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P05024

- AT1A1_PIG

UniProt

P05024 - AT1A1_PIG

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
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    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 intermediateBy similarity
    Binding sitei485 – 4851ATPBy similarity
    Metal bindingi715 – 7151MagnesiumBy similarity
    Metal bindingi719 – 7191MagnesiumBy 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

    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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91N6-acetyllysineBy similarity
    Modified residuei10 – 101PhosphotyrosineBy similarity
    Modified residuei16 – 161Phosphoserine; by PKCBy similarity
    Modified residuei21 – 211N6-acetyllysineBy similarity
    Modified residuei258 – 2581PhosphotyrosineBy similarity
    Modified residuei540 – 5401PhosphotyrosineBy similarity
    Modified residuei659 – 6591N6-succinyllysineBy similarity
    Modified residuei941 – 9411Phosphoserine; by PKABy 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.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP05024.
    PRIDEiP05024.

    Interactioni

    Subunit structurei

    Interacts with SIK1 By similarity. Interacts with SLC35G1 and STIM1 By similarity. Composed of three subunits: alpha (catalytic), beta and gamma.By similarity

    Protein-protein interaction databases

    DIPiDIP-60365N.

    Structurei

    Secondary structure

    1
    1021
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05024.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini6 – 8580CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini107 – 12923ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini151 – 286136CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini307 – 31812ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini337 – 770434CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini791 – 80010ExtracellularSequence Analysis
    Topological domaini822 – 84120CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini865 – 91652ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini937 – 94913CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini969 – 98315ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1005 – 102117CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei86 – 10621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei130 – 15021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei287 – 30620HelicalSequence AnalysisAdd
    BLAST
    Transmembranei319 – 33618HelicalSequence AnalysisAdd
    BLAST
    Transmembranei771 – 79020HelicalSequence AnalysisAdd
    BLAST
    Transmembranei801 – 82121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei842 – 86423HelicalSequence AnalysisAdd
    BLAST
    Transmembranei917 – 93620HelicalSequence AnalysisAdd
    BLAST
    Transmembranei950 – 96819HelicalSequence AnalysisAdd
    BLAST
    Transmembranei984 – 100421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni80 – 823Phosphoinositide-3 kinase bindingBy 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

    « Hide

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71R → P no nucleotide entry (PubMed:3032208)Curated
    Sequence conflicti7 – 71R → P no nucleotide entry (PubMed:2844194)Curated
    Sequence conflicti391 – 3911S → F no nucleotide entry (PubMed:3032208)Curated
    Sequence conflicti391 – 3911S → F no nucleotide entry (PubMed:2844194)Curated
    Sequence conflicti517 – 5171S → T no nucleotide entry (PubMed:3032208)Curated
    Sequence conflicti517 – 5171S → T no nucleotide entry (PubMed:2844194)Curated
    Sequence conflicti723 – 7231S → L no nucleotide entry (PubMed:3032208)Curated
    Sequence conflicti723 – 7231S → L no nucleotide entry (PubMed:2844194)Curated
    Sequence conflicti835 – 8351R → Q no nucleotide entry (PubMed:3032208)Curated
    Sequence conflicti835 – 8351R → Q no nucleotide entry (PubMed:2844194)Curated
    Sequence conflicti919 – 9191P → A no nucleotide entry (PubMed:3032208)Curated
    Sequence conflicti919 – 9191P → A no nucleotide entry (PubMed:2844194)Curated
    Sequence conflicti923 – 9231T → S no nucleotide entry (PubMed:3032208)Curated
    Sequence conflicti923 – 9231T → S no nucleotide entry (PubMed:2844194)Curated

    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: October 1, 2014
    This is version 129 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