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Q6PIE5 (AT1A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. 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:
Sodium/potassium-transporting ATPase subunit alpha-2

Short name=Na(+)/K(+) ATPase alpha-2 subunit
EC=3.6.3.9
Alternative name(s):
Na(+)/K(+) ATPase alpha(+) subunit
Sodium pump subunit alpha-2
Gene names
Name:Atp1a2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1020 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients By similarity.

Catalytic activity

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

Subunit structure

Composed of three subunits: alpha (catalytic), beta and gamma By similarity.

Subcellular location

Membrane; Multi-pass membrane protein By similarity. Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Sodium transport
Sodium/potassium transport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Potassium
Sodium
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

ATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: Ensembl

adult locomotory behavior

Inferred from mutant phenotype PubMed 17234593. Source: MGI

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

locomotion

Inferred from mutant phenotype PubMed 12458206. Source: MGI

negative regulation of cytosolic calcium ion concentration

Inferred from mutant phenotype PubMed 10360172. Source: MGI

negative regulation of heart contraction

Inferred from mutant phenotype PubMed 10360172. Source: MGI

negative regulation of striated muscle contraction

Inferred from mutant phenotype PubMed 11507009. Source: MGI

neurotransmitter uptake

Inferred from mutant phenotype PubMed 12805306. Source: MGI

regulation of blood pressure

Inferred from genetic interaction PubMed 16243970. Source: MGI

regulation of cardiac muscle cell contraction

Inferred from electronic annotation. Source: Ensembl

regulation of muscle contraction

Inferred from mutant phenotype PubMed 10360172. Source: MGI

regulation of respiratory gaseous exchange by neurological system process

Inferred from mutant phenotype PubMed 12458206PubMed 15564586. Source: MGI

regulation of smooth muscle contraction

Inferred from mutant phenotype PubMed 14627611. Source: MGI

regulation of striated muscle contraction

Inferred from mutant phenotype PubMed 15253893. Source: MGI

regulation of the force of heart contraction

Inferred from mutant phenotype PubMed 10360172. Source: MGI

regulation of vasoconstriction

Inferred from mutant phenotype PubMed 14627611. Source: MGI

response to nicotine

Inferred from electronic annotation. Source: Ensembl

sodium ion transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

visual learning

Inferred from mutant phenotype PubMed 17234593. Source: MGI

   Cellular_componentT-tubule

Inferred from direct assay PubMed 16292983. Source: BHF-UCL

caveola

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

sarcolemma

Inferred from direct assay PubMed 16292983. Source: BHF-UCL

sodium:potassium-exchanging ATPase complex

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 16292983. Source: BHF-UCL

sodium:potassium-exchanging ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 55 By similarity
PRO_0000002505
Chain6 – 10201015Sodium/potassium-transporting ATPase subunit alpha-2
PRO_0000002506

Regions

Topological domain6 – 8580Cytoplasmic Potential
Transmembrane86 – 10621Helical; Potential
Topological domain107 – 12923Extracellular Potential
Transmembrane130 – 15021Helical; Potential
Topological domain151 – 286136Cytoplasmic Potential
Transmembrane287 – 30620Helical; Potential
Topological domain307 – 31812Extracellular Potential
Transmembrane319 – 33618Helical; Potential
Topological domain337 – 769433Cytoplasmic Potential
Transmembrane770 – 78920Helical; Potential
Topological domain790 – 79910Extracellular Potential
Transmembrane800 – 82021Helical; Potential
Topological domain821 – 84020Cytoplasmic Potential
Transmembrane841 – 86323Helical; Potential
Topological domain864 – 91552Extracellular Potential
Transmembrane916 – 93520Helical; Potential
Topological domain936 – 94813Cytoplasmic Potential
Transmembrane949 – 96719Helical; Potential
Topological domain968 – 98215Extracellular Potential
Transmembrane983 – 100321Helical; Potential
Topological domain1004 – 102017Cytoplasmic Potential
Region80 – 823Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site37414-aspartylphosphate intermediate By similarity
Metal binding7141Magnesium By similarity
Metal binding7181Magnesium By similarity

Amino acid modifications

Modified residue5701Phosphothreonine By similarity
Modified residue5871Phosphoserine By similarity
Modified residue9401Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6PIE5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5436E795BD5B4CFA

FASTA1,020112,217
        10         20         30         40         50         60 
MGRGAGREYS PAATTAENGG GKKKQKEKEL DELKKEVAMD DHKLSLDELG RKYQVDLSKG 

        70         80         90        100        110        120 
LTNQRAQDIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSI LLWIGALLCF LAYGILAAME 

       130        140        150        160        170        180 
DEPSNDNLYL GIVLAAVVIV TGCFSYYQEA KSSKIMDSFK NMVPQQALVI REGEKMQINA 

       190        200        210        220        230        240 
EEVVVGDLVE VKGGDRVPAD LRIISSHGCK VDNSSLTGES EPQTRSPEFT HENPLETRNI 

       250        260        270        280        290        300 
CFFSTNCVEG TARGIVIATG DRTVMGRIAT LASGLEVGQT PIAMEIEHFI QLITGVAVFL 

       310        320        330        340        350        360 
GVSFFVLSLI LGYSWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE 

       370        380        390        400        410        420 
AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TEDQSGATFD KRSPTWTALS 

       430        440        450        460        470        480 
RIAGLCNRAV FKAGQENISV SKRDTAGDAS ESALLKCIEL SCGSVRKMRD RNPKVAEIPF 

       490        500        510        520        530        540 
NSTNKYQLSI HEREDSPQSH VLVMKGAPER ILDRCSTILV QGKEIPLDKE MQDAFQNAYM 

       550        560        570        580        590        600 
ELGGLGERVL GFCQLNLPSG KFPRGFKFDT DELNFPTEKL CFVGLMSMID PPRAAVPDAV 

       610        620        630        640        650        660 
GKCRSAGIKV IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPVS QVNPREAKAC 

       670        680        690        700        710        720 
VVHGSDLKDM TSEQLDEILR DHTEIVFART SPQQKLIIVE GCQRQGAIVA VTGDGVNDSP 

       730        740        750        760        770        780 
ALKKADIGIA MGISGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN 

       790        800        810        820        830        840 
IPEITPFLLF IIANIPLPLG TVTILCIDLG TDMVPAISLA YEAAESDIMK RQPRNSQTDK 

       850        860        870        880        890        900 
LVNERLISMA YGQIGMIQAL GGFFTYFVIL AENGFLPSRL LGIRLDWDDR TTNDLEDSYG 

       910        920        930        940        950        960 
QEWTYEQRKV VEFTCHTAFF ASIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLLEETA 

       970        980        990       1000       1010       1020 
LAAFLSYCPG MGVALRMYPL KVTWWFCAFP YSLLIFIYDE VRKLILRRYP GGWVEKETYY 

« Hide

References

« Hide 'large scale' references
[1]"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].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
[2]Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 44-59; 73-89; 161-171; 176-192; 211-238; 254-262; 358-375; 413-428; 433-442; 444-456; 475-485; 494-505; 524-561; 565-602; 610-622; 627-655; 659-680; 696-771; 891-908; 938-947 AND 1008-1016.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC036127 mRNA. Translation: AAH36127.1.
BC041774 mRNA. Translation: AAH41774.1.
CCDSCCDS35782.1.
RefSeqNP_848492.1. NM_178405.3.
UniGeneMm.207432.

3D structure databases

ProteinModelPortalQ6PIE5.
SMRQ6PIE5. Positions 28-1020.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid221101. 1 interaction.
DIPDIP-48355N.
IntActQ6PIE5. 3 interactions.
MINTMINT-7543414.
STRING10090.ENSMUSP00000083077.

PTM databases

PhosphoSiteQ6PIE5.

Proteomic databases

MaxQBQ6PIE5.
PaxDbQ6PIE5.
PRIDEQ6PIE5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000085913; ENSMUSP00000083077; ENSMUSG00000007097.
GeneID98660.
KEGGmmu:98660.
UCSCuc007dqc.1. mouse.

Organism-specific databases

CTD477.
MGIMGI:88106. Atp1a2.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00560000076866.
HOVERGENHBG004298.
InParanoidQ6PIE5.
KOK01539.
OMAIINIPLP.
OrthoDBEOG7327N0.
PhylomeDBQ6PIE5.
TreeFamTF312838.

Gene expression databases

ArrayExpressQ6PIE5.
BgeeQ6PIE5.
CleanExMM_ATP1A2.
GenevestigatorQ6PIE5.

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. 2 hits.
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

NextBio353565.
PROQ6PIE5.
SOURCESearch...

Entry information

Entry nameAT1A2_MOUSE
AccessionPrimary (citable) accession number: Q6PIE5
Secondary accession number(s): Q80UZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 103 of the entry and version 1 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