ID ATP4B_CANLF Reviewed; 290 AA. AC P33704; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 04-NOV-2026, entry version 134. 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 Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Stomach; RX PubMed=8250881; DOI=10.1006/bbrc.1993.2385; RA Song I., Mortell M.P., Gantz I., Brown D.R., Yamada T.; RT "Molecular cloning and structural analysis of canine gastric H+,K(+)- RT ATPase."; RL Biochem. Biophys. Res. Commun. 196:1240-1247(1993). 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 -!- 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; M76486; AAA16895.1; -; mRNA. DR PIR; JN0904; JN0904. DR RefSeq; XP_038287465.1; XM_038431537.1. DR RefSeq; XP_038312712.1; XM_038456784.1. DR RefSeq; XP_038426059.1; XM_038570131.1. DR SMR; P33704; -. DR STRING; 9615.ENSCAFP00000009569; -. DR GlyCosmos; P33704; 7 sites, No reported glycans. DR PaxDb; 9615-ENSCAFP00000009569; -. DR Ensembl; ENSCAFT00000010321; ENSCAFP00000009569; ENSCAFG00000006390. DR Ensembl; ENSCAFT00030041336; ENSCAFP00030036061; ENSCAFG00030022490. DR Ensembl; ENSCAFT00040020199; ENSCAFP00040017521; ENSCAFG00040010941. DR Ensembl; ENSCAFT00805042782; ENSCAFP00805033484; ENSCAFG00805023647. DR Ensembl; ENSCAFT00845047780.1; ENSCAFP00845037489.1; ENSCAFG00845027108.1. DR GeneID; 404020; -. DR KEGG; cfa:404020; -. DR CTD; 496; -. DR VEuPathDB; HostDB:ENSCAFG00845027108; -. DR VGNC; VGNC:38263; ATP4B. DR eggNOG; KOG3927; Eukaryota. DR GeneTree; ENSGT01030000234579; -. DR InParanoid; P33704; -. DR OMA; ACAFPQS; -. DR OrthoDB; 5912413at2759; -. DR Reactome; R-CFA-936837; Ion transport by P-type ATPases. DR Bgee; ENSCAFG00000006390; Expressed in stomach and 4 other cell types or tissues. DR FunFam; 1.20.5.170:FF:000061; Sodium/potassium-transporting ATPase subunit beta; 1. DR FunFam; 2.60.40.1660:FF:000006; Sodium/potassium-transporting ATPase subunit beta; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 2.60.40.1660; Na, k-atpase alpha subunit; 1. DR InterPro; IPR000402; Na/K_ATPase_sub_beta. DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf. DR PANTHER; PTHR11523:SF11; POTASSIUM-TRANSPORTING ATPASE SUBUNIT BETA; 1. DR PANTHER; PTHR11523; SODIUM/POTASSIUM-DEPENDENT ATPASE BETA SUBUNIT; 1. DR Pfam; PF00287; Na_K-ATPase; 1. DR NCBIfam; TIGR01107; Na_K_ATPase_bet; 1. DR PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1. DR PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. 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:0030007; P:intracellular potassium ion homeostasis; IBA:GO_Central. DR GO; GO:0006883; P:intracellular sodium ion homeostasis; IBA:GO_Central. DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central. DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central. DR Proteomes; UP000805418; Chromosome 22. DR AlphaFoldDB; P33704; -. DR FunCoup; P33704; 2. 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..290 FT /note="Potassium-transporting ATPase subunit beta" FT /id="PRO_0000219090" 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..290 FT /note="Extracellular" FT /evidence="ECO:0000255" FT REGION 194..290 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 221 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..262 FT /evidence="ECO:0000250|UniProtKB:P18434" SQ SEQUENCE 290 AA; 33481 MW; 51B9548362A94FC6 CRC64; MAALQEKKSC SQRMEEFQRY CWNPDTGQML GRTLSRWVWI SLYYVAFYVV MTGIFALCIY TLMCTLDPYT PDYQDQLKSP GVTLRPDVYG EKGLDISYNV SDNRTWVDLV NILHNFLEGY SPTSQEDNIN CTSEKYFFQD VFGAPNHTKF SCKFMADMLQ NCSGLTDPNF GFAEGKPCFI IKMNRIVNFL PSNSTAPRAD CTFLDQHKDD RPLQVEYYPP NGTFSLRYFP YYGKKAQPHY SNPLVAAKLL NVPRNTEVLI VCKILADYVT FDNPHDPYEG KVEFKLTIQQ //