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P05024

- AT1A1_PIG

UniProt

P05024 - AT1A1_PIG

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Protein
Sodium/potassium-transporting ATPase subunit alpha-1
Gene
ATP1A1
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

ATP + H2O + Na+(In) + K+(Out) = ADP + phosphate + Na+(Out) + K+(In).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei374 – 37414-aspartylphosphate intermediate By similarity
Binding sitei485 – 4851ATP By similarity
Metal bindingi715 – 7151Magnesium By similarity
Metal bindingi719 – 7191Magnesium By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. sodium:potassium-exchanging ATPase activity Source: UniProtKB

GO - Biological processi

  1. ATP biosynthetic process Source: InterPro
  2. regulation of sodium ion transport Source: UniProtKB
  3. sodium ion transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Ion transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Sodium

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium/potassium-transporting ATPase subunit alpha-1 (EC:3.6.3.9)
Short name:
Na(+)/K(+) ATPase alpha-1 subunit
Alternative name(s):
Sodium pump subunit alpha-1
Gene namesi
Name:ATP1A1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini6 – 8580Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei86 – 10621Helical; Reviewed prediction
Add
BLAST
Topological domaini107 – 12923Extracellular Reviewed prediction
Add
BLAST
Transmembranei130 – 15021Helical; Reviewed prediction
Add
BLAST
Topological domaini151 – 286136Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei287 – 30620Helical; Reviewed prediction
Add
BLAST
Topological domaini307 – 31812Extracellular Reviewed prediction
Add
BLAST
Transmembranei319 – 33618Helical; Reviewed prediction
Add
BLAST
Topological domaini337 – 770434Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei771 – 79020Helical; Reviewed prediction
Add
BLAST
Topological domaini791 – 80010Extracellular Reviewed prediction
Transmembranei801 – 82121Helical; Reviewed prediction
Add
BLAST
Topological domaini822 – 84120Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei842 – 86423Helical; Reviewed prediction
Add
BLAST
Topological domaini865 – 91652Extracellular Reviewed prediction
Add
BLAST
Transmembranei917 – 93620Helical; Reviewed prediction
Add
BLAST
Topological domaini937 – 94913Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei950 – 96819Helical; Reviewed prediction
Add
BLAST
Topological domaini969 – 98315Extracellular Reviewed prediction
Add
BLAST
Transmembranei984 – 100421Helical; Reviewed prediction
Add
BLAST
Topological domaini1005 – 102117Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. melanosome Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 55
PRO_0000002487
Chaini6 – 10211016Sodium/potassium-transporting ATPase subunit alpha-1
PRO_0000002488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysine By similarity
Modified residuei10 – 101Phosphotyrosine By similarity
Modified residuei16 – 161Phosphoserine; by PKC By similarity
Modified residuei21 – 211N6-acetyllysine By similarity
Modified residuei258 – 2581Phosphotyrosine By similarity
Modified residuei540 – 5401Phosphotyrosine By similarity
Modified residuei659 – 6591N6-succinyllysine By similarity
Modified residuei941 – 9411Phosphoserine; by PKA By similarity

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP05024.
PRIDEiP05024.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-60365N.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 304
Helixi31 – 333
Beta strandi42 – 443
Helixi46 – 538
Turni57 – 593
Helixi63 – 7311
Helixi86 – 949
Helixi98 – 11922
Beta strandi120 – 1223
Helixi126 – 15530
Helixi157 – 1593
Beta strandi166 – 1694
Beta strandi172 – 1743
Beta strandi176 – 1794
Helixi180 – 1823
Beta strandi185 – 1917
Beta strandi193 – 1964
Beta strandi199 – 21214
Helixi214 – 2174
Beta strandi223 – 2253
Turni234 – 2363
Beta strandi238 – 2414
Beta strandi246 – 25813
Helixi260 – 2623
Helixi264 – 2674
Beta strandi272 – 2743
Helixi281 – 31030
Helixi315 – 32814
Helixi333 – 35018
Turni351 – 3533
Beta strandi354 – 3574
Helixi361 – 3666
Beta strandi370 – 3734
Helixi375 – 3795
Beta strandi385 – 3917
Beta strandi394 – 3974
Beta strandi401 – 4033
Helixi414 – 42512
Beta strandi436 – 4383
Turni440 – 4423
Beta strandi445 – 4473
Helixi449 – 46113
Helixi465 – 4717
Beta strandi474 – 4785
Turni482 – 4843
Beta strandi486 – 4927
Beta strandi495 – 4973
Beta strandi500 – 5078
Helixi509 – 5146
Beta strandi516 – 5216
Beta strandi524 – 5274
Helixi530 – 54516
Beta strandi548 – 55811
Turni560 – 5623
Turni571 – 5744
Beta strandi578 – 59013
Helixi597 – 6059
Turni606 – 6083
Beta strandi610 – 6145
Helixi619 – 62810
Helixi639 – 6468
Helixi650 – 6523
Helixi655 – 6573
Beta strandi659 – 6646
Helixi665 – 6684
Helixi673 – 6819
Beta strandi684 – 6896
Helixi693 – 70513
Beta strandi710 – 7145
Helixi717 – 7193
Helixi720 – 7256
Beta strandi726 – 7327
Turni733 – 7353
Helixi738 – 7436
Beta strandi745 – 7484
Helixi755 – 77925
Helixi781 – 79313
Helixi802 – 81211
Helixi815 – 8195
Turni820 – 8223
Helixi829 – 8313
Turni837 – 8393
Beta strandi842 – 8443
Helixi845 – 8517
Turni852 – 8543
Helixi855 – 87319
Helixi878 – 8814
Turni882 – 8843
Helixi885 – 8884
Beta strandi895 – 8973
Beta strandi899 – 9013
Helixi906 – 93429
Beta strandi938 – 9403
Helixi942 – 9454
Helixi950 – 96819
Helixi972 – 9754
Helixi983 – 9886
Helixi990 – 100920
Beta strandi1010 – 10123
Helixi1016 – 10194

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP05024.
SMRiP05024. Positions 24-1021.

Miscellaneous databases

EvolutionaryTraceiP05024.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 823Phosphoinositide-3 kinase binding By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
KOiK01539.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. 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]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05024-1 [UniParc]FASTAAdd to Basket

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MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH     50
RKYGTDLSRG LTPARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM 100
LLWIGAILCF LAYGIQAATE EEPQNDNLYL GVVLSAVVII TGCFSYYQEA 150
KSSKIMESFK NMVPQQALVI RNGEKMSINA EEVVVGDLVE VKGGDRIPAD 200
LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI AFFSTNCVEG 250
TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL 300
GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA 350
RKNCLVKNLE AVETLGSTST ICSDKTGTLT QNRMTVAHMW SDNQIHEADT 400
TENQSGVSFD KTSATWLALS RIAGLCNRAV FQANQENLPI LKRAVAGDAS 450
ESALLKCIEL CCGSVKEMRE RYTKIVEIPF NSTNKYQLSI HKNPNTAEPR 500
HLLVMKGAPE RILDRCSSIL IHGKEQPLDE ELKDAFQNAY LELGGLGERV 550
LGFCHLFLPD EQFPEGFQFD TDDVNFPLDN LCFVGLISMI DPPRAAVPDA 600
VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISEGNETVE DIAARLNIPV 650
SQVNPRDAKA CVVHGSDLKD MTSEQLDDIL KYHTEIVFAR TSPQQKLIIV 700
EGCQRQGAIV AVTGDGVNDS PASKKADIGV AMGIAGSDVS KQAADMILLD 750
DNFASIVTGV EEGRLIFDNL KKSIAYTLTS NIPEITPFLI FIIANIPLPL 800
GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD KLVNEQLISM 850
AYGQIGMIQA LGGFFTYFVI LAENGFLPIH LLGLRVNWDD RWINDVEDSY 900
GQQWTYEQRK IVEFTCHTPF FVTIVVVQWA DLVICKTRRN SVFQQGMKNK 950
ILIFGLFEET ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD 1000
EVRKLIIRRR PGGWVEKETY Y 1021
Length:1,021
Mass (Da):112,681
Last modified:November 1, 1988 - v1
Checksum:iF369C6273CEB561D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71R → P no nucleotide entry 1 Publication
Sequence conflicti7 – 71R → P no nucleotide entry 1 Publication
Sequence conflicti391 – 3911S → F no nucleotide entry 1 Publication
Sequence conflicti391 – 3911S → F no nucleotide entry 1 Publication
Sequence conflicti517 – 5171S → T no nucleotide entry 1 Publication
Sequence conflicti517 – 5171S → T no nucleotide entry 1 Publication
Sequence conflicti723 – 7231S → L no nucleotide entry 1 Publication
Sequence conflicti723 – 7231S → L no nucleotide entry 1 Publication
Sequence conflicti835 – 8351R → Q no nucleotide entry 1 Publication
Sequence conflicti835 – 8351R → Q no nucleotide entry 1 Publication
Sequence conflicti919 – 9191P → A no nucleotide entry 1 Publication
Sequence conflicti919 – 9191P → A no nucleotide entry 1 Publication
Sequence conflicti923 – 9231T → S no nucleotide entry 1 Publication
Sequence conflicti923 – 9231T → S no nucleotide entry 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03938 mRNA. Translation: CAA27576.1.
M38445 mRNA. Translation: AAA31002.1.
M32512 mRNA. Translation: AAA31004.1.
PIRiB24862.
RefSeqiNP_999414.1. NM_214249.1.
UniGeneiSsc.12630.

Genome annotation databases

GeneIDi397481.
KEGGissc:397481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03938 mRNA. Translation: CAA27576.1 .
M38445 mRNA. Translation: AAA31002.1 .
M32512 mRNA. Translation: AAA31004.1 .
PIRi B24862.
RefSeqi NP_999414.1. NM_214249.1.
UniGenei Ssc.12630.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3B8E X-ray 3.50 A/C 24-1021 [» ]
3KDP X-ray 3.50 A/C 24-1021 [» ]
3N23 X-ray 4.60 A/C 30-1021 [» ]
3N2F X-ray 4.10 A/C 30-1021 [» ]
3WGU X-ray 2.80 A/C 6-1021 [» ]
3WGV X-ray 2.80 A/C 6-1021 [» ]
4HQJ X-ray 4.30 A/C 1-1021 [» ]
4HYT X-ray 3.40 A/C 1-1021 [» ]
ProteinModelPortali P05024.
SMRi P05024. Positions 24-1021.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60365N.

Chemistry

BindingDBi P05024.
ChEMBLi CHEMBL4131.

Proteomic databases

PaxDbi P05024.
PRIDEi P05024.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397481.
KEGGi ssc:397481.

Organism-specific databases

CTDi 476.

Phylogenomic databases

eggNOGi COG0474.
HOGENOMi HOG000265622.
HOVERGENi HBG004298.
KOi K01539.

Miscellaneous databases

EvolutionaryTracei P05024.

Family and domain databases

Gene3Di 1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProi 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 ]
Pfami PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
SMARTi SM00831. Cation_ATPase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsi TIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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. Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 24-1021.

Entry informationi

Entry nameiAT1A1_PIG
AccessioniPrimary (citable) accession number: P05024
Secondary accession number(s): P18874
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi