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Q92123 (AT1A1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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

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

Subcellular location

Cell membrane; Multi-pass membrane protein.

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

Chain1 – 10251025Sodium/potassium-transporting ATPase subunit alpha-1
PRO_0000046296

Regions

Topological domain1 – 8989Cytoplasmic Potential
Transmembrane90 – 11021Helical; Potential
Topological domain111 – 13323Extracellular Potential
Transmembrane134 – 15421Helical; Potential
Topological domain155 – 290136Cytoplasmic Potential
Transmembrane291 – 31020Helical; Potential
Topological domain311 – 32212Extracellular Potential
Transmembrane323 – 34018Helical; Potential
Topological domain341 – 774434Cytoplasmic Potential
Transmembrane775 – 79420Helical; Potential
Topological domain795 – 80410Extracellular Potential
Transmembrane805 – 82521Helical; Potential
Topological domain826 – 84520Cytoplasmic Potential
Transmembrane846 – 86823Helical; Potential
Topological domain869 – 92052Extracellular Potential
Transmembrane921 – 94020Helical; Potential
Topological domain941 – 95313Cytoplasmic Potential
Transmembrane954 – 97219Helical; Potential
Topological domain973 – 98715Extracellular Potential
Transmembrane988 – 100821Helical; Potential
Topological domain1009 – 102517Cytoplasmic Potential
Region84 – 863Interaction with phosphoinositide-3 kinase By similarity
Compositional bias21 – 288Poly-Lys

Sites

Active site37814-aspartylphosphate intermediate By similarity
Metal binding7191Magnesium By similarity
Metal binding7231Magnesium By similarity

Amino acid modifications

Modified residue161Phosphoserine; by PKC By similarity
Modified residue9451Phosphoserine; by PKA By similarity

Experimental info

Sequence conflict91K → Q in AAC59760. Ref.2
Sequence conflict29 – 302Missing in AAC59759. Ref.2
Sequence conflict29 – 302Missing in AAC59760. Ref.2
Sequence conflict311E → D in AAC59760. Ref.2
Sequence conflict61 – 633MQR → LQK in AAC59760. Ref.2
Sequence conflict671T → S in AAC59760. Ref.2
Sequence conflict811A → S in AAC59760. Ref.2
Sequence conflict921V → G in AAC59760. Ref.2
Sequence conflict1021F → L in AAC59760. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q92123 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B5F9B4EB6D86EEA0

FASTA1,025113,084
        10         20         30         40         50         60 
MGYGAGRDKY EPAATSEQGG KKKKGKGKGK EKDMDELKKE VTMEDHKLSL DELHRKFGTD 

        70         80         90        100        110        120 
MQRGLTTARA AEILARDGPN ALTPPPTTPE WVKFCRQLFG GFSMLLWIGA ILCFLAYGIQ 

       130        140        150        160        170        180 
AAMEEEPQND NLYLGVVLSA VVIITGCFSY YQEAKSSKIM ESFKNMVPQQ ALVIRSGEKL 

       190        200        210        220        230        240 
SINAEEVVLG DLVEVKGGDR IPADLRVISS HGCKVDNSSL TGESEPQTRS PDFTNENPLE 

       250        260        270        280        290        300 
TRNIAFFSTN CVEGTARGIV VNTGDRTVMG RIATLASGLD GGRTPIAIEI EHFIHIITGV 

       310        320        330        340        350        360 
AVFLGVSFFI LSLILQYTWL EAVIFLIGII VANVPEGLLA TVTVCLTLTA KRMARKNCLV 

       370        380        390        400        410        420 
KNLEAVETLG STSTICSDKT GTLTQNRMTV AHMWFDNQIH EADTTENQSG ASFDKSSPTW 

       430        440        450        460        470        480 
TALSRVAGLC NRAVFQAGQE NTPILKRDVA GDASESALLK CIELCCGSVR DMREKNHKVA 

       490        500        510        520        530        540 
EIPFNSTNKY QLSVHKNANP SESRYILVMK GAPERILDRC TSIILQGKEQ PLDEELKDAF 

       550        560        570        580        590        600 
QNAYLELGGL GERVLGFCHL ALPDDQFPDG FQFDTEEVNF PTENLCFVGL ISMIDPPRAA 

       610        620        630        640        650        660 
VPDAVGKCRS AGIKVIMVTG DHPITAKAIA KGVGIISEGN ETVEDIAARL NIPVNQVNPR 

       670        680        690        700        710        720 
DAKACVIHGT DLKDMTEEQI DDILRHHTEI VFARTSPQQK LIIVEGCQRQ GAIVAVTGDG 

       730        740        750        760        770        780 
VNDSPALKKA DIGIAMGIAG SDVSKQAADM ILLDDNFASI VTGVEEGRLI FDNLKKSIAY 

       790        800        810        820        830        840 
TLTSNIPEIT PFLIFIIANI PLPLGTVTIL CIDLGTDMVP AISLAYEQAE SDIMKRQPRN 

       850        860        870        880        890        900 
PKTDKLVNER LISMAYGQIG MIQALGGFFT YFVILAENGF LPWTLLGIRV NWDDRWTNDV 

       910        920        930        940        950        960 
EDSYGQQWTY EQRKIVEFTC HTSFFISIVV VQWADLIICK TRRNSVFQQG MKNKILIFGL 

       970        980        990       1000       1010       1020 
FEETALAAFL SYCPGMDVAL RMYPLKPTWW FCAFPYSLII FIYDEVRKLI IRRSPGGWVE 


KESYY

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References

[1]"Primary sequence of Xenopus laevis Na+-K+-ATPase and its localization in A6 kidney cells."
Verrey F., Kairouz P., Schaerer E., Fuentes P., Geering K., Rossier B.C., Kraehenbuhl J.-P.
Am. J. Physiol. 256:F1034-F1043(1989) [PubMed: 2544104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney epithelium.
[2]"Primary sequence and developmental expression pattern of mRNAs and protein for an alpha1 subunit of the sodium pump cloned from the neural plate of Xenopus laevis."
Davies C.S., Messenger N.J., Craig R., Warner A.E.
Dev. Biol. 174:431-447(1996) [PubMed: 8631513] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Neural plate.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U10108 mRNA. Translation: AAA19022.1.
U49238 mRNA. Translation: AAC59759.1.
U49239 mRNA. Translation: AAC59760.1.
PIRA60444.
RefSeqNP_001084064.1. NM_001090595.1.
UniGeneXl.3792.

3D structure databases

ProteinModelPortalQ92123.
SMRQ92123. Positions 30-1025.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID399285.
KEGGxla:399285.

Organism-specific databases

CTD399285.
XenbaseXB-GENE-6254180. atp1a1.

Phylogenomic databases

HOVERGENHBG004298.

Family and domain databases

InterProIPR023306. ATPase_cation_domN.
IPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR005775. ATPase_P-typ_cation-ex_asu_euk.
IPR006069. ATPase_P-typ_cation-exchng_asu.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits.
KOK01539.
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.
PR00121. NAKATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF81660. ATPase_cation_domN. 1 hit.
SSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAT1A1_XENLA
AccessionPrimary (citable) accession number: Q92123
Secondary accession number(s): Q91683, Q92127
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1996
Last modified: November 16, 2011
This is version 97 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

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