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Q5RCD8 (AT1A2_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. 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-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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length1020 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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, providing the energy for active transport of various nutrients By similarity.

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

Propeptide1 – 55 By similarity
PRO_0000305983
Chain6 – 10201015Sodium/potassium-transporting ATPase subunit alpha-2 By similarity
PRO_0000305984

Regions

Topological domain6 – 8580Cytoplasmic Potential
Transmembrane86 – 10621Helical; Potential
Topological domain107 – 12923Extracellular Potential
Transmembrane130 – 15021Helical; Potential
Topological domain151 – 286136Cytoplasmic Potential
Transmembrane287 – 30620Helical; Potential
Topological domain307 – 31812Extracellular Potential
Transmembrane319 – 33618Helical; Potential
Topological domain337 – 769433Cytoplasmic Potential
Transmembrane770 – 78920Helical; Potential
Topological domain790 – 79910Extracellular Potential
Transmembrane800 – 82021Helical; Potential
Topological domain821 – 84020Cytoplasmic Potential
Transmembrane841 – 86323Helical; Potential
Topological domain864 – 91552Extracellular Potential
Transmembrane916 – 93520Helical; Potential
Topological domain936 – 94813Cytoplasmic Potential
Transmembrane949 – 96719Helical; Potential
Topological domain968 – 98215Extracellular Potential
Transmembrane983 – 100321Helical; Potential
Topological domain1004 – 102017Cytoplasmic Potential
Region80 – 823Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site37414-aspartylphosphate intermediate By similarity
Metal binding7141Magnesium By similarity
Metal binding7181Magnesium By similarity

Amino acid modifications

Modified residue5701Phosphothreonine By similarity
Modified residue5871Phosphoserine By similarity
Modified residue9401Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RCD8 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: D4357A2367971D59

FASTA1,020112,250
        10         20         30         40         50         60 
MGRGAGREYS PAATTAENGG GKKKQKEKEL DELKKEVAMD DHKLSLDELG RKYQVDLSKG 

        70         80         90        100        110        120 
LTNQRAQDVL ARDGPNALTP PPTTPEWVKF CRQLFGGFSI LLWIGAILCF LAYGIQAAME 

       130        140        150        160        170        180 
DEPSNDNLYL GVVLAAVVIV TGCFSYYQEA KSSKIMDSFK NMVPQQALVI REGEKMQINA 

       190        200        210        220        230        240 
EEVVVGDLVE VKGGDRVPAD LRIISSHGCK VDNSSLTGES EPQTRSPEFT HENPLETRNI 

       250        260        270        280        290        300 
CFFSTNCVEG TARGIVIATG DRTVMGRIAT LASGLEVGRT PIAMEIEHFI QLITGVAVFP 

       310        320        330        340        350        360 
GVSFFVLSLI LGYSWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE 

       370        380        390        400        410        420 
AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIREADT TEDQSGATFD KRSPTWTALS 

       430        440        450        460        470        480 
RIAGLCNRAV FKAGQENISV SKRDTAGDAS ESALLKCIEL SCGSVRKMRD RNPKVAEIPF 

       490        500        510        520        530        540 
NSTNKYQLSI HEREDSPQSH VLVMKGAPER ILDRCPTILV QGKEIPLDKE MQDAFQNAYM 

       550        560        570        580        590        600 
ELGGLGERVL GFCQLNLPSG KFPRGFKFDT DELNFPTEKL CFVGLMSMID PPRAAVPDAV 

       610        620        630        640        650        660 
GKCRSAGIKV IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPMS QVNPREAKAC 

       670        680        690        700        710        720 
VVHGSDLKDM TSEQLDEILK NHTEIVFART SPQQKLVIVE GCQRQGAIVA VTGDGVNDSP 

       730        740        750        760        770        780 
ALKKADIGIA MGISGSDVSK QAADMILLDD NFASIVTGVE EGRLVFDNLK KSIAYTLTSN 

       790        800        810        820        830        840 
IPEITPFLLF IIANIPLPLG TVTILCIDLG TDMVPAISLA YEAAESDIMK RQPRNSQTDK 

       850        860        870        880        890        900 
LVNERLISMA YGQIGMIQAL GGFFTYFVIL AENGFLPSRL LGIRLDWDDR TMNDLEDSYG 

       910        920        930        940        950        960 
QEWTYEQRKV VEFTCHTAFF ASIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLLEETA 

       970        980        990       1000       1010       1020 
LAAFLSYCPG MGVALRMYPL KVTWWFCAFP YSLLIFIYDE VRKLILRRYP GGWVEKETYY 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858333 mRNA. Translation: CAH90569.1.
RefSeqNP_001125304.1. NM_001131832.1.
UniGenePab.5099.

3D structure databases

ProteinModelPortalQ5RCD8.
SMRQ5RCD8. Positions 25-1020.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5RCD8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100172203.
KEGGpon:100172203.

Organism-specific databases

CTD477.

Phylogenomic databases

HOVERGENHBG004298.
InParanoidQ5RCD8.
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]
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. 2 hits.
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...

Entry information

Entry nameAT1A2_PONAB
AccessionPrimary (citable) accession number: Q5RCD8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 69 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