ATP4B_MOUSE
ID ATP4B_MOUSE Reviewed; 294 AA.
AC P50992; Q9D6S3; Q9D6T2; Q9D6Y2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=1370459; DOI=10.1016/s0021-9258(18)48410-4;
RA Morley G.P., Callaghan J.M., Rose J.B., Toh H., Gleeson P.A.,
RA van Driel I.R.;
RT "The mouse gastric H,K-ATPase beta subunit. Gene structure and co-ordinate
RT expression with the alpha subunit during ontogeny.";
RL J. Biol. Chem. 267:1165-1174(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=1654563; DOI=10.1073/pnas.88.18.8247;
RA Canfield V.A., Levenson R.;
RT "Structural organization and transcription of the mouse gastric H+, K(+)-
RT ATPase beta subunit gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8247-8252(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=10764766; DOI=10.1074/jbc.m001558200;
RA Spicer Z., Miller M.L., Andringa A., Riddle T.M., Duffy J.J.,
RA Doetschman T., Shull G.E.;
RT "Stomachs of mice lacking the gastric H,K-ATPase alpha -subunit have
RT achlorhydria, abnormal parietal cells, and ciliated metaplasia.";
RL J. Biol. Chem. 275:21555-21565(2000).
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: Expressed in parietal cells (at protein level).
CC {ECO:0000269|PubMed:10764766}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M80251; AAA37270.1; -; Genomic_DNA.
DR EMBL; M80247; AAA37270.1; JOINED; Genomic_DNA.
DR EMBL; M80248; AAA37270.1; JOINED; Genomic_DNA.
DR EMBL; M80249; AAA37270.1; JOINED; Genomic_DNA.
DR EMBL; M80250; AAA37270.1; JOINED; Genomic_DNA.
DR EMBL; M64688; AAA37269.1; -; Genomic_DNA.
DR EMBL; M64685; AAA37269.1; JOINED; Genomic_DNA.
DR EMBL; M64686; AAA37269.1; JOINED; Genomic_DNA.
DR EMBL; M64687; AAA37269.1; JOINED; Genomic_DNA.
DR EMBL; AK008180; BAB25514.1; -; mRNA.
DR EMBL; AK009499; BAB26326.1; -; mRNA.
DR EMBL; AK009832; BAB26530.1; ALT_SEQ; mRNA.
DR EMBL; AK009994; BAB26632.1; -; mRNA.
DR EMBL; AK010003; BAB26635.1; -; mRNA.
DR EMBL; AK010030; BAB26654.1; -; mRNA.
DR EMBL; AK010049; BAB26665.1; -; mRNA.
DR CCDS; CCDS22111.1; -.
DR PIR; A40993; A40993.
DR RefSeq; NP_033854.1; NM_009724.2.
DR AlphaFoldDB; P50992; -.
DR SMR; P50992; -.
DR ComplexPortal; CPX-3075; Hydrogen:potassium-exchanging ATPase complex.
DR STRING; 10090.ENSMUSP00000033826; -.
DR GlyGen; P50992; 7 sites.
DR PhosphoSitePlus; P50992; -.
DR PaxDb; P50992; -.
DR PeptideAtlas; P50992; -.
DR PRIDE; P50992; -.
DR ProteomicsDB; 277074; -.
DR Antibodypedia; 25980; 277 antibodies from 30 providers.
DR Ensembl; ENSMUST00000033826; ENSMUSP00000033826; ENSMUSG00000031449.
DR GeneID; 11945; -.
DR KEGG; mmu:11945; -.
DR UCSC; uc009kxu.1; mouse.
DR CTD; 496; -.
DR MGI; MGI:88114; Atp4b.
DR VEuPathDB; HostDB:ENSMUSG00000031449; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_1_1_1; -.
DR InParanoid; P50992; -.
DR OMA; CKILADH; -.
DR OrthoDB; 998086at2759; -.
DR PhylomeDB; P50992; -.
DR TreeFam; TF314618; -.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 11945; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Atp4b; mouse.
DR PRO; PR:P50992; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P50992; protein.
DR Bgee; ENSMUSG00000031449; Expressed in epithelium of stomach and 46 other tissues.
DR ExpressionAtlas; P50992; baseline and differential.
DR Genevisible; P50992; MM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0008900; F:P-type potassium:proton transporter activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; ISO:MGI.
DR GO; GO:0010155; P:regulation of proton transport; ISO:MGI.
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..294
FT /note="Potassium-transporting ATPase subunit beta"
FT /id="PRO_0000219092"
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 33
FT /note="T -> P (in Ref. 3; BAB26635)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..215
FT /note="TE -> IK (in Ref. 3; BAB26654)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="Q -> L (in Ref. 3; BAB26654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 33566 MW; EAB8526C4C52431D CRC64;
MAALQEKKSC SQRMAEFRHY CWNPDTGQML GRTPARWVWI SLYYAGFYVV MTGLFALCIY
VLMQTIDPYT PDYQDQLKSP GVTLRPDVYG ERGLKISYNV SENSSWAGLT HTLHSFLAGY
TPASQQDSIN CTSEKYFFQE SFAAPNHTKF SCKFTADMLQ NCSGLADPSF GFEEGKPCFI
IKMNRIVKFL PSNNTAPRVD CTFQDDPQKP RKDTEPLQVE YYPPNGTFSL HYFPYYGKKA
QPHYSNPLVA AKLLNVPKNM QVSIVCKILA DHVTFNNPHD PYEGKVEFKL TIQK
