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D2WKD8 (AT1A2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length1020 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 By similarity.

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]

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Sodium transport
Sodium/potassium transport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Potassium
Sodium
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

adult locomotory behavior

Inferred from electronic annotation. Source: Compara

locomotion

Inferred from electronic annotation. Source: Compara

negative regulation of heart contraction

Inferred from electronic annotation. Source: Compara

negative regulation of striated muscle contraction

Inferred from electronic annotation. Source: Compara

neurotransmitter uptake

Inferred from electronic annotation. Source: Compara

reduction of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Compara

regulation of blood pressure

Inferred from electronic annotation. Source: Compara

regulation of respiratory gaseous exchange by neurological system process

Inferred from electronic annotation. Source: Compara

regulation of smooth muscle contraction

Inferred from electronic annotation. Source: Compara

regulation of the force of heart contraction

Inferred from electronic annotation. Source: Compara

regulation of vasoconstriction

Inferred from electronic annotation. Source: Compara

visual learning

Inferred from electronic annotation. Source: Compara

   Cellular_componentT-tubule

Inferred from electronic annotation. Source: Compara

cytoplasm

Inferred from electronic annotation. Source: Compara

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sodium:potassium-exchanging ATPase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 55 By similarity
PRO_0000411080
Chain6 – 10201015Sodium/potassium-transporting ATPase subunit alpha-2
PRO_0000411081

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 residue6501Phosphoserine By similarity
Modified residue9401Phosphoserine; by PKA By similarity

Secondary structure

1 ................................. 1020
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
D2WKD8 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: 0DFB46632BBA2E2D

FASTA1,020112,208
        10         20         30         40         50         60 
MGRGAGREYS PAATTAENGG GKKKQKEKEL DELKKEVAMD DHKLSLDELG RKYQVDLSKG 

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

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

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

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

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

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

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

       490        500        510        520        530        540 
NSTNKYQLSI HEREDNPQSH VLVMKGAPER ILDRCSSILV QGKEIPLDKE MQDAFQNAYL 

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

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

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

       730        740        750        760        770        780 
ALKKADIGIA MGIAGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN 

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

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

       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

« Hide 'large scale' references
[1]"Cloning of Porcine ATP1A2 mRNA."
Henriksen C., Bendixen C., Andersen J.P., Vilsen B., Larsen K.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Porcine genome sequencing project
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The crystallographic structure of Na,K-ATPase N-domain at 2.6A resolution."
Hakansson K.O.
J. Mol. Biol. 332:1175-1182(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 384-590.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		GQ340776 mRNA. Translation: ADB19854.1.
CU138477 Genomic DNA. No translation available.
RefSeqNP_001165012.1. NM_001171541.1.
UniGeneSsc.14403.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q3IX-ray2.60A384-590[»]
ProteinModelPortalD2WKD8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000007004; ENSSSCP00000006814; ENSSSCG00000006391.
GeneID396828.
KEGGssc:396828.

Organism-specific databases

CTD477.

Phylogenomic databases

GeneTreeENSGT00560000076866.
KOK01539.
OMAIINIPLP.

Gene expression databases

ArrayExpressD2WKD8.

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

EvolutionaryTraceD2WKD8.

Entry information

Entry nameAT1A2_PIG
AccessionPrimary (citable) accession number: D2WKD8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: March 2, 2010
Last modified: May 1, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents