ATP4B_PIG
ID ATP4B_PIG Reviewed; 290 AA.
AC P18434;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, 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;
DE AltName: Full=gp60-90;
GN Name=ATP4B;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1974721; DOI=10.1073/pnas.87.16.6418;
RA Toh B.-H., Gleeson P.A., Simpson R.J., Moritz R.L., Callaghan J.M.,
RA Goldkorn I., Jones C.M., Martinelli T.M., Mu F.-T., Humphris D.C.,
RA Pettitt J.M., Mori Y., Masuda T., Sobieszczuk P., Weinstock J.,
RA Mantamadiotis T., Baldwin G.S.;
RT "The 60- to 90-kDa parietal cell autoantigen associated with autoimmune
RT gastritis is a beta subunit of the gastric H+/K(+)-ATPase (proton pump).";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6418-6422(1990).
RN [2]
RP PROTEIN SEQUENCE OF 175-190 AND 216-245.
RX PubMed=2159787; DOI=10.1021/bi00455a016;
RA Hall K., Perez G., Anderson D., Gutierrez C., Munson K., Hersey S.J.,
RA Kaplan J.H., Sachs G.;
RT "Location of the carbohydrates present in the HK-ATPase vesicles isolated
RT from hog gastric mucosa.";
RL Biochemistry 29:701-706(1990).
RN [3]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.50 ANGSTROMS), FUNCTION, INTERACTION
RP WITH ATP4A, AND MUTAGENESIS OF 4-LEU--LYS-8.
RX PubMed=19387495; DOI=10.1038/emboj.2009.102;
RA Abe K., Tani K., Nishizawa T., Fujiyoshi Y.;
RT "Inter-subunit interaction of gastric H+,K+-ATPase prevents reverse
RT reaction of the transport cycle.";
RL EMBO J. 28:1637-1643(2009).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS) IN COMPLEX WITH ATP4A AND
RP INHIBITOR, SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX PubMed=21224846; DOI=10.1038/ncomms1154;
RA Abe K., Tani K., Fujiyoshi Y.;
RT "Conformational rearrangement of gastric H(+),K(+)-ATPase induced by an
RT acid suppressant.";
RL Nat. Commun. 2:155-155(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-290 IN COMPLEX WITH ATP4A,
RP DISULFIDE BOND, AND FUNCTION.
RX PubMed=29618813; DOI=10.1038/s41586-018-0003-8;
RA Abe K., Irie K., Nakanishi H., Suzuki H., Fujiyoshi Y.;
RT "Crystal structures of the gastric proton pump.";
RL Nature 556:214-218(2018).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-290, AND DISULFIDE BOND.
RX PubMed=31436534; DOI=10.7554/elife.47701;
RA Yamamoto K., Dubey V., Irie K., Nakanishi H., Khandelia H., Fujiyoshi Y.,
RA Abe K.;
RT "A single K(+)-binding site in the crystal structure of the gastric proton
RT pump.";
RL Elife 8:0-0(2019).
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
CC (PubMed:29618813, PubMed:19387495). {ECO:0000250|UniProtKB:P18597,
CC ECO:0000269|PubMed:19387495, ECO:0000269|PubMed:29618813}.
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) (PubMed:19387495,
CC PubMed:29618813). {ECO:0000250|UniProtKB:P18597,
CC ECO:0000269|PubMed:19387495, ECO:0000269|PubMed:29618813}.
CC -!- INTERACTION:
CC P18434; P19156: ATP4A; NbExp=2; IntAct=EBI-9009115, EBI-8803609;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P20648}; Single-pass type II membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:21224846}; Single-pass
CC type II membrane protein {ECO:0000255}. Note=Localized in the apical
CC canalicular membrane of parietal cells. {ECO:0000250|UniProtKB:P20648}.
CC -!- TISSUE SPECIFICITY: Stomach.
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 -!- DISEASE: Note=Parietal cell autoantigen associated with autoimmune
CC gastritis. {ECO:0000269|PubMed:1974721}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; M35497; AAA31040.1; -; mRNA.
DR PIR; A36021; A36021.
DR RefSeq; NP_001001258.1; NM_001001258.1.
DR RefSeq; XP_005653896.1; XM_005653839.2.
DR PDB; 2XZB; EM; 7.00 A; B=1-290.
DR PDB; 2YN9; EM; 8.00 A; B=1-290.
DR PDB; 3IXZ; EM; 6.50 A; B=1-290.
DR PDB; 4UX1; EM; 8.00 A; B=1-290.
DR PDB; 4UX2; EM; 7.00 A; B=1-290.
DR PDB; 5Y0B; EM; 6.70 A; B=1-290.
DR PDB; 5YLU; X-ray; 2.80 A; B=2-290.
DR PDB; 5YLV; X-ray; 2.80 A; B=2-290.
DR PDB; 6JXH; X-ray; 2.50 A; B=2-290.
DR PDB; 6JXI; X-ray; 2.60 A; B=2-286.
DR PDB; 6JXJ; X-ray; 2.50 A; B=2-290.
DR PDB; 6JXK; X-ray; 4.30 A; B/F=2-290.
DR PDB; 7EFL; X-ray; 3.40 A; B=37-290.
DR PDB; 7EFM; X-ray; 3.20 A; B=30-290.
DR PDB; 7EFN; X-ray; 3.20 A; B=30-290.
DR PDB; 7ET1; EM; 2.60 A; B=29-290.
DR PDB; 7W47; X-ray; 3.00 A; B=1-290.
DR PDB; 7W48; X-ray; 3.50 A; B=1-290.
DR PDB; 7W49; X-ray; 3.10 A; B=1-290.
DR PDB; 7W4A; EM; 2.76 A; B=1-290.
DR PDBsum; 2XZB; -.
DR PDBsum; 2YN9; -.
DR PDBsum; 3IXZ; -.
DR PDBsum; 4UX1; -.
DR PDBsum; 4UX2; -.
DR PDBsum; 5Y0B; -.
DR PDBsum; 5YLU; -.
DR PDBsum; 5YLV; -.
DR PDBsum; 6JXH; -.
DR PDBsum; 6JXI; -.
DR PDBsum; 6JXJ; -.
DR PDBsum; 6JXK; -.
DR PDBsum; 7EFL; -.
DR PDBsum; 7EFM; -.
DR PDBsum; 7EFN; -.
DR PDBsum; 7ET1; -.
DR PDBsum; 7W47; -.
DR PDBsum; 7W48; -.
DR PDBsum; 7W49; -.
DR PDBsum; 7W4A; -.
DR AlphaFoldDB; P18434; -.
DR SMR; P18434; -.
DR ComplexPortal; CPX-2195; Hydrogen:potassium-exchanging ATPase complex.
DR IntAct; P18434; 1.
DR STRING; 9823.ENSSSCP00000010209; -.
DR BindingDB; P18434; -.
DR ChEMBL; CHEMBL2538; -.
DR DrugCentral; P18434; -.
DR PaxDb; P18434; -.
DR PeptideAtlas; P18434; -.
DR Ensembl; ENSSSCT00000010481; ENSSSCP00000010209; ENSSSCG00000009561.
DR Ensembl; ENSSSCT00015006532; ENSSSCP00015002694; ENSSSCG00015004859.
DR Ensembl; ENSSSCT00025037061; ENSSSCP00025015510; ENSSSCG00025027365.
DR Ensembl; ENSSSCT00030011096; ENSSSCP00030004910; ENSSSCG00030008180.
DR Ensembl; ENSSSCT00035043522; ENSSSCP00035017407; ENSSSCG00035032852.
DR Ensembl; ENSSSCT00040026224; ENSSSCP00040011090; ENSSSCG00040019363.
DR Ensembl; ENSSSCT00045058795; ENSSSCP00045041137; ENSSSCG00045034353.
DR Ensembl; ENSSSCT00045058834; ENSSSCP00045041168; ENSSSCG00045034353.
DR Ensembl; ENSSSCT00050049928; ENSSSCP00050020855; ENSSSCG00050037103.
DR Ensembl; ENSSSCT00050049935; ENSSSCP00050020860; ENSSSCG00050037103.
DR Ensembl; ENSSSCT00055058033; ENSSSCP00055046428; ENSSSCG00055029233.
DR Ensembl; ENSSSCT00055058052; ENSSSCP00055046442; ENSSSCG00055029233.
DR Ensembl; ENSSSCT00060053134; ENSSSCP00060022633; ENSSSCG00060039283.
DR Ensembl; ENSSSCT00060053141; ENSSSCP00060022636; ENSSSCG00060039283.
DR Ensembl; ENSSSCT00065108712; ENSSSCP00065048656; ENSSSCG00065078438.
DR Ensembl; ENSSSCT00065108726; ENSSSCP00065048668; ENSSSCG00065078438.
DR Ensembl; ENSSSCT00070026294; ENSSSCP00070021829; ENSSSCG00070013475.
DR GeneID; 397131; -.
DR KEGG; ssc:397131; -.
DR CTD; 496; -.
DR VGNC; VGNC:85655; ATP4B.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_1_1_1; -.
DR InParanoid; P18434; -.
DR OMA; CKILADH; -.
DR OrthoDB; 998086at2759; -.
DR TreeFam; TF314618; -.
DR BRENDA; 7.2.2.19; 6170.
DR Reactome; R-SSC-936837; Ion transport by P-type ATPases.
DR EvolutionaryTrace; P18434; -.
DR PRO; PR:P18434; -.
DR Proteomes; UP000008227; Chromosome 11.
DR Proteomes; UP000314985; Chromosome 11.
DR Bgee; ENSSSCG00000009561; Expressed in heart and 8 other tissues.
DR Genevisible; P18434; SS.
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 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrogen ion transport; Ion transport;
KW Membrane; Potassium; Potassium transport; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..290
FT /note="Potassium-transporting ATPase subunit beta"
FT /id="PRO_0000219093"
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 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:0000269|PubMed:21224846,
FT ECO:0000269|PubMed:29618813, ECO:0000269|PubMed:31436534,
FT ECO:0007744|PDB:5YLU, ECO:0007744|PDB:6JXH"
FT DISULFID 162..178
FT /evidence="ECO:0000269|PubMed:29618813,
FT ECO:0000269|PubMed:31436534"
FT DISULFID 201..262
FT /evidence="ECO:0000269|PubMed:29618813,
FT ECO:0000269|PubMed:31436534"
FT MUTAGEN 4..8
FT /note="Missing: Has no effect on the forward reaction, but
FT substantially accelerates the reverse reaction of the
FT transport cycle."
FT /evidence="ECO:0000269|PubMed:19387495"
FT CONFLICT 185
FT /note="R -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 36..65
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5YLV"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 122..127
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:7ET1"
FT TURN 168..175
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5YLV"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:7EFL"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:7EFN"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 279..289
FT /evidence="ECO:0007829|PDB:6JXH"
SQ SEQUENCE 290 AA; 33076 MW; 90DAA9D5B8200590 CRC64;
MAALQEKKSC SQRMEEFQRY CWNPDTGQML GRTLSRWVWI SLYYVAFYVV MSGIFALCIY
VLMRTIDPYT PDYQDQLKSP GVTLRPDVYG EKGLDISYNV SDSTTWAGLA HTLHRFLAGY
SPAAQEGSIN CTSEKYFFQE SFLAPNHTKF SCKFTADMLQ NCSGRPDPTF GFAEGKPCFI
IKMNRIVKFL PGNSTAPRVD CAFLDQPRDG PPLQVEYFPA NGTYSLHYFP YYGKKAQPHY
SNPLVAAKLL NVPRNRDVVI VCKILAEHVS FDNPHDPYEG KVEFKLKIQK
