ATP4B_CANLF
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 03-AUG-2022, entry version 117.
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}.
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DR EMBL; M76486; AAA16895.1; -; mRNA.
DR PIR; JN0904; JN0904.
DR RefSeq; NP_001003328.1; NM_001003328.1.
DR AlphaFoldDB; P33704; -.
DR SMR; P33704; -.
DR STRING; 9615.ENSCAFP00000009569; -.
DR PaxDb; P33704; -.
DR PRIDE; P33704; -.
DR Ensembl; ENSCAFT00030041336; ENSCAFP00030036061; ENSCAFG00030022490.
DR Ensembl; ENSCAFT00040020199; ENSCAFP00040017521; ENSCAFG00040010941.
DR Ensembl; ENSCAFT00845047780; ENSCAFP00845037489; ENSCAFG00845027108.
DR GeneID; 404020; -.
DR CTD; 496; -.
DR VEuPathDB; HostDB:ENSCAFG00845027108; -.
DR VGNC; VGNC:38263; ATP4B.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR InParanoid; P33704; -.
DR OrthoDB; 998086at2759; -.
DR Proteomes; UP000002254; Chromosome 22.
DR Bgee; ENSCAFG00000006390; Expressed in stomach and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
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: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 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..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
