Sodium/potassium-transporting ATPase subunit alpha-1 precursor

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Q8VDN2 (AT1A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1023 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Ion transport Potassium transport Sodium transport Sodium/potassium transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Sodium
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara membrane hyperpolarization Inferred from electronic annotation. Source: Compara 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: Compara regulation of blood pressure Inferred from genetic interaction PubMed 16243970. Source: MGI regulation of cardiac muscle cell contraction Inferred from electronic annotation. Source: Compara 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 10360172 PubMed 15485817. Source: MGI response to drug Inferred from mutant phenotype PubMed 17234593. Source: MGI
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara T-tubule Inferred from direct assay PubMed 16292983. Source: BHF-UCL basolateral plasma membrane Inferred from direct assay PubMed 8144700. Source: MGI caveola Inferred from electronic annotation. Source: Compara endoplasmic reticulum Inferred from electronic annotation. Source: Compara endosome Inferred from electronic annotation. Source: Compara integral to membrane Inferred from sequence or structural similarity. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell sodium:potassium-exchanging ATPase complex Inferred from electronic annotation. Source: Compara
Molecular_function	4-nitrophenylphosphatase activity Inferred from mutant phenotype PubMed 10360172. Source: MGI ADP binding Inferred from electronic annotation. Source: Compara ATP binding Inferred from electronic annotation. Source: UniProtKB-KW potassium ion binding Inferred from electronic annotation. Source: Compara sodium ion binding Inferred from electronic annotation. Source: Compara sodium:potassium-exchanging ATPase activity Inferred from mutant phenotype PubMed 10360172 PubMed 15485817. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 5

By similarity

PRO_0000002485

Chain

6 – 1023

1018

Sodium/potassium-transporting ATPase subunit alpha-1

PRO_0000002486

Regions

Topological domain

6 – 96

Cytoplasmic Potential

Transmembrane

97 – 117

Helical; Potential

Topological domain

118 – 129

Extracellular Potential

Transmembrane

130 – 150

Helical; Potential

Topological domain

151 – 291

141

Cytoplasmic Potential

Transmembrane

292 – 312

Helical; Potential

Topological domain

313 – 319

Extracellular Potential

Transmembrane

320 – 340

Helical; Potential

Topological domain

341 – 789

449

Cytoplasmic Potential

Transmembrane

790 – 810

Helical; Potential

Topological domain

811 – 865

Extracellular Potential

Transmembrane

866 – 886

Helical; Potential

Topological domain

887 – 915

Cytoplasmic Potential

Transmembrane

916 – 936

Helical; Potential

Topological domain

937 – 952

Extracellular Potential

Transmembrane

953 – 973

Helical; Potential

Topological domain

974 – 979

Cytoplasmic Potential

Transmembrane

980 – 1000

Helical; Potential

Topological domain

1001 – 1023

Extracellular Potential

Region

82 – 84

Phosphoinositide-3 kinase binding By similarity

Sites

Active site

376

4-aspartylphosphate intermediate By similarity

Metal binding

717

Magnesium By similarity

Metal binding

721

Magnesium By similarity

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine Ref.3

Modified residue

217

Phosphoserine Ref.5

Modified residue

219

Phosphothreonine Ref.5

Modified residue

228

Phosphoserine Ref.5

Modified residue

260

Phosphotyrosine Ref.4

Modified residue

452

Phosphoserine Ref.5

Modified residue

542

Phosphotyrosine By similarity

Modified residue

943

Phosphoserine; by PKA By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8VDN2 [UniParc].

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

1,023

112,982

        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' referencesShow '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]	"Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[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, MASS SPECTROMETRY. Tissue: Brain.
[5]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; THR-219; SER-228 AND SER-452, MASS SPECTROMETRY. Tissue: Brain cortex.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, MASS SPECTROMETRY. Tissue: Melanoma.
+	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.
IPI	IPI00311682.
RefSeq	NP_659149.1. NM_144900.2.
UniGene	Mm.280103.
3D structure databases
ProteinModelPortal	Q8VDN2.
SMR	Q8VDN2. Positions 26-1023.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31885N.
IntAct	Q8VDN2. 12 interactions.
MINT	MINT-1797662.
PTM databases
PhosphoSite	Q8VDN2.
Proteomic databases
PaxDb	Q8VDN2.
PRIDE	Q8VDN2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000036493; ENSMUSP00000039657; ENSMUSG00000033161.
GeneID	11928.
KEGG	mmu:11928.
UCSC	uc008qrj.1. mouse.
Organism-specific databases
CTD	476.
MGI	MGI:88105. Atp1a1.
Phylogenomic databases
eggNOG	COG0474.
GeneTree	ENSGT00560000076866.
HOGENOM	HOG000265622.
HOVERGEN	HBG004298.
InParanoid	Q8VDN2.
KO	K01539.
OMA	QFPEGFQ.
OrthoDB	EOG46MBHS.
Gene expression databases
ArrayExpress	Q8VDN2.
Bgee	Q8VDN2.
CleanEx	MM_ATP1A1.
Genevestigator	Q8VDN2.
GermOnline	ENSMUSG00000033161. Mus musculus.
Family and domain databases
Gene3D	1.20.1110.10. 2 hits. 2.70.150.10. 2 hits. 3.40.1110.10. 1 hit.
InterPro	IPR006068. 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]
PANTHER	PTHR24093. PTHR24093. 1 hit.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01106. ATPase-IIC_X-K. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP1A1. mouse.
NextBio	280013.
SOURCE	Search...

Entry information

Entry name

AT1A1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents