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Q9Z1W8 (AT12A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Atp12a
Synonyms:Atp1al1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1035 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subunit structure

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

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Found in skin, kidney and distal colon. Ref.4

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10351035Potassium-transporting ATPase alpha chain 2
PRO_0000046261

Regions

Topological domain1 – 9999Cytoplasmic Potential
Transmembrane100 – 12021Helical; Potential
Topological domain121 – 14222Lumenal Potential
Transmembrane143 – 16321Helical; Potential
Topological domain164 – 299136Cytoplasmic Potential
Transmembrane300 – 31920Helical; Potential
Topological domain320 – 33112Lumenal Potential
Transmembrane332 – 34918Helical; Potential
Topological domain350 – 783434Cytoplasmic Potential
Transmembrane784 – 80320Helical; Potential
Topological domain804 – 81310Lumenal Potential
Transmembrane814 – 83421Helical; Potential
Topological domain835 – 85420Cytoplasmic Potential
Transmembrane855 – 87723Helical; Potential
Topological domain878 – 92952Lumenal Potential
Transmembrane930 – 94920Helical; Potential
Topological domain950 – 96314Cytoplasmic Potential
Transmembrane964 – 98219Helical; Potential
Topological domain983 – 99715Lumenal Potential
Transmembrane998 – 101821Helical; Potential
Topological domain1019 – 103517Cytoplasmic Potential

Sites

Active site38714-aspartylphosphate intermediate By similarity
Metal binding7281Magnesium By similarity
Metal binding7321Magnesium By similarity

Amino acid modifications

Modified residue9541Phosphoserine; by PKA By similarity

Experimental info

Sequence conflict4641E → K in AAL68709. Ref.1
Sequence conflict9751I → M in AAD03421. Ref.4
Sequence conflict9811S → F in AAD03421. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9Z1W8 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: BFB2C26D90305206

FASTA1,035114,727
        10         20         30         40         50         60 
MRRKTEIYSV ELNGTKDVEL ADQKDDKKFK GGKNKDSEPN KSQEEELKKE LDLDDHRLSN 

        70         80         90        100        110        120 
TDLEQKYGTN IIQGLSSIRA AELLARDGPN ALTPPKQTPE IIKFLKQMVG GFSILLWIGA 

       130        140        150        160        170        180 
ALCWIAYVIQ YVSSTASLDN VYLGAILVLV VILTGIFAYY QEAKSTNIMA SFSKMIPQQA 

       190        200        210        220        230        240 
LVIRDAEKKI IPAEQLVVGD VVEIKGGDQI PADIRLVFSQ GCKVDNSSLT GESEPQARST 

       250        260        270        280        290        300 
EFTHENPLET KNIGFYSTTC LEGTATGIVI NTGDRTIIGR IASLASGVGS EKTPIAIEIE 

       310        320        330        340        350        360 
HFVHIVAAVA VSVGVIFFIT AVCMKYYVLD AIIFLISIIV ANVPEGLLAT VTVTLSLTAK 

       370        380        390        400        410        420 
RMAKKNCLVK NLEAVETLGS TSIICSDKTG TLTQNRMTVA HLWFDNQIFV ADTSENQTKQ 

       430        440        450        460        470        480 
AFDQSSGTWA SLSKIITLCN RAEFRPGQES VPIMKRVVVG DASETALLKF SEVILGDVMD 

       490        500        510        520        530        540 
IRKRNHKVAE IPFNSTNKFQ LSIHETEDPN DKRFLMVMKG APERILEKCS TIMINGQEQP 

       550        560        570        580        590        600 
LDKSSADAFH TAYMELGGLG ERVLGFCHLY LPADKFPQSY TFDVDSINFP TSNLCFVGLL 

       610        620        630        640        650        660 
SMIDPPRSTV PDAVSKCRSA GIKVIMVTGD HPITAKAIAK SVGIISANNE TVEDIAKRRN 

       670        680        690        700        710        720 
IAVEQVNKRE AKAAVVTGME LKDMTPEQLD ELLINYQEIV FARTSPQQKL IIVEGCQRQD 

       730        740        750        760        770        780 
AVVAVTGDGV NDSPALKKAD IGIAMGIAGS DAAKNAADMV LLDDNFASIV TGVEEGRLIF 

       790        800        810        820        830        840 
DNLKKTIAYT LTKNIAELCP FLIYIVAGLP LPIGTITILF IDLGTDIIPS IALAYEKAES 

       850        860        870        880        890        900 
DIMNRKPRHK KKDRLVNKQL AIYSYLHIGL MQALGGFLVY FTVYAQQGFW PTSLINLRVS 

       910        920        930        940        950        960 
WETDDINDLE DSYGQEWTRY QRKYLEWTGS TAFFVAIMVQ QIADLIIRKT RRNSIFQQGL 

       970        980        990       1000       1010       1020 
FRNKVIWVGI ISQIIVALVL SYGLGSVTAL SFTMLRAQYW FVAVPHAILI WVYDEMRKLF 

      1030 
IRLYPGSWWD KNMYY 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF350499 Genomic DNA. Translation: AAL68709.1.
BC109011 mRNA. Translation: AAI09012.1.
AF100169 mRNA. Translation: AAD03421.1.
RefSeqNP_619593.2. NM_138652.2.
UniGeneMm.273271.

3D structure databases

ProteinModelPortalQ9Z1W8.
SMRQ9Z1W8. Positions 45-1035.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9Z1W8.

Proteomic databases

PaxDbQ9Z1W8.
PRIDEQ9Z1W8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000007340; ENSMUSP00000007340; ENSMUSG00000022229.
GeneID192113.
KEGGmmu:192113.
UCSCuc007ubw.2. mouse.

Organism-specific databases

CTD479.
MGIMGI:1926943. Atp12a.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00560000076866.
HOGENOMHOG000265622.
HOVERGENHBG004298.
InParanoidQ32MR8.
KOK01544.
OMANLRVEWE.
OrthoDBEOG7327N0.
TreeFamTF312838.

Gene expression databases

BgeeQ9Z1W8.
GenevestigatorQ9Z1W8.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR005775. ATPase_P-typ_Na/K_IIC.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio371111.
PROQ9Z1W8.
SOURCESearch...

Entry information

Entry nameAT12A_MOUSE
AccessionPrimary (citable) accession number: Q9Z1W8
Secondary accession number(s): Q32MR8, Q8VHY2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot