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Potassium-transporting ATPase alpha chain 2 (HK alpha 2) (Non-gastric H( )/K( ) ATPase subunit alpha) (EC 7.2.2.19) (Non-gastric Na( )/K( ) ATPase subunit alpha) (EC 7.2.2.13) (Proton pump) (Sodium pump)

 AT12A_MOUSE             Reviewed;        1035 AA.
Q9Z1W8; Q32MR8; Q8VHY2;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
02-JUN-2021, entry version 169.
RecName: Full=Potassium-transporting ATPase alpha chain 2;
AltName: Full=HK alpha 2 {ECO:0000250|UniProtKB:Q9TV52};
AltName: Full=Non-gastric H(+)/K(+) ATPase subunit alpha;
EC=7.2.2.19 {ECO:0000250|UniProtKB:P54707};
AltName: Full=Non-gastric Na(+)/K(+) ATPase subunit alpha;
EC=7.2.2.13 {ECO:0000250|UniProtKB:P54707};
AltName: Full=Proton pump;
AltName: Full=Sodium pump {ECO:0000250|UniProtKB:P54707};
Name=Atp12a; Synonyms=Atp1al1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=11729223;
Zhang W., Kuncewicz T., Higham S.C., Kone B.C.;
"Structure, promoter analysis, and chromosomal localization of the murine
H(+)/K(+)-ATPase alpha 2 subunit gene.";
J. Am. Soc. Nephrol. 12:2554-2564(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 488-498; 624-636; 710-718 AND 755-785, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 868-981, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Skin;
PubMed=9872395; DOI=10.1016/s0014-5793(98)01483-5;
Pestov N.B., Romanova L.G., Korneenko T.V., Egorov M.V., Kostina M.B.,
Sverdlov V.E., Askari A., Shakhparonov M.I., Modyanov N.N.;
"Ouabain-sensitive H,K-ATPase: tissue-specific expression of the mammalian
genes encoding the catalytic alpha subunit.";
FEBS Lett. 440:320-324(1998).
[5]
FUNCTION, TISSUE SPECIFICITY, INDUCTION BY DIET, AND DISRUPTION PHENOTYPE.
PubMed=9449685; DOI=10.1172/jci1720;
Meneton P., Schultheis P.J., Greeb J., Nieman M.L., Liu L.H., Clarke L.L.,
Duffy J.J., Doetschman T., Lorenz J.N., Shull G.E.;
"Increased sensitivity to K+ deprivation in colonic H,K-ATPase-deficient
mice.";
J. Clin. Invest. 101:536-542(1998).
-!- FUNCTION: The catalytic subunit of a H(+)/K(+) ATPase and/or Na(+)/K(+)
ATPase pump which transports K(+) ions in exchange for Na(+) and/or
H(+) ions across the apical membrane of epithelial cells. Uses ATP as
an energy source to pump K(+) ions into the cell while transporting
Na(+) and/or H(+) ions to the extracellular compartment (By
similarity). Involved in the maintenance of electrolyte homeostasis
through K(+) ion absorption in kidney and colon (PubMed:9449685). In
the airway epithelium, may play a primary role in mucus acidification
regulating its viscosity and clearance (By similarity).
{ECO:0000250|UniProtKB:P54707, ECO:0000269|PubMed:9449685}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) +
K(+)(in) + phosphate; Xref=Rhea:RHEA:22044, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.19;
Evidence={ECO:0000250|UniProtKB:P54707};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22045;
Evidence={ECO:0000250|UniProtKB:P54707};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
EC=7.2.2.13; Evidence={ECO:0000250|UniProtKB:P54707};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18354;
Evidence={ECO:0000250|UniProtKB:P54707};
-!- SUBUNIT: The ATPase pump is composed of a catalytic alpha subunit and
an auxiliary non-catalytic beta subunit. The alpha subunit pairs with
the beta subunit of gastric H(+)/K(+) ATPase ATP4B or the beta subunit
of Na(+)/K(+) ATPases ATP1B1 and ATP1B3; this interaction is required
for the formation of a functionally active pump and its targeting at
the plasma membrane. {ECO:0000250|UniProtKB:P54707,
ECO:0000250|UniProtKB:P54708}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000250|UniProtKB:P54707, ECO:0000250|UniProtKB:P54708}; Multi-
pass membrane protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Found in skin, kidney and distal colon.
{ECO:0000269|PubMed:9449685, ECO:0000269|PubMed:9872395}.
-!- INDUCTION: Up-regulated in kidney and down-regulated in colon in
response to K(+) ion free diet. {ECO:0000269|PubMed:9449685}.
-!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate.
{ECO:0000269|PubMed:9449685}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
family. Type IIC subfamily. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; AF350499; AAL68709.1; -; Genomic_DNA.
EMBL; BC109011; AAI09012.1; -; mRNA.
EMBL; AF100169; AAD03421.1; -; mRNA.
CCDS; CCDS27148.1; -.
RefSeq; NP_619593.2; NM_138652.2.
SMR; Q9Z1W8; -.
BioGRID; 228640; 3.
IntAct; Q9Z1W8; 3.
STRING; 10090.ENSMUSP00000007340; -.
iPTMnet; Q9Z1W8; -.
PhosphoSitePlus; Q9Z1W8; -.
EPD; Q9Z1W8; -.
jPOST; Q9Z1W8; -.
MaxQB; Q9Z1W8; -.
PaxDb; Q9Z1W8; -.
PeptideAtlas; Q9Z1W8; -.
PRIDE; Q9Z1W8; -.
ProteomicsDB; 277050; -.
Antibodypedia; 22475; 134 antibodies.
DNASU; 192113; -.
Ensembl; ENSMUST00000007340; ENSMUSP00000007340; ENSMUSG00000022229.
GeneID; 192113; -.
KEGG; mmu:192113; -.
UCSC; uc007ubw.2; mouse.
CTD; 479; -.
MGI; MGI:1926943; Atp12a.
eggNOG; KOG0203; Eukaryota.
GeneTree; ENSGT00940000159259; -.
HOGENOM; CLU_002360_4_1_1; -.
InParanoid; Q9Z1W8; -.
OMA; TFHTAYM; -.
OrthoDB; 388324at2759; -.
TreeFam; TF312838; -.
Reactome; R-MMU-936837; Ion transport by P-type ATPases.
BioGRID-ORCS; 192113; 0 hits in 52 CRISPR screens.
PRO; PR:Q9Z1W8; -.
Proteomes; UP000000589; Chromosome 14.
RNAct; Q9Z1W8; protein.
Bgee; ENSMUSG00000022229; Expressed in left colon and 75 other tissues.
Genevisible; Q9Z1W8; MM.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IMP:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008900; F:P-type potassium:proton transporter activity; ISS:UniProtKB.
GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; ISS:UniProtKB.
GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
GO; GO:0055075; P:potassium ion homeostasis; IMP:MGI.
GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
GO; GO:0006885; P:regulation of pH; IMP:MGI.
GO; GO:0010038; P:response to metal ion; ISO:MGI.
GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
CDD; cd02608; P-type_ATPase_Na-K_like; 1.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR030318; Atp12a.
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR005775; P-type_ATPase_IIC.
InterPro; IPR001757; P_typ_ATPase.
InterPro; IPR044492; P_typ_ATPase_HD_dom.
PANTHER; PTHR43294:SF1; PTHR43294:SF1; 1.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
SFLD; SFLDF00027; p-type_atpase; 1.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 1.
TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Direct protein sequencing;
Hydrogen ion transport; Ion transport; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport;
Reference proteome; Sodium; Sodium transport; Translocase; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1..1035
/note="Potassium-transporting ATPase alpha chain 2"
/id="PRO_0000046261"
TOPO_DOM 1..99
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 100..120
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 121..142
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 143..163
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 164..299
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 300..319
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 320..331
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 332..349
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 350..783
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 784..803
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 804..813
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 814..834
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 835..854
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 855..877
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 878..929
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 930..949
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 950..963
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 964..982
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 983..997
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 998..1018
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1019..1035
/note="Cytoplasmic"
/evidence="ECO:0000255"
REGION 22..49
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
ACT_SITE 387
/note="4-aspartylphosphate intermediate"
/evidence="ECO:0000250"
METAL 728
/note="Magnesium"
/evidence="ECO:0000250"
METAL 732
/note="Magnesium"
/evidence="ECO:0000250"
MOD_RES 954
/note="Phosphoserine; by PKA"
/evidence="ECO:0000250"
CONFLICT 464
/note="E -> K (in Ref. 1; AAL68709)"
/evidence="ECO:0000305"
CONFLICT 975
/note="I -> M (in Ref. 4; AAD03421)"
/evidence="ECO:0000305"
CONFLICT 981
/note="S -> F (in Ref. 4; AAD03421)"
/evidence="ECO:0000305"
SEQUENCE 1035 AA; 114727 MW; BFB2C26D90305206 CRC64;
MRRKTEIYSV ELNGTKDVEL ADQKDDKKFK GGKNKDSEPN KSQEEELKKE LDLDDHRLSN
TDLEQKYGTN IIQGLSSIRA AELLARDGPN ALTPPKQTPE IIKFLKQMVG GFSILLWIGA
ALCWIAYVIQ YVSSTASLDN VYLGAILVLV VILTGIFAYY QEAKSTNIMA SFSKMIPQQA
LVIRDAEKKI IPAEQLVVGD VVEIKGGDQI PADIRLVFSQ GCKVDNSSLT GESEPQARST
EFTHENPLET KNIGFYSTTC LEGTATGIVI NTGDRTIIGR IASLASGVGS EKTPIAIEIE
HFVHIVAAVA VSVGVIFFIT AVCMKYYVLD AIIFLISIIV ANVPEGLLAT VTVTLSLTAK
RMAKKNCLVK NLEAVETLGS TSIICSDKTG TLTQNRMTVA HLWFDNQIFV ADTSENQTKQ
AFDQSSGTWA SLSKIITLCN RAEFRPGQES VPIMKRVVVG DASETALLKF SEVILGDVMD
IRKRNHKVAE IPFNSTNKFQ LSIHETEDPN DKRFLMVMKG APERILEKCS TIMINGQEQP
LDKSSADAFH TAYMELGGLG ERVLGFCHLY LPADKFPQSY TFDVDSINFP TSNLCFVGLL
SMIDPPRSTV PDAVSKCRSA GIKVIMVTGD HPITAKAIAK SVGIISANNE TVEDIAKRRN
IAVEQVNKRE AKAAVVTGME LKDMTPEQLD ELLINYQEIV FARTSPQQKL IIVEGCQRQD
AVVAVTGDGV NDSPALKKAD IGIAMGIAGS DAAKNAADMV LLDDNFASIV TGVEEGRLIF
DNLKKTIAYT LTKNIAELCP FLIYIVAGLP LPIGTITILF IDLGTDIIPS IALAYEKAES
DIMNRKPRHK KKDRLVNKQL AIYSYLHIGL MQALGGFLVY FTVYAQQGFW PTSLINLRVS
WETDDINDLE DSYGQEWTRY QRKYLEWTGS TAFFVAIMVQ QIADLIIRKT RRNSIFQQGL
FRNKVIWVGI ISQIIVALVL SYGLGSVTAL SFTMLRAQYW FVAVPHAILI WVYDEMRKLF
IRLYPGSWWD KNMYY


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