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Protein

Potassium-transporting ATPase alpha chain 2

Gene

Atp12a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of ATP coupled with the exchange of H+ and K+ ions across the plasma membrane. Responsible for potassium absorption in various tissues.

Catalytic activityi

ATP + H2O + H+(In) + K+(Out) = ADP + phosphate + H+(Out) + K+(In).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei387 – 38714-aspartylphosphate intermediateBy similarity
Metal bindingi728 – 7281MagnesiumBy similarity
Metal bindingi732 – 7321MagnesiumBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. hydrogen:potassium-exchanging ATPase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. sodium:potassium-exchanging ATPase activity Source: InterPro

GO - Biological processi

  1. potassium ion homeostasis Source: MGI
  2. regulation of pH Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Potassium transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

ReactomeiREACT_338561. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium-transporting ATPase alpha chain 2 (EC:3.6.3.10)
Alternative name(s):
Non-gastric H(+)/K(+) ATPase subunit alpha
Proton pump
Gene namesi
Name:Atp12a
Synonyms:Atp1al1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1926943. Atp12a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9999CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei100 – 12021HelicalSequence AnalysisAdd
BLAST
Topological domaini121 – 14222LumenalSequence AnalysisAdd
BLAST
Transmembranei143 – 16321HelicalSequence AnalysisAdd
BLAST
Topological domaini164 – 299136CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei300 – 31920HelicalSequence AnalysisAdd
BLAST
Topological domaini320 – 33112LumenalSequence AnalysisAdd
BLAST
Transmembranei332 – 34918HelicalSequence AnalysisAdd
BLAST
Topological domaini350 – 783434CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei784 – 80320HelicalSequence AnalysisAdd
BLAST
Topological domaini804 – 81310LumenalSequence Analysis
Transmembranei814 – 83421HelicalSequence AnalysisAdd
BLAST
Topological domaini835 – 85420CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei855 – 87723HelicalSequence AnalysisAdd
BLAST
Topological domaini878 – 92952LumenalSequence AnalysisAdd
BLAST
Transmembranei930 – 94920HelicalSequence AnalysisAdd
BLAST
Topological domaini950 – 96314CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei964 – 98219HelicalSequence AnalysisAdd
BLAST
Topological domaini983 – 99715LumenalSequence AnalysisAdd
BLAST
Transmembranei998 – 101821HelicalSequence AnalysisAdd
BLAST
Topological domaini1019 – 103517CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10351035Potassium-transporting ATPase alpha chain 2PRO_0000046261Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei954 – 9541Phosphoserine; by PKABy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Z1W8.
PaxDbiQ9Z1W8.
PRIDEiQ9Z1W8.

PTM databases

PhosphoSiteiQ9Z1W8.

Expressioni

Tissue specificityi

Found in skin, kidney and distal colon.1 Publication

Gene expression databases

BgeeiQ9Z1W8.
GenevestigatoriQ9Z1W8.

Interactioni

Subunit structurei

Composed of two subunits: alpha (catalytic) and beta.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1W8.
SMRiQ9Z1W8. Positions 45-1035.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00760000119003.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiQ9Z1W8.
KOiK01544.
OMAiNLRVEWE.
OrthoDBiEOG7327N0.
TreeFamiTF312838.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR030318. Atp12a.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005775. P-type_ATPase_IIC.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF282. PTHR24093:SF282. 1 hit.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z1W8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRKTEIYSV ELNGTKDVEL ADQKDDKKFK GGKNKDSEPN KSQEEELKKE
60 70 80 90 100
LDLDDHRLSN TDLEQKYGTN IIQGLSSIRA AELLARDGPN ALTPPKQTPE
110 120 130 140 150
IIKFLKQMVG GFSILLWIGA ALCWIAYVIQ YVSSTASLDN VYLGAILVLV
160 170 180 190 200
VILTGIFAYY QEAKSTNIMA SFSKMIPQQA LVIRDAEKKI IPAEQLVVGD
210 220 230 240 250
VVEIKGGDQI PADIRLVFSQ GCKVDNSSLT GESEPQARST EFTHENPLET
260 270 280 290 300
KNIGFYSTTC LEGTATGIVI NTGDRTIIGR IASLASGVGS EKTPIAIEIE
310 320 330 340 350
HFVHIVAAVA VSVGVIFFIT AVCMKYYVLD AIIFLISIIV ANVPEGLLAT
360 370 380 390 400
VTVTLSLTAK RMAKKNCLVK NLEAVETLGS TSIICSDKTG TLTQNRMTVA
410 420 430 440 450
HLWFDNQIFV ADTSENQTKQ AFDQSSGTWA SLSKIITLCN RAEFRPGQES
460 470 480 490 500
VPIMKRVVVG DASETALLKF SEVILGDVMD IRKRNHKVAE IPFNSTNKFQ
510 520 530 540 550
LSIHETEDPN DKRFLMVMKG APERILEKCS TIMINGQEQP LDKSSADAFH
560 570 580 590 600
TAYMELGGLG ERVLGFCHLY LPADKFPQSY TFDVDSINFP TSNLCFVGLL
610 620 630 640 650
SMIDPPRSTV PDAVSKCRSA GIKVIMVTGD HPITAKAIAK SVGIISANNE
660 670 680 690 700
TVEDIAKRRN IAVEQVNKRE AKAAVVTGME LKDMTPEQLD ELLINYQEIV
710 720 730 740 750
FARTSPQQKL IIVEGCQRQD AVVAVTGDGV NDSPALKKAD IGIAMGIAGS
760 770 780 790 800
DAAKNAADMV LLDDNFASIV TGVEEGRLIF DNLKKTIAYT LTKNIAELCP
810 820 830 840 850
FLIYIVAGLP LPIGTITILF IDLGTDIIPS IALAYEKAES DIMNRKPRHK
860 870 880 890 900
KKDRLVNKQL AIYSYLHIGL MQALGGFLVY FTVYAQQGFW PTSLINLRVS
910 920 930 940 950
WETDDINDLE DSYGQEWTRY QRKYLEWTGS TAFFVAIMVQ QIADLIIRKT
960 970 980 990 1000
RRNSIFQQGL FRNKVIWVGI ISQIIVALVL SYGLGSVTAL SFTMLRAQYW
1010 1020 1030
FVAVPHAILI WVYDEMRKLF IRLYPGSWWD KNMYY
Length:1,035
Mass (Da):114,727
Last modified:July 27, 2011 - v3
Checksum:iBFB2C26D90305206
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti464 – 4641E → K in AAL68709 (PubMed:11729223).Curated
Sequence conflicti975 – 9751I → M in AAD03421 (PubMed:9872395).Curated
Sequence conflicti981 – 9811S → F in AAD03421 (PubMed:9872395).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF350499 Genomic DNA. Translation: AAL68709.1.
BC109011 mRNA. Translation: AAI09012.1.
AF100169 mRNA. Translation: AAD03421.1.
CCDSiCCDS27148.1.
RefSeqiNP_619593.2. NM_138652.2.
UniGeneiMm.273271.

Genome annotation databases

EnsembliENSMUST00000007340; ENSMUSP00000007340; ENSMUSG00000022229.
GeneIDi192113.
KEGGimmu:192113.
UCSCiuc007ubw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF350499 Genomic DNA. Translation: AAL68709.1.
BC109011 mRNA. Translation: AAI09012.1.
AF100169 mRNA. Translation: AAD03421.1.
CCDSiCCDS27148.1.
RefSeqiNP_619593.2. NM_138652.2.
UniGeneiMm.273271.

3D structure databases

ProteinModelPortaliQ9Z1W8.
SMRiQ9Z1W8. Positions 45-1035.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9Z1W8.

Proteomic databases

MaxQBiQ9Z1W8.
PaxDbiQ9Z1W8.
PRIDEiQ9Z1W8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007340; ENSMUSP00000007340; ENSMUSG00000022229.
GeneIDi192113.
KEGGimmu:192113.
UCSCiuc007ubw.2. mouse.

Organism-specific databases

CTDi479.
MGIiMGI:1926943. Atp12a.

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00760000119003.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiQ9Z1W8.
KOiK01544.
OMAiNLRVEWE.
OrthoDBiEOG7327N0.
TreeFamiTF312838.

Enzyme and pathway databases

ReactomeiREACT_338561. Ion transport by P-type ATPases.

Miscellaneous databases

NextBioi371111.
PROiQ9Z1W8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z1W8.
GenevestigatoriQ9Z1W8.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR030318. Atp12a.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005775. P-type_ATPase_IIC.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF282. PTHR24093:SF282. 1 hit.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure, promoter analysis, and chromosomal localization of the murine H(+)/K(+)-ATPase alpha 2 subunit gene."
    Zhang W., Kuncewicz T., Higham S.C., Kone B.C.
    J. Am. Soc. Nephrol. 12:2554-2564(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 488-498; 624-636; 710-718 AND 755-785, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Ouabain-sensitive H,K-ATPase: tissue-specific expression of the mammalian genes encoding the catalytic alpha subunit."
    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.
    FEBS Lett. 440:320-324(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 868-981, TISSUE SPECIFICITY.
    Strain: C57BL/6.
    Tissue: Skin.

Entry informationi

Entry nameiAT12A_MOUSE
AccessioniPrimary (citable) accession number: Q9Z1W8
Secondary accession number(s): Q32MR8, Q8VHY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.