Sodium/potassium-transporting ATPase subunit alpha-2 precursor

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Q6PIE5 (AT1A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 93. History...

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

Documents (2) |

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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-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

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	1020 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 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 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 ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: Compara adult locomotory behavior Inferred from mutant phenotype PubMed 17234593. Source: MGI cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara locomotion Inferred from mutant phenotype PubMed 12458206. 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 reduction of cytosolic calcium ion concentration Inferred from mutant phenotype PubMed 10360172. 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: Compara regulation of respiratory gaseous exchange by neurological system process Inferred from mutant phenotype PubMed 12458206 PubMed 15564586. Source: MGI regulation of smooth muscle contraction Inferred from mutant phenotype PubMed 14627611. 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: Compara visual learning Inferred from mutant phenotype PubMed 17234593. Source: MGI
Cellular_component	T-tubule Inferred from direct assay PubMed 16292983. Source: BHF-UCL caveola Inferred from electronic annotation. Source: Compara cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB dendritic spine Inferred from electronic annotation. Source: Compara endosome Inferred from electronic annotation. Source: Compara sodium:potassium-exchanging ATPase complex Inferred from electronic annotation. Source: Compara synapse Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sodium:potassium-exchanging ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 5

By similarity

PRO_0000002505

Chain

6 – 1020

1015

Sodium/potassium-transporting ATPase subunit alpha-2

PRO_0000002506

Regions

Topological domain

6 – 85

Cytoplasmic Potential

Transmembrane

86 – 106

Helical; Potential

Topological domain

107 – 129

Extracellular Potential

Transmembrane

130 – 150

Helical; Potential

Topological domain

151 – 286

136

Cytoplasmic Potential

Transmembrane

287 – 306

Helical; Potential

Topological domain

307 – 318

Extracellular Potential

Transmembrane

319 – 336

Helical; Potential

Topological domain

337 – 769

433

Cytoplasmic Potential

Transmembrane

770 – 789

Helical; Potential

Topological domain

790 – 799

Extracellular Potential

Transmembrane

800 – 820

Helical; Potential

Topological domain

821 – 840

Cytoplasmic Potential

Transmembrane

841 – 863

Helical; Potential

Topological domain

864 – 915

Extracellular Potential

Transmembrane

916 – 935

Helical; Potential

Topological domain

936 – 948

Cytoplasmic Potential

Transmembrane

949 – 967

Helical; Potential

Topological domain

968 – 982

Extracellular Potential

Transmembrane

983 – 1003

Helical; Potential

Topological domain

1004 – 1020

Cytoplasmic Potential

Region

80 – 82

Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site

374

4-aspartylphosphate intermediate By similarity

Metal binding

714

Magnesium By similarity

Metal binding

718

Magnesium By similarity

Amino acid modifications

Modified residue

570

Phosphothreonine By similarity

Modified residue

587

Phosphoserine By similarity

Modified residue

650

Phosphoserine Ref.3

Modified residue

940

Phosphoserine; by PKA By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6PIE5 [UniParc].

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

FASTA

1,020

112,217

        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' 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: 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.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC036127 mRNA. Translation: AAH36127.1. BC041774 mRNA. Translation: AAH41774.1.
IPI	IPI00420569.
RefSeq	NP_848492.1. NM_178405.3.
UniGene	Mm.207432.
3D structure databases
ProteinModelPortal	Q6PIE5.
SMR	Q6PIE5. Positions 25-1020.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48355N.
MINT	MINT-7543414.
STRING	10090.ENSMUSP00000083077.
PTM databases
PhosphoSite	Q6PIE5.
Proteomic databases
PaxDb	Q6PIE5.
PRIDE	Q6PIE5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000085913; ENSMUSP00000083077; ENSMUSG00000007097.
GeneID	98660.
KEGG	mmu:98660.
UCSC	uc007dqc.1. mouse.
Organism-specific databases
CTD	477.
MGI	MGI:88106. Atp1a2.
Phylogenomic databases
eggNOG	COG0474.
GeneTree	ENSGT00560000076866.
HOVERGEN	HBG004298.
InParanoid	Q6PIE5.
KO	K01539.
OMA	IINIPLP.
OrthoDB	EOG46MBHS.
Gene expression databases
ArrayExpress	Q6PIE5.
Bgee	Q6PIE5.
CleanEx	MM_ATP1A2.
Genevestigator	Q6PIE5.
GermOnline	ENSMUSG00000007097. 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
NextBio	353565.
SOURCE	Search...

Entry information

Entry name

AT1A2_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 93 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