human gastric adenocarcinoma MKN45
RT cells.";
RL FEBS Lett. 414:333-337(1997).
RN [6]
RP FUNCTION, AND DOMAIN IMMUNOGLOBULIN-LIKE.
RX PubMed=19694409; DOI=10.1021/bi900868e;
RA Bab-Dinitz E., Albeck S., Peleg Y., Brumfeld V., Gottschalk K.E.,
RA Karlish S.J.;
RT "A C-terminal lobe of the beta subunit of Na,K-ATPase and H,K-ATPase
RT resembles cell adhesion molecules.";
RL Biochemistry 48:8684-8691(2009).
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 -!- INTERACTION:
CC P51164; O95273: CCNDBP1; NbExp=3; IntAct=EBI-3904463, EBI-748961;
CC P51164; O15529: GPR42; NbExp=3; IntAct=EBI-3904463, EBI-18076404;
CC P51164; Q9NQZ6: ZC4H2; NbExp=3; IntAct=EBI-3904463, EBI-747993;
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 -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC and mediates cell adhesion properties. {ECO:0000269|PubMed:19694409}.
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; M75110; AAA35987.1; -; mRNA.
DR EMBL; BX537316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471085; EAX09221.1; -; Genomic_DNA.
DR EMBL; BC029059; AAH29059.1; -; mRNA.
DR EMBL; AB008783; BAA23425.1; -; Genomic_DNA.
DR CCDS; CCDS9539.1; -.
DR PIR; JH0480; JH0480.
DR RefSeq; NP_000696.1; NM_000705.3.
DR AlphaFoldDB; P51164; -.
DR SMR; P51164; -.
DR BioGRID; 106986; 7.
DR ComplexPortal; CPX-2160; Hydrogen:potassium-exchanging ATPase complex.
DR CORUM; P51164; -.
DR IntAct; P51164; 6.
DR STRING; 9606.ENSP00000334216; -.
DR BindingDB; P51164; -.
DR ChEMBL; CHEMBL2095173; -.
DR DrugBank; DB05351; Dexlansoprazole.
DR DrugBank; DB13620; Potassium gluconate.
DR DrugCentral; P51164; -.
DR TCDB; 3.A.3.1.2; the p-type atpase (p-atpase) superfamily.
DR GlyGen; P51164; 7 sites.
DR iPTMnet; P51164; -.
DR PhosphoSitePlus; P51164; -.
DR BioMuta; ATP4B; -.
DR DMDM; 1703461; -.
DR jPOST; P51164; -.
DR MassIVE; P51164; -.
DR PaxDb; P51164; -.
DR PeptideAtlas; P51164; -.
DR PRIDE; P51164; -.
DR ProteomicsDB; 56294; -.
DR Antibodypedia; 25980; 277 antibodies from 30 providers.
DR DNASU; 496; -.
DR Ensembl; ENST00000335288.5; ENSP00000334216.3; ENSG00000186009.5.
DR Ensembl; ENST00000672885.1; ENSP00000500492.1; ENSG00000288359.1.
DR GeneID; 496; -.
DR KEGG; hsa:496; -.
DR MANE-Select; ENST00000335288.5; ENSP00000334216.3; NM_000705.4; NP_000696.1.
DR UCSC; uc001vtz.5; human.
DR CTD; 496; -.
DR DisGeNET; 496; -.
DR GeneCards; ATP4B; -.
DR HGNC; HGNC:820; ATP4B.
DR HPA; ENSG00000186009; Tissue enriched (stomach).
DR MIM; 137217; gene.
DR neXtProt; NX_P51164; -.
DR OpenTargets; ENSG00000186009; -.
DR PharmGKB; PA25114; -.
DR VEuPathDB; HostDB:ENSG00000186009; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_1_1_1; -.
DR InParanoid; P51164; -.
DR OMA; CKILADH; -.
DR PhylomeDB; P51164; -.
DR TreeFam; TF314618; -.
DR BioCyc; MetaCyc:G66-33511-MON; -.
DR PathwayCommons; P51164; -.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; P51164; -.
DR BioGRID-ORCS; 496; 5 hits in 1059 CRISPR screens.
DR GenomeRNAi; 496; -.
DR Pharos; P51164; Tclin.
DR PRO; PR:P51164; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P51164; protein.
DR Bgee; ENSG00000186009; Expressed in body of stomach and 68 other tissues.
DR Genevisible; P51164; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:1901363; F:heterocyclic compound binding; IEA:Ensembl.
DR GO; GO:0008900; F:P-type potassium:proton transporter activity; TAS:ProtInc.
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; IEA:Ensembl.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
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 1: Evidence at protein 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..291
FT /note="Potassium-transporting ATPase subunit beta"
FT /id="PRO_0000219091"
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..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 194..291
FT /note="immunoglobulin-like"
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 222
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..263
FT /evidence="ECO:0000250|UniProtKB:P18434"
SQ SEQUENCE 291 AA; 33367 MW; 573F6D729CED1C3D CRC64;
MAALQEKKTC GQRMEEFQRY CWNPDTGQML GRTLSRWVWI SLYYVAFYVV MTGLFALCLY
VLMQTVDPYT PDYQDQLRSP GVTLRPDVYG EKGLEIVYNV SDNRTWADLT QTLHAFLAGY
SPAAQEDSIN CTSEQYFFQE SFRAPNHTKF SCKFTADMLQ NCSGLADPNF GFEEGKPCFI
IKMNRIVKFL PSNGSAPRVD CAFLDQPREL GQPLQVKYYP PNGTFSLHYF PYYGKKAQPH
YSNPLVAAKL LNIPRNAEVA IVCKVMAEHV TFNNPHDPYE GKVEFKLKIE K
