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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_RAT               Reviewed;        1036 AA.
P54708;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
02-JUN-2021, entry version 165.
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:0000269|PubMed:10644526, ECO:0000269|PubMed:7560093};
AltName: Full=Non-gastric Na(+)/K(+) ATPase subunit alpha;
EC=7.2.2.13 {ECO:0000269|PubMed:10644526, ECO:0000269|PubMed:7560093};
AltName: Full=Proton pump;
AltName: Full=Sodium pump {ECO:0000250|UniProtKB:P54707};
Name=Atp12a; Synonyms=Atp1al1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE (ISOFORM LONG).
STRAIN=Sprague-Dawley; TISSUE=Colon;
PubMed=1320029;
Crowson M.S., Shull G.E.;
"Isolation and characterization of a cDNA encoding the putative distal
colon H+,K(+)-ATPase. Similarity of deduced amino acid sequence to gastric
H+,K(+)-ATPase and Na+,K(+)-ATPase and mRNA expression in distal colon,
kidney, and uterus.";
J. Biol. Chem. 267:13740-13748(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LONG AND SHORT).
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=9446555; DOI=10.1074/jbc.273.5.2543;
Kone B.C., Higham S.C.;
"A novel N-terminal splice variant of the rat H+-K+-ATPase alpha2 subunit.
Cloning, functional expression, and renal adaptive response to chronic
hypokalemia.";
J. Biol. Chem. 273:2543-2552(1998).
[3]
PROTEIN SEQUENCE OF 779-785, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[4]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
PubMed=7560093; DOI=10.1172/jci118247;
Lee J., Rajendran V.M., Mann A.S., Kashgarian M., Binder H.J.;
"Functional expression and segmental localization of rat colonic K-
adenosine triphosphatase.";
J. Clin. Invest. 96:2002-2008(1995).
[5]
TISSUE SPECIFICITY.
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).
[6]
INTERACTION WITH ATP1B3, AND SUBCELLULAR LOCATION.
PubMed=9950762; DOI=10.1152/ajpcell.1999.276.2.c350;
Sangan P., Kolla S.S., Rajendran V.M., Kashgarian M., Binder H.J.;
"Colonic H-K-ATPase beta-subunit: identification in apical membranes and
regulation by dietary K depletion.";
Am. J. Physiol. 276:C350-C360(1999).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
PubMed=10644526; DOI=10.1152/ajpcell.2000.278.1.c182;
Sangan P., Thevananther S., Sangan S., Rajendran V.M., Binder H.J.;
"Colonic H-K-ATPase alpha- and beta-subunits express ouabain-insensitive H-
K-ATPase.";
Am. J. Physiol. 278:C182-C189(2000).
[8]
INTERACTION WITH ATP1B1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=14749213; DOI=10.1152/ajpcell.00393.2003;
Pestov N.B., Korneenko T.V., Radkov R., Zhao H., Shakhparonov M.I.,
Modyanov N.N.;
"Identification of the beta-subunit for nongastric H-K-ATPase in rat
anterior prostate.";
Am. J. Physiol. 286:C1229-C1237(2004).
-!- 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
(PubMed:10644526, PubMed:7560093). Involved in the maintenance of
electrolyte homeostasis through K(+) ion absorption in kidney and colon
(By similarity). In the airway epithelium, may play a primary role in
mucus acidification regulating its viscosity and clearance (By
similarity). {ECO:0000250|UniProtKB:P54707,
ECO:0000250|UniProtKB:Q9Z1W8, ECO:0000269|PubMed:10644526,
ECO:0000269|PubMed:7560093}.
-!- 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:0000269|PubMed:10644526, ECO:0000269|PubMed:7560093};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22045;
Evidence={ECO:0000305|PubMed:10644526, ECO:0000305|PubMed:7560093};
-!- 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:0000269|PubMed:10644526,
ECO:0000269|PubMed:7560093};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18354;
Evidence={ECO:0000305|PubMed:10644526, ECO:0000305|PubMed:7560093};
-!- ACTIVITY REGULATION: Up-regulated by K(+) ions in a dose-dependent way.
{ECO:0000269|PubMed:10644526, ECO:0000269|PubMed:7560093}.
-!- 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:0000269|PubMed:14749213, ECO:0000269|PubMed:9950762}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:14749213, ECO:0000269|PubMed:7560093,
ECO:0000269|PubMed:9950762}; Multi-pass membrane protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long; Synonyms=2a;
IsoId=P54708-1; Sequence=Displayed;
Name=Short; Synonyms=2b;
IsoId=P54708-2; Sequence=VSP_000414;
-!- TISSUE SPECIFICITY: Expressed at high levels in distal colon,
coagulating and preputial glands; at much lower levels in proximal
colon, kidney, uterus, brain, placenta and lung; and at trace levels in
heart and forestomach (PubMed:9872395). Expressed in distal colon
epithelium (at protein level) (PubMed:7560093). Expressed in anterior
prostate (at protein level) (PubMed:14749213).
{ECO:0000269|PubMed:14749213, ECO:0000269|PubMed:7560093,
ECO:0000269|PubMed:9872395}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
family. Type IIC subfamily. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; M90398; AAA40779.1; -; mRNA.
EMBL; U94911; AAB93900.1; -; Genomic_DNA.
EMBL; U94912; AAB93901.1; -; mRNA.
EMBL; U94913; AAB93902.1; -; mRNA.
PIR; A42895; A42895.
SMR; P54708; -.
STRING; 10116.ENSRNOP00000028093; -.
TCDB; 3.A.3.1.4; the p-type atpase (p-atpase) superfamily.
iPTMnet; P54708; -.
PhosphoSitePlus; P54708; -.
jPOST; P54708; -.
PaxDb; P54708; -.
PRIDE; P54708; -.
UCSC; RGD:620569; rat. [P54708-1]
RGD; 620569; Atp12a.
eggNOG; KOG0203; Eukaryota.
InParanoid; P54708; -.
PhylomeDB; P54708; -.
Reactome; R-RNO-936837; Ion transport by P-type ATPases.
PRO; PR:P54708; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
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; IEA:UniProtKB-EC.
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; ISO:RGD.
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; ISO:RGD.
GO; GO:0010038; P:response to metal ion; IDA:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
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;
Alternative splicing; 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..1036
/note="Potassium-transporting ATPase alpha chain 2"
/id="PRO_0000046263"
TOPO_DOM 1..99
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 100..120
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 121..143
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 144..164
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 165..300
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 301..320
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 321..332
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 333..350
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 351..784
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 785..804
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 805..814
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 815..835
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 836..855
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 856..878
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 879..930
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 931..950
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 951..964
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 965..983
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 984..998
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 999..1019
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1020..1036
/note="Cytoplasmic"
/evidence="ECO:0000255"
REGION 1..50
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 17..50
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
ACT_SITE 388
/note="4-aspartylphosphate intermediate"
/evidence="ECO:0000250"
METAL 729
/note="Magnesium"
/evidence="ECO:0000250"
METAL 733
/note="Magnesium"
/evidence="ECO:0000250"
MOD_RES 955
/note="Phosphoserine; by PKA"
/evidence="ECO:0000250"
VAR_SEQ 1..108
/note="Missing (in isoform Short)"
/evidence="ECO:0000303|PubMed:9446555"
/id="VSP_000414"
SEQUENCE 1036 AA; 114975 MW; 453918E65CD4813B CRC64;
MRRKTEIYSV ELNGTKDVKP ADQRDDKKFK GAKNKDLEPN KSHEKEELKK ELDLDDHRLS
NTELEQKYGT NIIQGLSSVR ATELLARDGP NTLTPPKQTP EIIKFLKQMV GGFSILLWIG
AALCWIAFVI QYVNNSASLD NVYLGAILVL VVILTGIFAY YQEAKSTNIM ASFSKMIPQQ
ALVIRDAEKK VISAEQLVVG DVVEIKGGDQ IPADIRLVFS QGCKVDNSSL TGESEPQARS
TEFTHENPLE TKNIGFYSTT CLEGTATGIV INTGDRTIIG RIASLASGVG SEKTPIAIEI
EHFVHIVAGV AVSIDIIFFI TAVCMKYYVL DAIIFLISII VANVPEGLLA TVTVTLSLTA
KRMAKKNCLV KNLEAVETLG STSIICSDKT GTLTQNRMTV AHLWFDNQIF VADTSENQTK
QAFDQSSGTW ASLSKIITLC NRAEFRPGQE SVPIMKRTVV GDASETALLK FSEVILGDVM
GIRKRNHKVA EIPFNSTNKF QLSIHETEDP NNKRFLVVMK GAPERILEKC STIMINGQEQ
PLDKSSADSF HTAYMELGGL GERVLGFCHL YLPAEQFPQS YIFDVDSVNF PTSNFCFVGL
LSMIDPPRST VPDAVSKCRS AGIKVIMVTG DHPITAKAIA KSVGIISANN ETVEDIAKRR
NIAVEQVNKR EAKAAVVTGM ELKDMTPEQL DELLTNYQEI VFARTSPQQK LIIVEGCQRQ
DAIVAVTGDG VNDSPALKKA DIGIAMGIAG SDAAKNAADM VLLDDNFASI VTGVEEGRLI
FDNLKKTIAY TLTKNIAELC PFLIYIVAGL PLPIGTITIL FIDLGTDIIP SIALAYEKAE
SDIMNRKPRH KKKDRLVNTQ LAIYSYLHIG LMQALGGFLV YFTVYAQQGF WPTSLINLRV
AWETDDINDL EDSYGQEWTR YQRKYLEWTG STAFFVAIMI QQIADLIIRK TRRNSIFQQG
LFRNKVIWVG IASQVIVALI LSYGLGSVPA LSFTMLRVQY WFVAVPHAIL IWVYDEMRKL
FIRLYPGSWW DKNMYY


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