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Q8VDN2 (AT1A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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-1

Short name=Na(+)/K(+) ATPase alpha-1 subunit
EC=3.6.3.9
Alternative name(s):
Sodium pump subunit alpha-1
Gene names
Name:Atp1a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1023 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. Interacts with SIK1 By similarity.

Subcellular location

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

Post-translational modification

Phosphorylation on Tyr-10 modulates pumping activity. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity 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
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

dephosphorylation

Inferred from mutant phenotype PubMed 10360172. Source: GOC

membrane hyperpolarization

Inferred from electronic annotation. Source: Ensembl

negative regulation of glucocorticoid biosynthetic process

Inferred from mutant phenotype PubMed 17234593. Source: MGI

negative regulation of heart contraction

Inferred from mutant phenotype PubMed 15485817. Source: MGI

positive regulation of heart contraction

Inferred from mutant phenotype PubMed 10360172. Source: MGI

positive regulation of striated muscle contraction

Inferred from mutant phenotype PubMed 11507009. Source: MGI

potassium ion import

Inferred from electronic annotation. Source: Ensembl

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 sodium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of the force of heart contraction

Inferred from mutant phenotype PubMed 10360172PubMed 15485817. Source: MGI

response to drug

Inferred from mutant phenotype PubMed 17234593. Source: MGI

sodium ion transmembrane transport

Inferred from mutant phenotype PubMed 10360172PubMed 15485817. Source: GOC

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

T-tubule

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

apical plasma membrane

Inferred from direct assay PubMed 21705333. Source: MGI

basolateral plasma membrane

Inferred from direct assay PubMed 8144700. Source: MGI

caveola

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 10468580PubMed 10837135. Source: MGI

sarcolemma

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

sodium:potassium-exchanging ATPase complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionADP binding

Inferred from electronic annotation. Source: Ensembl

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatase activity

Inferred from mutant phenotype PubMed 10360172. Source: MGI

potassium ion binding

Inferred from electronic annotation. Source: Ensembl

sodium ion binding

Inferred from electronic annotation. Source: Ensembl

sodium:potassium-exchanging ATPase activity

Inferred from mutant phenotype PubMed 10360172PubMed 15485817. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 55 By similarity
PRO_0000002485
Chain6 – 10231018Sodium/potassium-transporting ATPase subunit alpha-1
PRO_0000002486

Regions

Topological domain6 – 9691Cytoplasmic Potential
Transmembrane97 – 11721Helical; Potential
Topological domain118 – 12912Extracellular Potential
Transmembrane130 – 15021Helical; Potential
Topological domain151 – 291141Cytoplasmic Potential
Transmembrane292 – 31221Helical; Potential
Topological domain313 – 3197Extracellular Potential
Transmembrane320 – 34021Helical; Potential
Topological domain341 – 789449Cytoplasmic Potential
Transmembrane790 – 81021Helical; Potential
Topological domain811 – 86555Extracellular Potential
Transmembrane866 – 88621Helical; Potential
Topological domain887 – 91529Cytoplasmic Potential
Transmembrane916 – 93621Helical; Potential
Topological domain937 – 95216Extracellular Potential
Transmembrane953 – 97321Helical; Potential
Topological domain974 – 9796Cytoplasmic Potential
Transmembrane980 – 100021Helical; Potential
Topological domain1001 – 102323Extracellular Potential
Region82 – 843Phosphoinositide-3 kinase binding By similarity

Sites

Active site37614-aspartylphosphate intermediate By similarity
Metal binding7171Magnesium By similarity
Metal binding7211Magnesium By similarity
Binding site4871ATP By similarity

Amino acid modifications

Modified residue91N6-acetyllysine Ref.5
Modified residue101Phosphotyrosine By similarity
Modified residue161Phosphoserine By similarity
Modified residue211N6-acetyllysine Ref.5
Modified residue2601Phosphotyrosine Ref.4
Modified residue5421Phosphotyrosine By similarity
Modified residue6611N6-succinyllysine Ref.5
Modified residue9431Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VDN2 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 1E806D3FDFC5AD80

FASTA1,023112,982
        10         20         30         40         50         60 
MGKGVGRDKY EPAAVSEHGD KKGKKAKKER DMDELKKEVS MDDHKLSLDE LHRKYGTDLS 

        70         80         90        100        110        120 
RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SMLLWIGAIL CFLAYGIRSA 

       130        140        150        160        170        180 
TEEEPPNDDL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI 

       190        200        210        220        230        240 
NAEDVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR 

       250        260        270        280        290        300 
NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV 

       310        320        330        340        350        360 
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN 

       370        380        390        400        410        420 
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWFA 

       430        440        450        460        470        480 
LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI EVCCGSVMEM REKYSKIVEI 

       490        500        510        520        530        540 
PFNSTNKYQL SIHKNPNASE PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN 

       550        560        570        580        590        600 
AYLELGGLGE RVLGFCHLLL PDEQFPEGFQ FDTDDVNFPV DNLCFVGLIS MIDPPRAAVP 

       610        620        630        640        650        660 
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVNQVNPRDA 

       670        680        690        700        710        720 
KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN 

       730        740        750        760        770        780 
DSPALKKADI GVAMGIVGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL 

       790        800        810        820        830        840 
TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK 

       850        860        870        880        890        900 
TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRETW DDRWVNDVED 

       910        920        930        940        950        960 
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE 

       970        980        990       1000       1010       1020 
ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE 


TYY 

« 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: FVB/N.
Tissue: Liver and Mammary gland.
[2]Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 55-61; 75-91; 163-173; 178-194; 213-240; 256-264; 360-377; 414-444; 446-458; 477-494; 536-551; 597-605; 613-625; 630-658; 662-683; 699-774 AND 941-950.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[3]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[4]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9 AND LYS-21, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC010319 mRNA. Translation: AAH10319.1.
BC021496 mRNA. Translation: AAH21496.1.
BC023794 mRNA. Translation: AAH23794.1.
BC025618 mRNA. Translation: AAH25618.1.
BC025627 mRNA. Translation: AAH25627.1.
BC025811 mRNA. Translation: AAH25811.1.
BC032187 mRNA. Translation: AAH32187.1.
BC033435 mRNA. Translation: AAH33435.1.
BC033471 mRNA. Translation: AAH33471.1.
BC042435 mRNA. Translation: AAH42435.1.
RefSeqNP_659149.1. NM_144900.2.
UniGeneMm.280103.

3D structure databases

ProteinModelPortalQ8VDN2.
SMRQ8VDN2. Positions 30-1023.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198243. 7 interactions.
DIPDIP-31885N.
IntActQ8VDN2. 21 interactions.
MINTMINT-1797662.

PTM databases

PhosphoSiteQ8VDN2.

Proteomic databases

PaxDbQ8VDN2.
PRIDEQ8VDN2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000036493; ENSMUSP00000039657; ENSMUSG00000033161.
GeneID11928.
KEGGmmu:11928.
UCSCuc008qrj.2. mouse.

Organism-specific databases

CTD476.
MGIMGI:88105. Atp1a1.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00560000076866.
HOGENOMHOG000265622.
HOVERGENHBG004298.
InParanoidQ8VDN2.
KOK01539.
OMAQFPEGFQ.
OrthoDBEOG7327N0.
PhylomeDBQ8VDN2.
TreeFamTF312838.

Gene expression databases

ArrayExpressQ8VDN2.
BgeeQ8VDN2.
CleanExMM_ATP1A1.
GenevestigatorQ8VDN2.

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

ChiTaRSATP1A1. mouse.
NextBio280013.
PROQ8VDN2.
SOURCESearch...

Entry information

Entry nameAT1A1_MOUSE
AccessionPrimary (citable) accession number: Q8VDN2
Secondary accession number(s): Q91Z09
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 115 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