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P24798 (AT1A3_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium/potassium-transporting ATPase subunit alpha-3

Short name=Na(+)/K(+) ATPase alpha-3 subunit
EC=3.6.3.9
Alternative name(s):
Na(+)/K(+) ATPase alpha(III) subunit
Sodium pump subunit alpha-3
Gene names
Name:ATP1A3
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length1010 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 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 – 10101010Sodium/potassium-transporting ATPase subunit alpha-3
PRO_0000046301

Regions

Topological domain1 – 7474Cytoplasmic Potential
Transmembrane75 – 9521Helical; Potential
Topological domain96 – 11823Extracellular Potential
Transmembrane119 – 13921Helical; Potential
Topological domain140 – 275136Cytoplasmic Potential
Transmembrane276 – 29520Helical; Potential
Topological domain296 – 30712Extracellular Potential
Transmembrane308 – 32518Helical; Potential
Topological domain326 – 759434Cytoplasmic Potential
Transmembrane760 – 77920Helical; Potential
Topological domain780 – 78910Extracellular Potential
Transmembrane790 – 81021Helical; Potential
Topological domain811 – 83020Cytoplasmic Potential
Transmembrane831 – 85323Helical; Potential
Topological domain854 – 90552Extracellular Potential
Transmembrane906 – 92520Helical; Potential
Topological domain926 – 93813Cytoplasmic Potential
Transmembrane939 – 95719Helical; Potential
Topological domain958 – 97215Extracellular Potential
Transmembrane973 – 99321Helical; Potential
Topological domain994 – 101017Cytoplasmic Potential
Region69 – 713Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site36314-aspartylphosphate intermediate By similarity
Metal binding7041Magnesium By similarity
Metal binding7081Magnesium By similarity

Amino acid modifications

Modified residue9301Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
P24798 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 71526BC25633BFA6

FASTA1,010111,284
        10         20         30         40         50         60 
MGDKGEKESP KKGKGKRDLD DLKKEVAMTE HKMSIEEVCR KYNTDCVQGL THSKAQEILA 

        70         80         90        100        110        120 
RDGPNALTPP PTTPEWVKFC RQLFGGFSIL LWIGAILCFL AYGIQAGTED EPSNDNLYLG 

       130        140        150        160        170        180 
IVLAAVVIIT GCFSYYQEAK SSKIMESFKN MVPQQALVIR EGEKMQLNAE EVVVGDLVEV 

       190        200        210        220        230        240 
KGGDRVPADL RIISAHGCKV DNSSLTGESE PQTRSPDCTH DNPLETRNIT FFSTNCVEGT 

       250        260        270        280        290        300 
ARGVVIATGD RTVMGRIATL ASGLEVGKTP IAVEIEHFIQ LITGVAVFLG ISFFVLSLIL 

       310        320        330        340        350        360 
GYTWLEAVIF LIGIIVANVP EGLLATVTVC LTLTAKRMAR KNCLVKNLEA VETLGSTSTI 

       370        380        390        400        410        420 
CSDKTGTLTQ NRMTVAHMWF DNQIHEADTT EDQSGTSFDK SSATWVALSH IAGLCNRAVF 

       430        440        450        460        470        480 
KGGQENVPIL KRDVAGDASE SALLKCIELS SGSVKVMRER NKKVAEIPFN STNKYQLSIH 

       490        500        510        520        530        540 
ETEDPNDNRY LLVMKGAPER ILDRCSTILL QGKEQPLDEE MKEAFQNAYL ELGGLGERVL 

       550        560        570        580        590        600 
GFCHFYLPEE QYPKGFAFDC DDVNFATDNL CFVGLMSMID PPRAAVPDAV GKCRSAGIKV 

       610        620        630        640        650        660 
IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPVS QVNPRDAKAC VIHGTDLKDM 

       670        680        690        700        710        720 
SSEQIDEILQ NHTEIVFART SPQQKLIIVE GCQRQGAIVA VTGDGVNDSP ALKKADIGVA 

       730        740        750        760        770        780 
MGIRGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN IPEITPFLLF 

       790        800        810        820        830        840 
IMANIPLPLG TITILCIDLG TDMVPAISLA YEAAESDIMK RQPRNPRSDK LVNERLISMA 

       850        860        870        880        890        900 
YGQIGMIQAL GGFFSYFVIL AENGFLPSCL VGIRLSWDDR TINDLEDSYG QQWTYEQRKV 

       910        920        930        940        950        960 
VEFTCHTAFF VSIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLFEETA LAAFLSYCPG 

       970        980        990       1000       1010 
MDVALRMYPL KPSWWFCAFP YSFLIFVYDE IRKLILRRNP GGWVEKETYY 

« 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
M59960 mRNA. Translation: AAA48982.1.
PIRB37227.
RefSeqNP_990806.1. NM_205475.1.
UniGeneGga.838.

3D structure databases

ProteinModelPortalP24798.
SMRP24798. Positions 13-1010.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP24798.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396467.
KEGGgga:396467.

Organism-specific databases

CTD478.

Phylogenomic databases

HOVERGENHBG004298.
KOK01539.
PhylomeDBP24798.

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]
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]
SUPFAMSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 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

NextBio20816506.

Entry information

Entry nameAT1A3_CHICK
AccessionPrimary (citable) accession number: P24798
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 111 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