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Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

Atp1a1

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

Functioni

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei376 – 37614-aspartylphosphate intermediateBy similarity
Binding sitei487 – 4871ATPBy similarity
Metal bindingi717 – 7171MagnesiumBy similarity
Metal bindingi721 – 7211MagnesiumBy similarity

GO - Molecular functioni

  1. ADP binding Source: Ensembl
  2. ATP binding Source: UniProtKB-KW
  3. chaperone binding Source: MGI
  4. phosphatase activity Source: MGI
  5. potassium ion binding Source: Ensembl
  6. sodium:potassium-exchanging ATPase activity Source: MGI
  7. sodium ion binding Source: Ensembl
  8. steroid hormone binding Source: MGI

GO - Biological processi

  1. cellular potassium ion homeostasis Source: MGI
  2. cellular response to mechanical stimulus Source: Ensembl
  3. cellular response to steroid hormone stimulus Source: MGI
  4. cellular sodium ion homeostasis Source: MGI
  5. dephosphorylation Source: GOC
  6. membrane hyperpolarization Source: Ensembl
  7. membrane repolarization Source: MGI
  8. negative regulation of glucocorticoid biosynthetic process Source: MGI
  9. negative regulation of heart contraction Source: MGI
  10. positive regulation of heart contraction Source: MGI
  11. positive regulation of striated muscle contraction Source: MGI
  12. potassium ion import Source: MGI
  13. regulation of blood pressure Source: MGI
  14. regulation of cardiac muscle cell contraction Source: Ensembl
  15. regulation of sodium ion transport Source: UniProtKB
  16. regulation of the force of heart contraction Source: MGI
  17. response to drug Source: MGI
  18. sodium ion export from cell Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Ion transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_338561. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium/potassium-transporting ATPase subunit alpha-1 (EC:3.6.3.9)
Short name:
Na(+)/K(+) ATPase alpha-1 subunit
Alternative name(s):
Sodium pump subunit alpha-1
Gene namesi
Name:Atp1a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:88105. Atp1a1.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini6 – 9691CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei97 – 11721HelicalSequence AnalysisAdd
BLAST
Topological domaini118 – 12912ExtracellularSequence AnalysisAdd
BLAST
Transmembranei130 – 15021HelicalSequence AnalysisAdd
BLAST
Topological domaini151 – 291141CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei292 – 31221HelicalSequence AnalysisAdd
BLAST
Topological domaini313 – 3197ExtracellularSequence Analysis
Transmembranei320 – 34021HelicalSequence AnalysisAdd
BLAST
Topological domaini341 – 789449CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei790 – 81021HelicalSequence AnalysisAdd
BLAST
Topological domaini811 – 86555ExtracellularSequence AnalysisAdd
BLAST
Transmembranei866 – 88621HelicalSequence AnalysisAdd
BLAST
Topological domaini887 – 91529CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei916 – 93621HelicalSequence AnalysisAdd
BLAST
Topological domaini937 – 95216ExtracellularSequence AnalysisAdd
BLAST
Transmembranei953 – 97321HelicalSequence AnalysisAdd
BLAST
Topological domaini974 – 9796CytoplasmicSequence Analysis
Transmembranei980 – 100021HelicalSequence AnalysisAdd
BLAST
Topological domaini1001 – 102323ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: MGI
  2. basolateral plasma membrane Source: MGI
  3. caveola Source: Ensembl
  4. endoplasmic reticulum Source: Ensembl
  5. endosome Source: Ensembl
  6. extracellular vesicular exosome Source: MGI
  7. Golgi apparatus Source: Ensembl
  8. integral component of membrane Source: UniProtKB
  9. melanosome Source: UniProtKB-SubCell
  10. membrane Source: MGI
  11. myelin sheath Source: UniProtKB
  12. neuronal postsynaptic density Source: MGI
  13. plasma membrane Source: MGI
  14. protein complex Source: MGI
  15. sarcolemma Source: BHF-UCL
  16. sodium:potassium-exchanging ATPase complex Source: MGI
  17. T-tubule Source: BHF-UCL
  18. vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 55By similarityPRO_0000002485
Chaini6 – 10231018Sodium/potassium-transporting ATPase subunit alpha-1PRO_0000002486Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysine1 Publication
Modified residuei10 – 101PhosphotyrosineBy similarity
Modified residuei16 – 161PhosphoserineBy similarity
Modified residuei21 – 211N6-acetyllysine1 Publication
Modified residuei260 – 2601Phosphotyrosine1 Publication
Modified residuei542 – 5421PhosphotyrosineBy similarity
Modified residuei661 – 6611N6-succinyllysine1 Publication
Modified residuei943 – 9431Phosphoserine; by PKABy similarity

Post-translational modificationi

Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8VDN2.
PaxDbiQ8VDN2.
PRIDEiQ8VDN2.

PTM databases

PhosphoSiteiQ8VDN2.

Expressioni

Gene expression databases

BgeeiQ8VDN2.
CleanExiMM_ATP1A1.
ExpressionAtlasiQ8VDN2. baseline and differential.
GenevestigatoriQ8VDN2.

Interactioni

Subunit structurei

Composed of three subunits: alpha (catalytic), beta and gamma. Interacts with SIK1 (By similarity). Interacts with SLC35G1 and STIM1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi198243. 11 interactions.
DIPiDIP-31885N.
IntActiQ8VDN2. 22 interactions.
MINTiMINT-1797662.

Structurei

3D structure databases

ProteinModelPortaliQ8VDN2.
SMRiQ8VDN2. Positions 30-1023.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 843Phosphoinositide-3 kinase bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00760000119003.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiQ8VDN2.
KOiK01539.
OMAiFLPTHLL.
OrthoDBiEOG7327N0.
PhylomeDBiQ8VDN2.
TreeFamiTF312838.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. 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]
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8VDN2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGVGRDKY EPAAVSEHGD KKGKKAKKER DMDELKKEVS MDDHKLSLDE
60 70 80 90 100
LHRKYGTDLS RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF
110 120 130 140 150
SMLLWIGAIL CFLAYGIRSA TEEEPPNDDL YLGVVLSAVV IITGCFSYYQ
160 170 180 190 200
EAKSSKIMES FKNMVPQQAL VIRNGEKMSI NAEDVVVGDL VEVKGGDRIP
210 220 230 240 250
ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR NIAFFSTNCV
260 270 280 290 300
EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV
310 320 330 340 350
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR
360 370 380 390 400
MARKNCLVKN LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA
410 420 430 440 450
DTTENQSGVS FDKTSATWFA LSRIAGLCNR AVFQANQENL PILKRAVAGD
460 470 480 490 500
ASESALLKCI EVCCGSVMEM REKYSKIVEI PFNSTNKYQL SIHKNPNASE
510 520 530 540 550
PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN AYLELGGLGE
560 570 580 590 600
RVLGFCHLLL PDEQFPEGFQ FDTDDVNFPV DNLCFVGLIS MIDPPRAAVP
610 620 630 640 650
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI
660 670 680 690 700
PVNQVNPRDA KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI
710 720 730 740 750
IVEGCQRQGA IVAVTGDGVN DSPALKKADI GVAMGIVGSD VSKQAADMIL
760 770 780 790 800
LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LIFIIANIPL
810 820 830 840 850
PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK TDKLVNERLI
860 870 880 890 900
SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRETW DDRWVNDVED
910 920 930 940 950
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK
960 970 980 990 1000
NKILIFGLFE ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV
1010 1020
YDEVRKLIIR RRPGGWVEKE TYY
Length:1,023
Mass (Da):112,982
Last modified:March 1, 2002 - v1
Checksum:i1E806D3FDFC5AD80
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17683.1.
RefSeqiNP_659149.1. NM_144900.2.
UniGeneiMm.280103.

Genome annotation databases

EnsembliENSMUST00000036493; ENSMUSP00000039657; ENSMUSG00000033161.
GeneIDi11928.
KEGGimmu:11928.
UCSCiuc008qrj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17683.1.
RefSeqiNP_659149.1. NM_144900.2.
UniGeneiMm.280103.

3D structure databases

ProteinModelPortaliQ8VDN2.
SMRiQ8VDN2. Positions 30-1023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198243. 11 interactions.
DIPiDIP-31885N.
IntActiQ8VDN2. 22 interactions.
MINTiMINT-1797662.

PTM databases

PhosphoSiteiQ8VDN2.

Proteomic databases

MaxQBiQ8VDN2.
PaxDbiQ8VDN2.
PRIDEiQ8VDN2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036493; ENSMUSP00000039657; ENSMUSG00000033161.
GeneIDi11928.
KEGGimmu:11928.
UCSCiuc008qrj.2. mouse.

Organism-specific databases

CTDi476.
MGIiMGI:88105. Atp1a1.

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00760000119003.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiQ8VDN2.
KOiK01539.
OMAiFLPTHLL.
OrthoDBiEOG7327N0.
PhylomeDBiQ8VDN2.
TreeFamiTF312838.

Enzyme and pathway databases

ReactomeiREACT_338561. Ion transport by P-type ATPases.

Miscellaneous databases

ChiTaRSiAtp1a1. mouse.
NextBioi280013.
PROiQ8VDN2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VDN2.
CleanExiMM_ATP1A1.
ExpressionAtlasiQ8VDN2. baseline and differential.
GenevestigatoriQ8VDN2.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. 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]
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. "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(2003) [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 (DEC-2008) to UniProtKB
    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(2006) [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(2007) [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(2012) [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.

Entry informationi

Entry nameiAT1A1_MOUSE
AccessioniPrimary (citable) accession number: Q8VDN2
Secondary accession number(s): Q91Z09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: March 1, 2002
Last modified: April 1, 2015
This is version 125 of the entry and version 1 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.