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P04074 (AT1A1_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. 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-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
OrganismOvis aries (Sheep) [Reference proteome]
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

Sequence length1021 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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).

Enzyme regulation

Specifically inhibited by cardiac glycosides such as digoxin or ouabain.

Subunit structure

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

Subcellular location

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

Post-translational modification

Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-941 by PKA modulates the response of ATP1A1 to PKC By similarity. 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 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
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

negative regulation of glucocorticoid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of heart contraction

Inferred from electronic annotation. Source: Ensembl

positive regulation of heart contraction

Inferred from electronic annotation. Source: Ensembl

positive regulation of striated muscle contraction

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

regulation of sodium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of the force of heart contraction

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

sodium ion transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

   Cellular_componentT-tubule

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

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

Propeptide1 – 55 By similarity
PRO_0000002491
Chain6 – 10211016Sodium/potassium-transporting ATPase subunit alpha-1
PRO_0000002492

Regions

Topological domain6 – 8580Cytoplasmic Potential
Transmembrane86 – 10621Helical; Potential
Topological domain107 – 12923Extracellular Potential
Transmembrane130 – 15021Helical; Potential
Topological domain151 – 286136Cytoplasmic Potential
Transmembrane287 – 30620Helical; Potential
Topological domain307 – 31812Extracellular Potential
Transmembrane319 – 33618Helical; Potential
Topological domain337 – 770434Cytoplasmic Potential
Transmembrane771 – 79020Helical; Potential
Topological domain791 – 80010Extracellular Potential
Transmembrane801 – 82121Helical; Potential
Topological domain822 – 84120Cytoplasmic Potential
Transmembrane842 – 86423Helical; Potential
Topological domain865 – 91652Extracellular Potential
Transmembrane917 – 93620Helical; Potential
Topological domain937 – 94913Cytoplasmic Potential
Transmembrane950 – 96819Helical; Potential
Topological domain969 – 98315Extracellular Potential
Transmembrane984 – 100421Helical; Potential
Topological domain1005 – 102117Cytoplasmic Potential
Region80 – 823Phosphoinositide-3 kinase binding By similarity

Sites

Active site37414-aspartylphosphate intermediate By similarity
Metal binding7151Magnesium By similarity
Metal binding7191Magnesium By similarity
Binding site4851ATP By similarity

Amino acid modifications

Modified residue91N6-acetyllysine By similarity
Modified residue101Phosphotyrosine By similarity
Modified residue161Phosphoserine; by PKC By similarity
Modified residue211N6-acetyllysine By similarity
Modified residue2581Phosphotyrosine By similarity
Modified residue5401Phosphotyrosine By similarity
Modified residue9411Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
P04074 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: 0D493D95BD9D4312

FASTA1,021112,658
        10         20         30         40         50         60 
MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH RKYGTDLNRG 

        70         80         90        100        110        120 
LTTARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM LLWIGAVLCF LAYGIQAATE 

       130        140        150        160        170        180 
EEPQNDNLYL GVVLSAVVII TGCFSYYQEA KSSKIMESFK NMVPQQALVI RNGEKMSINA 

       190        200        210        220        230        240 
EEVVVGDLVE VKGGDRIPAD LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI 

       250        260        270        280        290        300 
AFFSTNCVEG TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL 

       310        320        330        340        350        360 
GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE 

       370        380        390        400        410        420 
AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TENQSGVSFD KTSATWLALS 

       430        440        450        460        470        480 
RIAGLCNRAV FQANQDNLPI LKRAVAGDAS ESALLKCIEV CCGSVKEMRE RYAKIVEIPF 

       490        500        510        520        530        540 
NSTNKYQLSI HKNANAGEPR HLLVMKGAPE RILDRCSSIL IHGKEQPLDE ELKDAFQNAY 

       550        560        570        580        590        600 
LELGGLGERV LGFCHLMLPD EQFPEGFQFD TDDVNFPVDN LCFVGLISMI DPPRAAVPDA 

       610        620        630        640        650        660 
VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISEGNETVE DIAARLNIPV SQVNPRDARA 

       670        680        690        700        710        720 
CVVHGSDLKD MTPEQLDDIL KYHTEIVFAR TSPQQKLIIV EGCQRQGAIV AVTGDGVNDS 

       730        740        750        760        770        780 
PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS 

       790        800        810        820        830        840 
NIPEITPFLI FIIANIPLPL GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPQTD 

       850        860        870        880        890        900 
KLVNERLISM AYGQIGMIQA LGGFFTYFVI MAENGFLPNH LLGIRVTWDD RWINDVEDSY 

       910        920        930        940        950        960 
GQQWTYEQRK IVEFTCHTAF FVSIVVVQWA DLVICKTRRN SVFQQGMKNK ILIFGLFEET 

       970        980        990       1000       1010       1020 
ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD EVRKLIIRRR PGGWVEKETY 


Y 

« Hide

References

[1]"Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA."
Shull G.E., Schwartz A., Lingrel J.B.
Nature 316:691-695(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"Lysine 480 is an essential residue in the putative ATP site of lamb kidney (Na,K)-ATPase. Identification of the pyridoxal 5'-diphospho-5'-adenosine and pyridoxal phosphate reactive residue."
Hinz H.R., Kirley T.L.
J. Biol. Chem. 265:10260-10265(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 475-492.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02813 mRNA. Translation: CAA26581.1.
X02813 mRNA. Translation: CAA26582.1.
PIRPWSHNA. A01074.
RefSeqNP_001009360.1. NM_001009360.1.
UniGeneOar.424.

3D structure databases

ProteinModelPortalP04074.
SMRP04074. Positions 24-1021.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOART00000022009; ENSOARP00000021706; ENSOARG00000020213.
GeneID443381.

Organism-specific databases

CTD476.

Phylogenomic databases

GeneTreeENSGT00560000076866.
HOVERGENHBG004298.

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...

Entry information

Entry nameAT1A1_SHEEP
AccessionPrimary (citable) accession number: P04074
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: July 9, 2014
This is version 120 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