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Q6PIC6 (AT1A3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. 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-3

Short name=Na(+)/K(+) ATPase alpha-3 subunit
EC=3.6.3.9
Alternative name(s):
Na(+)/K(+) ATPase alpha(III) subunit
Sodium pump subunit alpha-3
Gene names
Name:Atp1a3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1013 AA.
Sequence statusComplete.
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

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

adult locomotory behavior

Inferred from mutant phenotype PubMed 17234593. Source: MGI

ionotropic glutamate receptor signaling pathway

Inferred from mutant phenotype PubMed 17234593. Source: MGI

memory

Inferred from mutant phenotype PubMed 17234593. Source: MGI

response to drug

Inferred from mutant phenotype PubMed 17234593. Source: MGI

sodium ion transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

visual learning

Inferred from mutant phenotype PubMed 17234593. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 10837135. Source: MGI

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay PubMed 10837135. Source: MGI

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

synapse

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10131013Sodium/potassium-transporting ATPase subunit alpha-3
PRO_0000046299

Regions

Topological domain1 – 7777Cytoplasmic Potential
Transmembrane78 – 9821Helical; Potential
Topological domain99 – 12123Extracellular Potential
Transmembrane122 – 14221Helical; Potential
Topological domain143 – 278136Cytoplasmic Potential
Transmembrane279 – 29820Helical; Potential
Topological domain299 – 31012Extracellular Potential
Transmembrane311 – 32818Helical; Potential
Topological domain329 – 762434Cytoplasmic Potential
Transmembrane763 – 78220Helical; Potential
Topological domain783 – 79210Extracellular Potential
Transmembrane793 – 81321Helical; Potential
Topological domain814 – 83320Cytoplasmic Potential
Transmembrane834 – 85623Helical; Potential
Topological domain857 – 90852Extracellular Potential
Transmembrane909 – 92820Helical; Potential
Topological domain929 – 94113Cytoplasmic Potential
Transmembrane942 – 96019Helical; Potential
Topological domain961 – 97515Extracellular Potential
Transmembrane976 – 99621Helical; Potential
Topological domain997 – 101317Cytoplasmic Potential
Region72 – 743Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site36614-aspartylphosphate intermediate By similarity
Metal binding7071Magnesium By similarity
Metal binding7111Magnesium By similarity

Amino acid modifications

Modified residue2651Phosphoserine Ref.3
Modified residue5481Phosphotyrosine Ref.4
Modified residue9331Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6PIC6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 72F051406284EA8A

FASTA1,013111,692
        10         20         30         40         50         60 
MGDKKDDKSS PKKSKAKERR DLDDLKKEVA MTEHKMSVEE VCRKYNTDCV QGLTHSKAQE 

        70         80         90        100        110        120 
ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SILLWIGAIL CFLAYGIQAG TEDDPSGDNL 

       130        140        150        160        170        180 
YLGIVLAAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIREGEKMQV NAEEVVVGDL 

       190        200        210        220        230        240 
VEIKGGDRVP ADLRIISAHG CKVDNSSLTG ESEPQTRSPD CTHDNPLETR NITFFSTNCV 

       250        260        270        280        290        300 
EGTARGVVVA TGDRTVMGRI ATLASGLEVG KTPIAIEIEH FIQLITGVAV FLGVSFFILS 

       310        320        330        340        350        360 
LILGYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN LEAVETLGST 

       370        380        390        400        410        420 
STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTEDQSGTS FDKSSHTWVA LSHIAGLCNR 

       430        440        450        460        470        480 
AVFKGGQDNI PVLKRDVAGD ASESALLKCI ELSSGSVKLM RERNKKVAEI PFNSTNKYQL 

       490        500        510        520        530        540 
SIHETEDPND NRYLLVMKGA PERILDRCAT ILLQGKEQPL DEEMKEAFQN AYLELGGLGE 

       550        560        570        580        590        600 
RVLGFCHYYL PEEQFPKGFA FDCDDVNFTT DNLCFVGLMS MIDPPRAAVP DAVGKCRSAG 

       610        620        630        640        650        660 
IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA KACVIHGTDL 

       670        680        690        700        710        720 
KDFTSEQIDE ILQNHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN DSPALKKADI 

       730        740        750        760        770        780 
GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF 

       790        800        810        820        830        840 
LLFIMANIPL PLGTITILCI DLGTDMVPAI SLAYEAAESD IMKRQPRNPR TDKLVNERLI 

       850        860        870        880        890        900 
SMAYGQIGMI QALGGFFSYF VILAENGFLP GNLVGIRLNW DDRTVNDLED SYGQQWTYEQ 

       910        920        930        940        950        960 
RKVVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE ETALAAFLSY 

       970        980        990       1000       1010 
CPGMDVALRM YPLKPSWWFC AFPYSFLIFV YDEIRKLILR RNPGGWVEKE 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].
Tissue: Eye.
[2]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 21-27; 36-81; 153-163; 168-184; 203-254; 260-271; 350-367; 404-420; 425-434; 436-458; 466-492; 517-557; 587-595; 603-615; 620-648; 652-682; 689-764; 878-901; 931-940; 943-969 AND 1001-1009.
Strain: C57BL/6.
Tissue: Brain.
[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-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC034645 mRNA. Translation: AAH34645.1.
BC037206 mRNA. Translation: AAH37206.1.
BC042894 mRNA. Translation: AAH42894.1.
RefSeqXP_006539912.1. XM_006539849.1.
UniGeneMm.44101.

3D structure databases

ProteinModelPortalQ6PIC6.
SMRQ6PIC6. Positions 20-1013.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ6PIC6. 6 interactions.

PTM databases

PhosphoSiteQ6PIC6.

Proteomic databases

PaxDbQ6PIC6.
PRIDEQ6PIC6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080882; ENSMUSP00000079691; ENSMUSG00000040907.
GeneID232975.
UCSCuc009frf.1. mouse.

Organism-specific databases

MGIMGI:88107. Atp1a3.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00560000076866.
HOGENOMHOG000265622.
HOVERGENHBG004298.

Gene expression databases

ArrayExpressQ6PIC6.
BgeeQ6PIC6.
CleanExMM_ATP1A3.
GenevestigatorQ6PIC6.

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. 3 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

ChiTaRSATP1A3. mouse.
PROQ6PIC6.
SOURCESearch...

Entry information

Entry nameAT1A3_MOUSE
AccessionPrimary (citable) accession number: Q6PIC6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 91 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