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P06687 (AT1A3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

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.

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

ATP hydrolysis coupled proton transport

Traceable author statement Ref.3. Source: RGD

adult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

ionotropic glutamate receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from electronic annotation. Source: Ensembl

potassium ion transport

Inferred from direct assay PubMed 12093728. Source: RGD

response to drug

Inferred from electronic annotation. Source: Ensembl

sodium ion transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

sodium ion transport

Inferred from direct assay PubMed 12093728. Source: RGD

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

axon

Inferred from direct assay PubMed 12617948. Source: RGD

dendritic spine head

Inferred from direct assay PubMed 21809413. Source: RGD

dendritic spine neck

Inferred from direct assay PubMed 21809413. Source: RGD

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

myelin sheath

Inferred from direct assay PubMed 12617948. Source: RGD

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

sodium:potassium-exchanging ATPase complex

Inferred from direct assay PubMed 12093728. Source: RGD

synapse

Inferred from direct assay PubMed 16630822. Source: UniProtKB

   Molecular_functionATP binding

Traceable author statement Ref.3. Source: RGD

D1 dopamine receptor binding

Inferred from physical interaction PubMed 21809413. Source: RGD

cation-transporting ATPase activity

Traceable author statement Ref.3. Source: RGD

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_0000046300

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 By similarity
Modified residue5481Phosphotyrosine By similarity
Modified residue9331Phosphoserine; by PKA By similarity

Experimental info

Sequence conflict1 – 33MGD → MNL in AAA41672. Ref.3
Sequence conflict1041A → R in AAA41672. Ref.3
Sequence conflict1141D → E in AAA41672. Ref.3
Sequence conflict1281A → G in AAA41672. Ref.3
Sequence conflict1491E → Q in AAA41672. Ref.3
Sequence conflict1521K → T in AAA41672. Ref.3
Sequence conflict1661E → D in AAA41672. Ref.3
Sequence conflict192 – 1943DLR → ELG in AAA41672. Ref.3
Sequence conflict2001G → R in AAA41672. Ref.3
Sequence conflict3391Missing in AAA41672. Ref.3
Sequence conflict6211V → K in AAA41672. Ref.3
Sequence conflict807 – 8093VPA → DPT in AAA41672. Ref.3
Sequence conflict9081C → F in AAA40777. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P06687 [UniParc].

Last modified October 18, 2001. Version 2.
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

[1]"Molecular cloning of three distinct forms of the Na+,K+-ATPase alpha-subunit from rat brain."
Shull G.E., Greeb J., Lingrel J.B.
Biochemistry 25:8125-8132(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Primary structures of two types of alpha-subunit of rat brain Na+,K+,-ATPase deduced from cDNA sequences."
Hara Y., Urayama O., Kawakami K., Nojima H., Nagamune H., Kojima T., Ohta T., Nagano K., Nakao M.
J. Biochem. 102:43-58(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Three differentially expressed Na,K-ATPase alpha subunit isoforms: structural and functional implications."
Herrera V.L.M., Emanuel J.R., Ruiz-Opazo N., Levenson R., Nadal-Ginard B.
J. Cell Biol. 105:1855-1865(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-930.
Tissue: Brain and Liver.
[4]Lubec G., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 58-64; 147-152; 246-254; 260-271; 425-434; 436-448; 517-525; 587-595; 620-648; 734-763 AND 878-883, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14513 mRNA. Translation: AAA40777.1.
X05883 mRNA. Translation: CAA29307.1.
M28648 mRNA. Translation: AAA41672.1.
PIRC24639.
RefSeqNP_036638.1. NM_012506.1.
UniGeneRn.87329.

3D structure databases

ProteinModelPortalP06687.
SMRP06687. Positions 20-1013.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246401. 5 interactions.
IntActP06687. 1 interaction.
MINTMINT-7138201.

PTM databases

PhosphoSiteP06687.

Proteomic databases

PaxDbP06687.
PRIDEP06687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027497; ENSRNOP00000027497; ENSRNOG00000020263.
GeneID24213.
KEGGrno:24213.
UCSCRGD:2169. rat.

Organism-specific databases

CTD478.
RGD2169. Atp1a3.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00560000076866.
HOGENOMHOG000265622.
HOVERGENHBG004298.
KOK01539.
OMAFQTHPEN.
OrthoDBEOG7327N0.

Enzyme and pathway databases

SABIO-RKP06687.

Gene expression databases

GenevestigatorP06687.

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

NextBio602625.

Entry information

Entry nameAT1A3_RAT
AccessionPrimary (citable) accession number: P06687
Secondary accession number(s): Q16732, Q9Z1G6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 18, 2001
Last modified: April 16, 2014
This is version 139 of the entry and version 2 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