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P50997

- AT1A1_CANFA

UniProt

P50997 - AT1A1_CANFA

Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

ATP1A1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: 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 – 55By similarityPRO_0000002479
    Chaini6 – 10211016Sodium/potassium-transporting ATPase subunit alpha-1PRO_0000002480Add
    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

    PaxDbiP50997.
    PRIDEiP50997.

    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

    STRINGi9615.ENSCAFP00000014393.

    Structurei

    3D structure databases

    ProteinModelPortaliP50997.
    SMRiP50997. Positions 24-1021.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini4 – 8582CytoplasmicSequence 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.
    InParanoidiP50997.
    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.

    P50997-1 [UniParc]FASTAAdd to Basket

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    MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH     50
    RKYGTDLSRG LTTARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM 100
    LLWIGAILCF LAYGIQAATE EEPQNDNLYL GVVLSAVVII TGCFSYYQEA 150
    KSSKIMESFK NMVPQQALVI RNGEKMSINA EEVVIGDLVE VKGGDRIPAD 200
    LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI AFFSTNCVKG 250
    TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL 300
    GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA 350
    RKNCLVKNLE AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT 400
    TENQSGVSFD KSSATWLALS RIAGLCNRAV FQANQENLPI LKRAVAGDAS 450
    ESALLKCIEL CCGSVKEMRD RYAKIVEIPF NSTNKYQLSI HKNPNTSEPR 500
    HLLVMKGAPE RILDRCSSIL LHGKEQPLDE ELKDALQNAY LELGGLGERV 550
    LGFRHLFLPD EQFPEGFQFD TDDVNFPVEN LCFVGFISMI GPPRAAVPDA 600
    VGKCRGAGIK VIMVTGDHPI TAKAIAKGAG IISEGNETVE DIAARLNIPV 650
    RQVNPRDAKA CVVHGSDLKD MTSEQLDGIL KYHTEIVFAR TSPQQKLIIV 700
    EGCQRQGAIV AVTGDGVNDS PALKKADIGV AMGIVGSDAS KQAADMILLD 750
    DNFASIVTGV EEGRLIFDNL KKSIAYTLTS NIPEITPFLI FIIANIPLPL 800
    GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD KLVNERLISM 850
    AYGQIGMIQA LGGFFTYFVI LAENGFLPTH LLGLRVDWDD RWINDVEDSY 900
    GQQWTYEQRK IVEFTCHTAF FVSIVVVQWA DLVICKTRRN SVFQQGMKNK 950
    ILIFGLFEET ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD 1000
    EVRKLIIRRR PGGWVEKETY Y 1021
    Length:1,021
    Mass (Da):112,667
    Last modified:October 1, 1996 - v1
    Checksum:i938A19AA487CBEAA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti109 – 1091C → Y in CAA46950. (PubMed:1316269)Curated
    Sequence conflicti185 – 1851I → V in CAA46950. (PubMed:1316269)Curated
    Sequence conflicti249 – 2491K → E in CAA46950. (PubMed:1316269)Curated
    Sequence conflicti309 – 3091L → F in CAA46950. (PubMed:1316269)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42173 mRNA. Translation: AAA67372.1.
    X66174 mRNA. Translation: CAA46950.1.
    RefSeqiNP_001003306.1. NM_001003306.1.
    UniGeneiCfa.3039.

    Genome annotation databases

    GeneIDi403992.
    KEGGicfa:403992.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42173 mRNA. Translation: AAA67372.1 .
    X66174 mRNA. Translation: CAA46950.1 .
    RefSeqi NP_001003306.1. NM_001003306.1.
    UniGenei Cfa.3039.

    3D structure databases

    ProteinModelPortali P50997.
    SMRi P50997. Positions 24-1021.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000014393.

    Chemistry

    BindingDBi P50997.
    ChEMBLi CHEMBL4838.

    Proteomic databases

    PaxDbi P50997.
    PRIDEi P50997.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 403992.
    KEGGi cfa:403992.

    Organism-specific databases

    CTDi 476.

    Phylogenomic databases

    eggNOGi COG0474.
    HOGENOMi HOG000265622.
    HOVERGENi HBG004298.
    InParanoidi P50997.
    KOi K01539.

    Miscellaneous databases

    NextBioi 20817480.

    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. "Cloning of the dog Na/K-ATPase alpha 1 subunit."
      Xie Z., Li H., Liu G., Wang Y., Askari A., Mercer R.W.
      (In) Bamberg E., Schoner W. (eds.); The sodium pump, pp.49-52, Springer-Verlag, New York (1994)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Mutation of a cysteine in the first transmembrane segment of Na,K-ATPase alpha subunit confers ouabain resistance."
      Canessa C.M., Horisberger J.-D., Louvard D., Rossier B.C.
      EMBO J. 11:1681-1687(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 92-311.
      Strain: Cocker spaniel.
      Tissue: Kidney.

    Entry informationi

    Entry nameiAT1A1_CANFA
    AccessioniPrimary (citable) accession number: P50997
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 112 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3