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P24797 (AT1A2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. 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-2
Short name=Na(+)/K(+) ATPase alpha-2 subunit
EC=3.6.3.9
Alternative name(s):
Sodium pump subunit alpha-2
Gene names
Name:ATP1A2
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length1017 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

Membrane; Multi-pass membrane protein By similarity. Cell membrane; Multi-pass membrane protein By similarity.

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 – 10171017Sodium/potassium-transporting ATPase subunit alpha-2
PRO_0000046297

Regions

Topological domain1 – 8282Cytoplasmic Potential
Transmembrane83 – 10321Helical; Potential
Topological domain104 – 12623Extracellular Potential
Transmembrane127 – 14721Helical; Potential
Topological domain148 – 283136Cytoplasmic Potential
Transmembrane284 – 30320Helical; Potential
Topological domain304 – 31512Extracellular Potential
Transmembrane316 – 33318Helical; Potential
Topological domain334 – 766433Cytoplasmic Potential
Transmembrane767 – 78620Helical; Potential
Topological domain787 – 79610Extracellular Potential
Transmembrane797 – 81721Helical; Potential
Topological domain818 – 83720Cytoplasmic Potential
Transmembrane838 – 86023Helical; Potential
Topological domain861 – 91252Extracellular Potential
Transmembrane913 – 93220Helical; Potential
Topological domain933 – 94513Cytoplasmic Potential
Transmembrane946 – 96419Helical; Potential
Topological domain965 – 97915Extracellular Potential
Transmembrane980 – 100021Helical; Potential
Topological domain1001 – 101717Cytoplasmic Potential
Region77 – 793Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site37114-aspartylphosphate intermediate By similarity
Metal binding7111Magnesium By similarity
Metal binding7151Magnesium By similarity
Binding site5021ATP By similarity

Amino acid modifications

Modified residue9371Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
P24797 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 38E87C1BDE93B8C5

FASTA1,017112,051
        10         20         30         40         50         60 
MDGREYSPAA TTSENGGGRR KQKEKELDEL KKEVNLDDHK LSLDELGRKY QVDLSRGLSN 

        70         80         90        100        110        120 
ARAAEVLAQD GPNALTPPPT TPEWVKFCRQ LFGGFSILLW IGAILCFLAY GIQAAMEDEP 

       130        140        150        160        170        180 
SNDNLYLGVV LAAVVIVTGC FSYYQEAKSS KIMDSFKNMV PQQALVIREG EKIQINAENV 

       190        200        210        220        230        240 
VVGDLVEVKG GDRVPADMRI ISSHGCKVDN SSLTGESEPQ TRSPEFTHEN PLETRNICFF 

       250        260        270        280        290        300 
STNCVEGTAR GIVISTGDRT VMGRIASLAS GLEVGRTPIA MEIEHFIRLI TGVAVFLGLS 

       310        320        330        340        350        360 
FFILSLILGY TWLEAVIFLI GIIVANVPEG LLATVTVCLT LTAKRMARKN CLVKNLEAVE 

       370        380        390        400        410        420 
TLGSTSTICS DKTGTLTQNR MTVAHMWFDN QIHEADTTED QSGATFDKRS PTWAALSRIA 

       430        440        450        460        470        480 
GLCNRAVFKP GQENISISKR DTAGDASESA LLKCIQLSCG SVKKMRDKNP KVTEIPFNST 

       490        500        510        520        530        540 
NKYQLSIHER EEDPQGHILV MKGAPERILE RCSRILLQGQ EVPLDEEMKE AFQNAYLELG 

       550        560        570        580        590        600 
GLGERVLGFC HLYLPPDKFP RGFRFDADEV NFPTSDLCFV GLMSMIDPPR AAVPDAVGKC 

       610        620        630        640        650        660 
RSAGIKVIMV TGDHPITAKA IAKGVGIISE GNETVEDIAA RLNIPVSQVN PREAKACVVH 

       670        680        690        700        710        720 
GSDLKDMTAE QLDEILRNHT EIVFARTSPQ QKLIIVEGCQ RQGAIVAVTG DGVNDSPALK 

       730        740        750        760        770        780 
KADIGIAMGI AGSDVSKQAA DMILLDDNFA SIVTGVEEGR LIFDNLKKSI AYTLTSNIPE 

       790        800        810        820        830        840 
ITPFLLFIIA NIPLPLGTVT ILCIDLGTDM VPAISLAYEA AESDIMKRQP RNPRTDKLVN 

       850        860        870        880        890        900 
ERLISMAYGQ IGMIQALGGF FTYFVILAEN GFLPARLLGV RLAWDDRSTN DLEDSYGQEW 

       910        920        930        940        950        960 
TYEQRKVVEF TCHTAFFASI VVVQWADLII CKTRRNSVFQ QGMKNKILIF GLLEETALAA 

       970        980        990       1000       1010 
FLSYCPGMGV ALRMYPLKVT WWFCAFPYSL LIFAYDEVRK LILRRYPGGW VEKETYY

« Hide

References

[1]"Stability of Na(+)-K(+)-ATPase alpha-subunit isoforms in evolution."
Takeyasu K., Lemas V., Fambrough D.M.
Am. J. Physiol. 259:C619-C630(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M59959 mRNA. Translation: AAA48981.1.
IPIIPI00583240.
PIRA37227. I50394.
RefSeqNP_990807.1. NM_205476.1.
UniGeneGga.4300.

3D structure databases

ProteinModelPortalP24797.
SMRP24797. Positions 22-1017.
ModBaseSearch...

Proteomic databases

PRIDEP24797.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396468.
KEGGgga:396468.

Organism-specific databases

CTD477.

Phylogenomic databases

HOVERGENHBG004298.
KOK01539.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR006068. 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]
PANTHERPTHR24093. PTHR24093. 1 hit.
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.
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...

Other

NextBio20816507.

Entry information

Entry nameAT1A2_CHICK
AccessionPrimary (citable) accession number: P24797
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: May 1, 2013
This is version 108 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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