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P30714

- AT1A1_BUFMA

UniProt

P30714 - AT1A1_BUFMA

Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

ATP1A1

Organism
Bufo marinus (Giant toad) (Cane toad)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (16 May 2003)
      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).

    Enzyme regulationi

    This alpha subunit is resistant to ouabain.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei376 – 37614-aspartylphosphate intermediateBy similarity
    Binding sitei487 – 4871ATPBy similarity
    Metal bindingi717 – 7171MagnesiumBy similarity
    Metal bindingi721 – 7211MagnesiumBy 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-EC

    GO - Biological processi

    1. ATP biosynthetic process Source: InterPro

    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
    OrganismiBufo marinus (Giant toad) (Cane toad)
    Taxonomic identifieri8386 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaBufonidaeRhinella

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 55By similarityPRO_0000002501
    Chaini6 – 10231018Sodium/potassium-transporting ATPase subunit alpha-1PRO_0000002502Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151Phosphothreonine; by PKC1 Publication
    Modified residuei16 – 161Phosphoserine; by PKC1 Publication
    Modified residuei943 – 9431Phosphoserine; by PKA1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP30714.

    Expressioni

    Tissue specificityi

    Mainly expressed in kidney. Found in bladder, colon, eye, and testis. Found in low levels in brain, heart, spleen and liver.

    Interactioni

    Subunit structurei

    Composed of three subunits: alpha (catalytic), beta and gamma.

    Structurei

    3D structure databases

    ProteinModelPortaliP30714.
    SMRiP30714. Positions 28-1023.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini6 – 8782CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini109 – 13123ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini153 – 288136CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini309 – 32012ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini339 – 772434CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini793 – 80210ExtracellularSequence Analysis
    Topological domaini824 – 84320CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini867 – 91852ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini939 – 95113CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini971 – 98515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1007 – 102317CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei88 – 10821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei132 – 15221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei289 – 30820HelicalSequence AnalysisAdd
    BLAST
    Transmembranei321 – 33818HelicalSequence AnalysisAdd
    BLAST
    Transmembranei773 – 79220HelicalSequence AnalysisAdd
    BLAST
    Transmembranei803 – 82321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei844 – 86623HelicalSequence AnalysisAdd
    BLAST
    Transmembranei919 – 93820HelicalSequence AnalysisAdd
    BLAST
    Transmembranei952 – 97019HelicalSequence AnalysisAdd
    BLAST
    Transmembranei986 – 100621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni82 – 843Interaction with phosphoinositide-3 kinaseBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG004298.

    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. 1 hit.
    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.

    P30714-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGYGAGRDKY EPAATSEHGG KKGKGKGKDR DMEELKKEVT MEDHKMTLEE     50
    LHRKYGTDLT RGLTTARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF 100
    SMLLWIGAIL CFLAYGIRKA SDLEPDNDNL YLGVVLSAVV IITGCFSYYQ 150
    EAKSSRIMES FKNMVPQQAL VIRNGEKLSI NAENVVQGDL VEVKGGDRIP 200
    ADLRIISAHG CKVDNSSLTG ESEPQTRSPD FTNENPLETR NIAFFSTNCV 250
    EGTARGIVIN TGDRTVMGRI ATLASGLEGG QTPIAVEIGH FIHIITGVAV 300
    FLGVSFFILS LILHYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR 350
    MARKNCLVKN LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA 400
    DTTENQSGAS FDKSSPTWTA LARIAGLCNR AVFPAGQENT PILKRDVVGD 450
    ASESALLKCI ELCCGSVKDM REKNQKVAEI PFNSTNKYQL SVHKNANPSE 500
    SRYLLVMKGA PERILDRCSS ILLQGKEQPL DEELKDAFQN AYLELGGLGE 550
    RVLGFCHLLL DDEQFPDGFS FDTEDVNFPT EGLCFVGLIS MIDPPRAAVP 600
    DRVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI 650
    PVNQVNPRDA KACVIHGTDL KDMNADQIDD ILRHHTEIVF ARTSPQQKLI 700
    IVEGCQRQGA IVAVTGDGVN DSPALKKADI GIAMGIAGSD VSKQAADMIL 750
    LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LIFIIADIPL 800
    PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK KDKLVNERLI 850
    SMAYGQIGMI QALGGFFAYF VILAENGFLP STLLGIRVAW EDRYVNDVED 900
    SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK 950
    NKILIFGLFE ETALAAFLSY CPGMDVALRM YPLKPTWWFC AFPYSLLIFI 1000
    YDEVRKLILR RSPGGWVEKE TYY 1023
    Length:1,023
    Mass (Da):112,617
    Last modified:May 16, 2003 - v2
    Checksum:iD66E8C4028F41BF1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11798 mRNA. Translation: CAA77842.2.
    PIRiA43451. S24650.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11798 mRNA. Translation: CAA77842.2 .
    PIRi A43451. S24650.

    3D structure databases

    ProteinModelPortali P30714.
    SMRi P30714. Positions 28-1023.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P30714.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG004298.

    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. 1 hit.
    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. "Primary sequence and functional expression of a novel ouabain-resistant Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-pump."
      Jaisser F., Canessa C.M., Horisberger J.-D., Rossier B.C.
      J. Biol. Chem. 267:16895-16903(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Urinary bladder urothelium.
    2. Jaisser F.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 835-836.
    3. "Phosphorylation of the Na,K-ATPase alpha-subunit by protein kinase A and C in vitro and in intact cells. Identification of a novel motif for PKC-mediated phosphorylation."
      Beguin P., Beggah A.T., Chibalin A.V., Burgener-Kairuz P., Jaisser F., Mathews P.M., Rossier B.C., Cotecchia S., Geering K.
      J. Biol. Chem. 269:24437-24445(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CAMP-DEPENDENT KINASE AND PROTEIN KINASE C.

    Entry informationi

    Entry nameiAT1A1_BUFMA
    AccessioniPrimary (citable) accession number: P30714
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: May 16, 2003
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3