AT12A_HUMAN
ID AT12A_HUMAN Reviewed; 1039 AA.
AC P54707; Q13816; Q13817; Q16734; Q5W035; Q8N5U2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Potassium-transporting ATPase alpha chain 2;
DE AltName: Full=HK alpha 2 {ECO:0000250|UniProtKB:Q9TV52};
DE AltName: Full=Non-gastric H(+)/K(+) ATPase subunit alpha {ECO:0000303|PubMed:16914892};
DE EC=7.2.2.19 {ECO:0000269|PubMed:11341842, ECO:0000269|PubMed:7485470, ECO:0000269|PubMed:8853415};
DE AltName: Full=Non-gastric Na(+)/K(+) ATPase subunit alpha {ECO:0000303|PubMed:9774385};
DE EC=7.2.2.13 {ECO:0000269|PubMed:11341842, ECO:0000269|PubMed:9774385};
DE AltName: Full=Proton pump;
DE AltName: Full=Sodium pump {ECO:0000303|PubMed:9774385};
GN Name=ATP12A {ECO:0000303|PubMed:29391451, ECO:0000312|HGNC:HGNC:13816};
GN Synonyms=ATP1AL1 {ECO:0000303|PubMed:7485470};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Skin;
RX PubMed=8045293; DOI=10.1016/0014-5793(94)00655-5;
RA Grishin A.V., Sverdlov V.E., Kostina M.B., Modyanov N.N.;
RT "Cloning and characterization of the entire cDNA encoded by ATP1AL1 -- a
RT member of the human Na,K/H,K-ATPase gene family.";
RL FEBS Lett. 349:144-150(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8838794; DOI=10.1006/geno.1996.0125;
RA Sverdlov V.E., Kostina M.B., Modyanov N.N.;
RT "Genomic organization of the human ATP1AL1 gene encoding a ouabain-
RT sensitive H,K-ATPase.";
RL Genomics 32:317-327(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-348 AND 681-780.
RX PubMed=1847115; DOI=10.1016/0014-5793(91)80091-g;
RA Modyanov N.N., Petrukhin K.E., Sverdlov V.E., Grishin A.V., Orlova M.Y.,
RA Kostina M.B., Makarevich O.I., Broude N.E., Monastyrskaya G.S.,
RA Sverdlov E.D.;
RT "The family of human Na,K-ATPase genes. ATP1AL1 gene is transcriptionally
RT competent and probably encodes the related ion transport ATPase.";
RL FEBS Lett. 278:91-94(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 183-253.
RX PubMed=3035563; DOI=10.1073/pnas.84.12.4039;
RA Shull M.M., Lingrel J.B.;
RT "Multiple genes encode the human Na+,K+-ATPase catalytic subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4039-4043(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-412.
RX PubMed=3036582; DOI=10.1016/0014-5793(87)80677-4;
RA Sverdlov E.D., Monastyrskaya G.S., Broude N.E., Ushkaryov Y.A.,
RA Allikmets R.L., Melkov A.M., Smirnov Y.V., Malyshev I.V., Dulubova I.E.,
RA Petrukhin K.E., Gryshin A.V., Kiyatkin N.I., Kostina M.B., Sverdlov V.E.,
RA Modyanov N.N., Ovchinnikov Y.A.;
RT "The family of human Na+,K+-ATPase genes. No less than five genes and/or
RT pseudogenes related to the alpha-subunit.";
RL FEBS Lett. 217:275-278(1987).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, 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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=8853415; DOI=10.1152/ajprenal.1996.271.3.f539;
RA Grishin A.V., Bevensee M.O., Modyanov N.N., Rajendran V., Boron W.F.,
RA Caplan M.J.;
RT "Functional expression of the cDNA encoded by the human ATP1AL1 gene.";
RL Am. J. Physiol. 271:F539-F551(1996).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=9872395; DOI=10.1016/s0014-5793(98)01483-5;
RA Pestov N.B., Romanova L.G., Korneenko T.V., Egorov M.V., Kostina M.B.,
RA Sverdlov V.E., Askari A., Shakhparonov M.I., Modyanov N.N.;
RT "Ouabain-sensitive H,K-ATPase: tissue-specific expression of the mammalian
RT genes encoding the catalytic alpha subunit.";
RL FEBS Lett. 440:320-324(1998).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9774385; DOI=10.1074/jbc.273.43.27772;
RA Grishin A.V., Caplan M.J.;
RT "ATP1AL1, a member of the non-gastric H,K-ATPase family, functions as a
RT sodium pump.";
RL J. Biol. Chem. 273:27772-27778(1998).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=11341842; DOI=10.1021/bi010191y;
RA Adams G., Tillekeratne M., Yu C., Pestov N.B., Modyanov N.N.;
RT "Catalytic function of nongastric H,K-ATPase expressed in Sf-21 insect
RT cells.";
RL Biochemistry 40:5765-5776(2001).
RN [15]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-329.
RX PubMed=16914892; DOI=10.1159/000095169;
RA Lerner M., Lemke D., Bertram H., Schillers H., Oberleithner H.,
RA Caplan M.J., Reinhardt J.;
RT "An extracellular loop of the human non-gastric H,K-ATPase alpha-subunit is
RT involved in apical plasma membrane polarization.";
RL Cell. Physiol. Biochem. 18:75-84(2006).
RN [16]
RP TISSUE SPECIFICITY.
RX PubMed=22179016; DOI=10.1159/000335860;
RA Streif D., Iglseder E., Hauser-Kronberger C., Fink K.G., Jakab M.,
RA Ritter M.;
RT "Expression of the non-gastric H+/K+ ATPase ATP12A in normal and
RT pathological human prostate tissue.";
RL Cell. Physiol. Biochem. 28:1287-1294(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY IL13.
RX PubMed=29391451; DOI=10.1038/s41598-018-20444-8;
RA Lennox A.T., Coburn S.L., Leech J.A., Heidrich E.M., Kleyman T.R.,
RA Wenzel S.E., Pilewski J.M., Corcoran T.E., Myerburg M.M.;
RT "ATP12A promotes mucus dysfunction during Type 2 airway inflammation.";
RL Sci. Rep. 8:2109-2109(2018).
CC -!- FUNCTION: The catalytic subunit of a H(+)/K(+) ATPase and/or Na(+)/K(+)
CC ATPase pump which transports K(+) ions in exchange for Na(+) and/or
CC H(+) ions across the apical membrane of epithelial cells. Uses ATP as
CC an energy source to pump K(+) ions into the cell while transporting
CC Na(+) and/or H(+) ions to the extracellular compartment
CC (PubMed:9774385, PubMed:7485470, PubMed:8853415, PubMed:11341842).
CC Involved in the maintenance of electrolyte homeostasis through K(+) ion
CC absorption in kidney and colon (By similarity). In the airway
CC epithelium, may play a primary role in mucus acidification regulating
CC its viscosity and clearance (PubMed:29391451).
CC {ECO:0000250|UniProtKB:Q9Z1W8, ECO:0000269|PubMed:11341842,
CC ECO:0000269|PubMed:29391451, ECO:0000269|PubMed:7485470,
CC ECO:0000269|PubMed:8853415, ECO:0000269|PubMed:9774385}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) +
CC K(+)(in) + phosphate; Xref=Rhea:RHEA:22044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.19;
CC Evidence={ECO:0000269|PubMed:11341842, ECO:0000269|PubMed:7485470,
CC ECO:0000269|PubMed:8853415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22045;
CC Evidence={ECO:0000305|PubMed:11341842, ECO:0000305|PubMed:7485470,
CC ECO:0000305|PubMed:8853415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
CC Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC EC=7.2.2.13; Evidence={ECO:0000269|PubMed:11341842,
CC ECO:0000269|PubMed:9774385};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18354;
CC Evidence={ECO:0000305|PubMed:11341842, ECO:0000305|PubMed:9774385};
CC -!- ACTIVITY REGULATION: The ATPase activity is regulated by monovalent
CC cations and pH. Up-regulated by K(+) ions in a dose-dependent way.
CC Down-regulated by Na(+) ions (PubMed:11341842). Inhibited by
CC Na(+)/K(+)-ATPase inhibitor ouabain and H(+)/K(+)-ATPase inhibitor SCH-
CC 28080 with an intermediate sensitivity to completely resistant
CC Na(+)/K(+)-ATPases and highly sensitive H(+)/K(+)-ATPases
CC (PubMed:7485470, PubMed:8853415, PubMed:11341842).
CC {ECO:0000269|PubMed:11341842, ECO:0000269|PubMed:7485470,
CC ECO:0000269|PubMed:8853415}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.2-7.8. {ECO:0000269|PubMed:11341842};
CC -!- SUBUNIT: The ATPase pump is composed of a catalytic alpha subunit and
CC an auxiliary non-catalytic beta subunit. The alpha subunit pairs with
CC the beta subunit of gastric H(+)/K(+) ATPase ATP4B or the beta subunit
CC of Na(+)/K(+) ATPases ATP1B1 and ATP1B3; this interaction is required
CC for the formation of a functionally active pump and its targeting at
CC the plasma membrane. {ECO:0000250|UniProtKB:P54708,
CC ECO:0000269|PubMed:7485470, ECO:0000269|PubMed:8853415}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:16914892}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P54707-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54707-2; Sequence=VSP_034640;
CC -!- TISSUE SPECIFICITY: Expressed in airway epithelial cells (at protein
CC level) (PubMed:29391451). Found in skin and kidney. Detected in
CC prostate basal cells (at protein level). Expression is increased in
CC benign prostate hyperplasia and tumor tissues (at protein level).
CC {ECO:0000269|PubMed:22179016, ECO:0000269|PubMed:29391451,
CC ECO:0000269|PubMed:9872395}.
CC -!- INDUCTION: Up-regulated by inflammatory cytokine IL13.
CC {ECO:0000269|PubMed:29391451}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
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DR EMBL; U02076; AAB37755.1; -; mRNA.
DR EMBL; L42563; AAC37589.2; -; Genomic_DNA.
DR EMBL; L42558; AAC37589.2; JOINED; Genomic_DNA.
DR EMBL; L42559; AAC37589.2; JOINED; Genomic_DNA.
DR EMBL; L42565; AAC37589.2; JOINED; Genomic_DNA.
DR EMBL; L42566; AAC37589.2; JOINED; Genomic_DNA.
DR EMBL; L42567; AAC37589.2; JOINED; Genomic_DNA.
DR EMBL; L42560; AAC37589.2; JOINED; Genomic_DNA.
DR EMBL; L42561; AAC37589.2; JOINED; Genomic_DNA.
DR EMBL; L42568; AAC37589.2; JOINED; Genomic_DNA.
DR EMBL; L42562; AAC37589.2; JOINED; Genomic_DNA.
DR EMBL; L42569; AAC37589.2; JOINED; Genomic_DNA.
DR EMBL; AK292968; BAF85657.1; -; mRNA.
DR EMBL; AL157364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08346.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08345.1; -; Genomic_DNA.
DR EMBL; BC031609; AAH31609.1; -; mRNA.
DR EMBL; X69823; CAA49477.1; -; Genomic_DNA.
DR EMBL; X69824; CAA49478.1; -; Genomic_DNA.
DR EMBL; M16797; AAA51802.1; -; mRNA.
DR EMBL; M27574; AAA35576.1; -; Genomic_DNA.
DR CCDS; CCDS31948.1; -. [P54707-1]
DR CCDS; CCDS53858.1; -. [P54707-2]
DR PIR; A26641; A26641.
DR PIR; D27795; D27795.
DR PIR; E27397; E27397.
DR PIR; I38401; I38401.
DR PIR; S13028; S13028.
DR PIR; S31504; S31504.
DR RefSeq; NP_001172014.1; NM_001185085.1. [P54707-2]
DR RefSeq; NP_001667.4; NM_001676.5. [P54707-1]
DR AlphaFoldDB; P54707; -.
DR SMR; P54707; -.
DR BioGRID; 106969; 210.
DR IntAct; P54707; 59.
DR STRING; 9606.ENSP00000218548; -.
DR BindingDB; P54707; -.
DR ChEMBL; CHEMBL2933; -.
DR TCDB; 3.A.3.1.13; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P54707; -.
DR PhosphoSitePlus; P54707; -.
DR SwissPalm; P54707; -.
DR BioMuta; ATP12A; -.
DR DMDM; 212287925; -.
DR EPD; P54707; -.
DR jPOST; P54707; -.
DR MassIVE; P54707; -.
DR MaxQB; P54707; -.
DR PaxDb; P54707; -.
DR PeptideAtlas; P54707; -.
DR PRIDE; P54707; -.
DR ProteomicsDB; 56695; -. [P54707-1]
DR ProteomicsDB; 56696; -. [P54707-2]
DR Antibodypedia; 22475; 139 antibodies from 28 providers.
DR DNASU; 479; -.
DR Ensembl; ENST00000218548.10; ENSP00000218548.6; ENSG00000075673.12. [P54707-2]
DR Ensembl; ENST00000381946.5; ENSP00000371372.3; ENSG00000075673.12. [P54707-1]
DR GeneID; 479; -.
DR KEGG; hsa:479; -.
DR MANE-Select; ENST00000381946.5; ENSP00000371372.3; NM_001676.7; NP_001667.4.
DR UCSC; uc001upp.4; human. [P54707-1]
DR CTD; 479; -.
DR DisGeNET; 479; -.
DR GeneCards; ATP12A; -.
DR HGNC; HGNC:13816; ATP12A.
DR HPA; ENSG00000075673; Group enriched (esophagus, kidney, lymphoid tissue, placenta, skin).
DR MIM; 182360; gene.
DR neXtProt; NX_P54707; -.
DR OpenTargets; ENSG00000075673; -.
DR PharmGKB; PA25104; -.
DR VEuPathDB; HostDB:ENSG00000075673; -.
DR eggNOG; KOG0203; Eukaryota.
DR GeneTree; ENSGT00940000159259; -.
DR HOGENOM; CLU_002360_4_3_1; -.
DR InParanoid; P54707; -.
DR OMA; NNVMGCV; -.
DR PhylomeDB; P54707; -.
DR TreeFam; TF312838; -.
DR BRENDA; 7.2.2.19; 2681.
DR PathwayCommons; P54707; -.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; P54707; -.
DR BioGRID-ORCS; 479; 8 hits in 1065 CRISPR screens.
DR ChiTaRS; ATP12A; human.
DR GeneWiki; ATP12A; -.
DR GenomeRNAi; 479; -.
DR Pharos; P54707; Tchem.
DR PRO; PR:P54707; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P54707; protein.
DR Bgee; ENSG00000075673; Expressed in trachea and 71 other tissues.
DR Genevisible; P54707; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005889; C:potassium:proton exchanging ATPase complex; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008900; F:P-type potassium:proton transporter activity; IDA:UniProtKB.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IDA:UniProtKB.
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:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0006885; P:regulation of pH; IEA:Ensembl.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030318; Atp12a.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PANTHER; PTHR43294:SF1; PTHR43294:SF1; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Hydrogen ion transport;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Potassium; Potassium transport; Reference proteome; Sodium;
KW Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1039
FT /note="Potassium-transporting ATPase alpha chain 2"
FT /id="PRO_0000046260"
FT TOPO_DOM 1..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..146
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..335
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..787
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 788..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..817
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 839..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..881
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 882..933
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 934..953
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 954..967
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 968..986
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 987..1001
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1023..1039
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 391
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 732
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 736
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 958
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT VAR_SEQ 266
FT /note="E -> EASTSPV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034640"
FT VARIANT 863
FT /note="P -> L (in dbSNP:rs2289909)"
FT /id="VAR_020186"
FT MUTAGEN 329
FT /note="K->E: Abolishes targeting to the apical plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:16914892"
FT CONFLICT 3
FT /note="Q -> QLFQ (in Ref. 2; AAC37589)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="V -> VRLWGVQV (in Ref. 7; CAA49477)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..227
FT /note="Missing (in Ref. 7; CAA49477)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="E -> V (in Ref. 7; CAA49477)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="L -> P (in Ref. 9; AAA35576)"
FT /evidence="ECO:0000305"
FT CONFLICT 724..727
FT /note="DAVV -> VGGQ (in Ref. 7; CAA49478)"
FT /evidence="ECO:0000305"
FT CONFLICT 772..773
FT /note="SI -> LH (in Ref. 7; CAA49478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1039 AA; 115511 MW; C906897E11FA406C CRC64;
MHQKTPEIYS VELSGTKDIV KTDKGDGKEK YRGLKNNCLE LKKKNHKEEF QKELHLDDHK
LSNRELEEKY GTDIIMGLSS TRAAELLARD GPNSLTPPKQ TPEIVKFLKQ MVGGFSILLW
VGAFLCWIAY GIQYSSDKSA SLNNVYLGCV LGLVVILTGI FAYYQEAKST NIMSSFNKMI
PQQALVIRDS EKKTIPSEQL VVGDIVEVKG GDQIPADIRV LSSQGCRVDN SSLTGESEPQ
PRSSEFTHEN PLETKNICFY STTCLEGTVT GMVINTGDRT IIGHIASLAS GVGNEKTPIA
IEIEHFVHIV AGVAVSIGIL FFIIAVSLKY QVLDSIIFLI GIIVANVPEG LLATVTVTLS
LTAKRMAKKN CLVKNLEAVE TLGSTSIICS DKTGTLTQNR MTVAHLWFDN QIFVADTSED
HSNQVFDQSS RTWASLSKII TLCNRAEFKP GQENVPIMKK AVIGDASETA LLKFSEVILG
DVMEIRKRNR KVAEIPFNST NKFQLSIHEM DDPHGKRFLM VMKGAPERIL EKCSTIMING
EEHPLDKSTA KTFHTAYMEL GGLGERVLGF CHLYLPADEF PETYSFDIDA MNFPTSNLCF
VGLLSMIDPP RSTVPDAVTK CRSAGIKVIM VTGDHPITAK AIAKSVGIIS ANSETVEDIA
HRLNIAVEQV NKRDAKAAVV TGMELKDMSS EQLDEILANY QEIVFARTSP QQKLIIVEGC
QRQDAVVAVT GDGVNDSPAL KKADIGIAMG IAGSDAAKNA ADMVLLDDNF ASIVTGVEEG
RLIFDNLKKT IAYSLTKNIA ELCPFLIYII VGLPLPIGTI TILFIDLGTD IIPSIALAYE
KAESDIMNRK PRHKNKDRLV NQPLAVYSYL HIGLMQALGA FLVYFTVYAQ EGFLPRTLIN
LRVEWEKDYV NDLKDSYGQE WTRYQREYLE WTGYTAFFVG ILVQQIADLI IRKTRRNSIF
QQGLFRNKVI WVGITSQIII GLILSYGLGS VTALSFTMLR AQYWFVAVPH AILIWVYDEV
RKLFIRLYPG SWWDKNMYY
