Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P05024 (AT1A1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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-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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

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).

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. 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]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 55
PRO_0000002487
Chain6 – 10211016Sodium/potassium-transporting ATPase subunit alpha-1
PRO_0000002488

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 residue6591N6-succinyllysine By similarity
Modified residue9411Phosphoserine; by PKA By similarity

Experimental info

Sequence conflict71R → P no nucleotide entry Ref.3
Sequence conflict71R → P no nucleotide entry Ref.4
Sequence conflict3911S → F no nucleotide entry Ref.3
Sequence conflict3911S → F no nucleotide entry Ref.4
Sequence conflict5171S → T no nucleotide entry Ref.3
Sequence conflict5171S → T no nucleotide entry Ref.4
Sequence conflict7231S → L no nucleotide entry Ref.3
Sequence conflict7231S → L no nucleotide entry Ref.4
Sequence conflict8351R → Q no nucleotide entry Ref.3
Sequence conflict8351R → Q no nucleotide entry Ref.4
Sequence conflict9191P → A no nucleotide entry Ref.3
Sequence conflict9191P → A no nucleotide entry Ref.4
Sequence conflict9231T → S no nucleotide entry Ref.3
Sequence conflict9231T → S no nucleotide entry Ref.4

Secondary structure

........................................................................................................................................................................................ 1021
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05024 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: F369C6273CEB561D

FASTA1,021112,681
        10         20         30         40         50         60 
MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH RKYGTDLSRG 

        70         80         90        100        110        120 
LTPARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM LLWIGAILCF 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 SDNQIHEADT TENQSGVSFD KTSATWLALS 

       430        440        450        460        470        480 
RIAGLCNRAV FQANQENLPI LKRAVAGDAS ESALLKCIEL CCGSVKEMRE RYTKIVEIPF 

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

       550        560        570        580        590        600 
LELGGLGERV LGFCHLFLPD EQFPEGFQFD TDDVNFPLDN LCFVGLISMI DPPRAAVPDA 

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

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

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

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

       850        860        870        880        890        900 
KLVNEQLISM AYGQIGMIQA LGGFFTYFVI LAENGFLPIH LLGLRVNWDD RWINDVEDSY 

       910        920        930        940        950        960 
GQQWTYEQRK IVEFTCHTPF FVTIVVVQWA DLVICKTRRN SVFQQGMKNK ILIFGLFEET 

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


Y 

« Hide

References

[1]"Pig kidney Na+,K+-ATPase. Primary structure and spatial organization."
Ovchinnikov Y.A., Modyanov N.N., Broude N.E., Petrukhin K.E., Grishin A.V., Arzamazova N.M., Aldanova N.A., Monastyrskaya G.S., Sverdlov E.D.
FEBS Lett. 201:237-245(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of cDNA and primary structure of the alpha-subunit of porcine kidney Na(+)-K(+)-ATPase."
Ovchinnikov Y.A., Arsenyan S.G., Broude N.E., Petrukhin K.E., Grishin A.V., Aldanova N.A., Arzamazova N.M., Aristarkhova E.A., Melkov A.M., Smirnov Y.V., Gur'Ev S.O., Monastyrskaya G.S., Modyanov N.N.
Dokl. Biochem. 285:403-407(1986)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Primary structure of the alpha-subunit of Na+,K+-ATPase from the swine kidney. III. Complete nucleotide sequence corresponding to the structural region of the gene."
Monastyrskaya G.S., Broude N.E., Melkov A.M., Smirnov Y.V., Malyshev I.V., Arsenyan S.G., Salomatina I.S., Sverdlov V.E., Grishin A.V., Petrukhin K.E., Modyanov N.N.
Bioorg. Khim. 13:20-26(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Reconstruction of long polynucleotide sequences from fragments using the Iskra-226 personal computer."
Kostetsky P.V., Dobrova I.E.
Bioorg. Khim. 14:515-521(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Amino acid sequence of the 17-kilodalton fragment of the cytoplasmic region of the alpha-subunit of Na+,K+ -ATPase."
Ovchinnikov Y.A., Monastyrskaya G.S., Arsenyan S.G., Broude N.E., Petrukhin K.E., Grishin A.V., Arzamazova N.M., Severtsova I.V., Modyanov N.N.
Dokl. Biochem. 283:270-272(1985)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 469-617.
[6]"Crystal structure of the sodium-potassium pump."
Morth J.P., Pedersen B.P., Toustrup-Jensen M.S., Sorensen T.L., Petersen J., Andersen J.P., Vilsen B., Nissen P.
Nature 450:1043-1049(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 24-1021.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03938 mRNA. Translation: CAA27576.1.
M38445 mRNA. Translation: AAA31002.1.
M32512 mRNA. Translation: AAA31004.1.
PIRB24862.
RefSeqNP_999414.1. NM_214249.1.
UniGeneSsc.12630.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3B8EX-ray3.50A/C24-1021[»]
3KDPX-ray3.50A/C24-1021[»]
3N23X-ray4.60A/C30-1021[»]
3N2FX-ray4.10A/C30-1021[»]
3WGUX-ray2.80A/C6-1021[»]
3WGVX-ray2.80A/C6-1021[»]
4HQJX-ray4.30A/C1-1021[»]
4HYTX-ray3.40A/C1-1021[»]
ProteinModelPortalP05024.
SMRP05024. Positions 24-1021.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60365N.

Chemistry

BindingDBP05024.
ChEMBLCHEMBL4131.

Proteomic databases

PaxDbP05024.
PRIDEP05024.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397481.
KEGGssc:397481.

Organism-specific databases

CTD476.

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265622.
HOVERGENHBG004298.
KOK01539.

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

EvolutionaryTraceP05024.

Entry information

Entry nameAT1A1_PIG
AccessionPrimary (citable) accession number: P05024
Secondary accession number(s): P18874
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1988
Last modified: July 9, 2014
This is version 128 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references