ATP4B_RABIT
ID ATP4B_RABIT Reviewed; 291 AA.
AC P18597;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2168558; DOI=10.1073/pnas.87.17.6767;
RA Reuben M.A., Lasater L.S., Sachs G.;
RT "Characterization of a beta subunit of the gastric H+/K(+)-transporting
RT ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6767-6771(1990).
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=7485470; DOI=10.1152/ajpcell.1995.269.4.c992;
RA Modyanov N.N., Mathews P.M., Grishin A.V., Beguin P., Beggah A.T.,
RA Rossier B.C., Horisberger J.D., Geering K.;
RT "Human ATP1AL1 gene encodes a ouabain-sensitive H-K-ATPase.";
RL Am. J. Physiol. 269:C992-C997(1995).
RN [3]
RP FUNCTION, INTERACTION WITH ATP4A, SUBCELLULAR LOCATION, GLYCOSYLATION AT
RP ASN-99; ASN-103; ASN-130; ASN-146; ASN-161; ASN-193 AND ASN-222, AND
RP MUTAGENESIS OF ASN-99; ASN-103; ASN-130; ASN-146; ASN-161; ASN-193 AND
RP ASN-222.
RX PubMed=10722662; DOI=10.1074/jbc.275.12.8324;
RA Asano S., Kawada K., Kimura T., Grishin A.V., Caplan M.J., Takeguchi N.;
RT "The roles of carbohydrate chains of the beta-subunit on the functional
RT expression of gastric H(+),K(+)-ATPase.";
RL J. Biol. Chem. 275:8324-8330(2000).
RN [4]
RP FUNCTION, INTERACTION WITH ATP4A, AND MUTAGENESIS OF CYS-10; CYS-21;
RP CYS-58; CYS-131; CYS-152; CYS-162; CYS-178; CYS-201 AND CYS-263.
RX PubMed=11909858; DOI=10.1074/jbc.m200523200;
RA Kimura T., Tabuchi Y., Takeguchi N., Asano S.;
RT "Mutational study on the roles of disulfide bonds in the beta-subunit of
RT gastric H+,K+-ATPase.";
RL J. Biol. Chem. 277:20671-20677(2002).
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 (PubMed:7485470, PubMed:10722662,
CC PubMed:11909858). Plays a structural and regulatory role in the
CC assembly and membrane targeting of a functionally active pump
CC (PubMed:7485470, PubMed:10722662, PubMed:11909858). Within a transport
CC cycle, the transfer of a H(+) ion across the membrane is coupled to ATP
CC hydrolysis and is associated with a transient phosphorylation of the
CC alpha subunit that shifts the pump conformation from inward-facing (E1)
CC to outward-facing state (E2) (By similarity). Interacts with the
CC phosphorylation domain of the alpha subunit and functions as a ratchet,
CC stabilizing the lumenal-open E2 conformation and preventing the reverse
CC reaction of the transport cycle (By similarity).
CC {ECO:0000250|UniProtKB:P19156, ECO:0000269|PubMed:10722662,
CC ECO:0000269|PubMed:11909858, ECO:0000269|PubMed:7485470}.
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 (PubMed:7485470). Interacts (via
CC N-terminus) with alpha subunit ATP4A (via the P-domain)
CC (PubMed:11909858, PubMed:10722662) (By similarity).
CC {ECO:0000250|UniProtKB:P18434, ECO:0000269|PubMed:10722662,
CC ECO:0000269|PubMed:11909858, ECO:0000269|PubMed:7485470}.
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:10722662}; 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 -!- 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:0000269|PubMed:10722662}.
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; M35544; AAA31256.1; -; mRNA.
DR PIR; A36051; A36051.
DR RefSeq; NP_001075758.1; NM_001082289.1.
DR AlphaFoldDB; P18597; -.
DR SMR; P18597; -.
DR BioGRID; 1172148; 3.
DR STRING; 9986.ENSOCUP00000021394; -.
DR DrugCentral; P18597; -.
DR Ensembl; ENSOCUT00000028473; ENSOCUP00000021394; ENSOCUG00000027254.
DR GeneID; 100009125; -.
DR KEGG; ocu:100009125; -.
DR CTD; 496; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_1_1_1; -.
DR InParanoid; P18597; -.
DR OMA; CKILADH; -.
DR OrthoDB; 998086at2759; -.
DR BRENDA; 7.2.2.19; 1749.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000027254; Expressed in adult mammalian kidney and 1 other tissue.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:InterPro.
DR GO; GO:0008900; F:P-type potassium:proton transporter activity; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0045851; P:pH reduction; IDA:MGI.
DR GO; GO:0010155; P:regulation of proton transport; IDA:MGI.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
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_0000219094"
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 /evidence="ECO:0000250"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10722662"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10722662"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10722662"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10722662"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10722662"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10722662"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10722662"
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"
FT MUTAGEN 10
FT /note="C->S: Has no effect on pump ATPase activity."
FT /evidence="ECO:0000269|PubMed:11909858"
FT MUTAGEN 21
FT /note="C->S: Has no effect on pump ATPase activity."
FT /evidence="ECO:0000269|PubMed:11909858"
FT MUTAGEN 58
FT /note="C->S: Has no effect on pump ATPase activity."
FT /evidence="ECO:0000269|PubMed:11909858"
FT MUTAGEN 99
FT /note="N->Q: Impairs pump targeting to the plasma membrane;
FT when associated with Q-130 and Q-222. Loss of pump ATPase
FT activity; when associated with Q-103; Q-130; Q-146; Q-161;
FT Q-193 and Q-222."
FT /evidence="ECO:0000269|PubMed:10722662"
FT MUTAGEN 103
FT /note="N->Q: Loss of pump ATPase activity; when associated
FT with Q-99; Q-130; Q-146; Q-161; Q-193 and Q-222."
FT /evidence="ECO:0000269|PubMed:10722662"
FT MUTAGEN 130
FT /note="N->Q: Impairs targeting to the plasma membrane; when
FT associated with Q-99 and Q-222. Loss of pump ATPase
FT activity; when associated with Q-99; Q-103; Q-146; Q-161;
FT Q-193 and Q-222."
FT /evidence="ECO:0000269|PubMed:10722662"
FT MUTAGEN 131
FT /note="C->S: Impairs the assembly of an active pump and its
FT targeting to the plasma membrane; when associated with S-
FT 152."
FT /evidence="ECO:0000269|PubMed:11909858"
FT MUTAGEN 146
FT /note="N->Q: Loss of pump ATPase activity; when associated
FT with Q-99; Q-103; Q-130; Q-161; Q-193 and Q-222."
FT /evidence="ECO:0000269|PubMed:10722662"
FT MUTAGEN 152
FT /note="C->S: Impairs the assembly of an active pump and its
FT targeting to the plasma membrane; when associated with S-
FT 131."
FT /evidence="ECO:0000269|PubMed:11909858"
FT MUTAGEN 161
FT /note="N->Q: Loss of pump ATPase activity; when associated
FT with Q-99; Q-103; Q-130; Q-146; Q-193 and Q-222."
FT /evidence="ECO:0000269|PubMed:10722662"
FT MUTAGEN 162
FT /note="C->S: Impairs the assembly of an active pump and its
FT targeting to the plasma membrane; when associated with S-
FT 178."
FT /evidence="ECO:0000269|PubMed:11909858"
FT MUTAGEN 178
FT /note="C->S: Impairs the assembly of an active pump and its
FT targeting to the plasma membrane; when associated with S-
FT 162."
FT /evidence="ECO:0000269|PubMed:11909858"
FT MUTAGEN 193
FT /note="N->Q: Loss of pump ATPase activity; when associated
FT with Q-99; Q-103; Q-130; Q-146; Q-161 and Q-222."
FT /evidence="ECO:0000269|PubMed:10722662"
FT MUTAGEN 201
FT /note="C->S: Impairs the assembly of an active pump and its
FT targeting to the plasma membrane; when associated with S-
FT 263."
FT /evidence="ECO:0000269|PubMed:11909858"
FT MUTAGEN 222
FT /note="N->Q: Impairs targeting to the plasma membrane; when
FT associated with Q-99 and Q-130. Loss of pump ATPase
FT activity; when associated with Q-99; Q-103; Q-130; Q-146;
FT Q-161 and Q-193."
FT /evidence="ECO:0000269|PubMed:10722662"
FT MUTAGEN 263
FT /note="C->S: Impairs the assembly of an active pump and its
FT targeting to the plasma membrane; when associated with S-
FT 201."
FT /evidence="ECO:0000269|PubMed:11909858"
SQ SEQUENCE 291 AA; 33419 MW; 6D2FE467A36CC103 CRC64;
MAALQEKKSC SQRMEEFRHY CWNPDTGQML GRTLSRWVWI SLYYVAFYVV MTGLFALCIY
VLMQTIDPYT PDYQDQLKSP GVTLRPDVYG EKGLEIHYNI SDNRTWTSLT HTLRSFLAGY
SPAAQVDNIN CTSKTYFFQE SFGAPNHTKF SCKFTADMLE NCSGLTDPSF GFKEGKPCFI
IKMNRIVRFL PSNSTPPRVD CTFLDMPHQA LTPLQVEYYP PNGTFSLHYF PYYGKKAQPH
YSNPLVAAKL LNVPTNTEVV VLCKILADHV TFDNPHDPYE GKVEFKLKIQ K
