Sodium/potassium-transporting ATPase subunit alpha-2 precursor

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P06686 (AT1A2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 134. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sodium/potassium-transporting ATPase subunit alpha-2
Short name=Na(+)/K(+) ATPase alpha-2 subunit
EC=3.6.3.9

Alternative name(s):
Na(+)/K(+) ATPase alpha(+) subunit
Sodium pump subunit alpha-2

Gene names

Name:

Atp1a2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1020 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 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]

Ontologies

Keywords
Biological process	Ion transport Potassium transport Sodium transport Sodium/potassium transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Sodium
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro ATP hydrolysis coupled proton transport Inferred from mutant phenotype PubMed 12529322. Source: RGD adult locomotory behavior Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from direct assay PubMed 17458903. Source: RGD 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 cardiac muscle cell contraction Inferred from mutant phenotype PubMed 17442282. Source: RGD 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 response to nicotine Inferred from direct assay PubMed 22442718. Source: RGD visual learning Inferred from electronic annotation. Source: Compara
Cellular_component	T-tubule Inferred from direct assay PubMed 17442282. Source: RGD caveola Inferred from direct assay PubMed 16624992. Source: RGD dendritic spine Inferred from direct assay PubMed 11950769. Source: RGD endosome Inferred from direct assay PubMed 16893515. Source: RGD sodium:potassium-exchanging ATPase complex Inferred from direct assay PubMed 12093728 PubMed 16624992. Source: RGD synapse Inferred from direct assay PubMed 11950769. Source: RGD
Molecular_function	ATP binding Inferred from mutant phenotype PubMed 12529322. Source: RGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sodium:potassium-exchanging ATPase activity Inferred from direct assay PubMed 16624992. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 5

PRO_0000002507

Chain

6 – 1020

1015

Sodium/potassium-transporting ATPase subunit alpha-2

PRO_0000002508

Regions

Topological domain

6 – 85

Cytoplasmic Potential

Transmembrane

86 – 106

Helical; Potential

Topological domain

107 – 129

Extracellular Potential

Transmembrane

130 – 150

Helical; Potential

Topological domain

151 – 286

136

Cytoplasmic Potential

Transmembrane

287 – 306

Helical; Potential

Topological domain

307 – 318

Extracellular Potential

Transmembrane

319 – 336

Helical; Potential

Topological domain

337 – 769

433

Cytoplasmic Potential

Transmembrane

770 – 789

Helical; Potential

Topological domain

790 – 799

Extracellular Potential

Transmembrane

800 – 820

Helical; Potential

Topological domain

821 – 840

Cytoplasmic Potential

Transmembrane

841 – 863

Helical; Potential

Topological domain

864 – 915

Extracellular Potential

Transmembrane

916 – 935

Helical; Potential

Topological domain

936 – 948

Cytoplasmic Potential

Transmembrane

949 – 967

Helical; Potential

Topological domain

968 – 982

Extracellular Potential

Transmembrane

983 – 1003

Helical; Potential

Topological domain

1004 – 1020

Cytoplasmic Potential

Region

80 – 82

Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site

374

4-aspartylphosphate intermediate By similarity

Metal binding

714

Magnesium By similarity

Metal binding

718

Magnesium By similarity

Amino acid modifications

Modified residue

570

Phosphothreonine By similarity

Modified residue

587

Phosphoserine By similarity

Modified residue

650

Phosphoserine By similarity

Modified residue

940

Phosphoserine; by PKA By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P06686 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 5436E795BD5B4CFA
Show »

FASTA

1,020

112,217

        10         20         30         40         50         60 
MGRGAGREYS PAATTAENGG GKKKQKEKEL DELKKEVAMD DHKLSLDELG RKYQVDLSKG 

        70         80         90        100        110        120 
LTNQRAQDIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSI LLWIGALLCF LAYGILAAME 

       130        140        150        160        170        180 
DEPSNDNLYL GIVLAAVVIV 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 LASGLEVGQT 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 HEREDSPQSH VLVMKGAPER ILDRCSTILV QGKEIPLDKE MQDAFQNAYM 

       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 TSEQLDEILR DHTEIVFART SPQQKLIIVE GCQRQGAIVA VTGDGVNDSP 

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

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

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

       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' referencesShow 'large scale' references »
[1]	"Molecular cloning of three distinct forms of the Na+,K+-ATPase alpha-subunit from rat brain." Shull G.E., Greeb J., Lingrel J.B. Biochemistry 25:8125-8132(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
[3]	"Regulation of Na+,K(+)-ATPases. I. Cloning and analysis of the 5'-flanking region of the rat NKAA2 gene encoding the alpha 2 subunit." Kawakami K., Yagawa Y., Nagano K. Gene 91:267-270(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
[4]	Lubec G., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 594-602; 645-655; 659-668 AND 741-770, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M14512 mRNA. Translation: AAA40776.1. BC085764 mRNA. Translation: AAH85764.1. D90049 Genomic DNA. Translation: BAA14102.1.
IPI	IPI00205693.
PIR	B24639. I54059.
RefSeq	NP_036637.1. NM_012505.2.
UniGene	Rn.1042. Rn.214222.
3D structure databases
ProteinModelPortal	P06686.
SMR	P06686. Positions 25-1020.
ModBase	Search...
Protein-protein interaction databases
IntAct	P06686. 1 interaction.
STRING	10116.ENSRNOP00000054947.
PTM databases
PhosphoSite	P06686.
Proteomic databases
PaxDb	P06686.
PRIDE	P06686.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000058143; ENSRNOP00000054947; ENSRNOG00000007290.
GeneID	24212.
KEGG	rno:24212.
UCSC	RGD:2168. rat.
Organism-specific databases
CTD	477.
RGD	2168. Atp1a2.
Phylogenomic databases
eggNOG	COG0474.
GeneTree	ENSGT00560000076866.
HOGENOM	HOG000265622.
HOVERGEN	HBG004298.
KO	K01539.
OrthoDB	EOG46MBHS.
Enzyme and pathway databases
SABIO-RK	P06686.
Gene expression databases
ArrayExpress	P06686.
Genevestigator	P06686.
GermOnline	ENSRNOG00000007290. Rattus norvegicus.
Family and domain databases
Gene3D	1.20.1110.10. 2 hits. 2.70.150.10. 2 hits. 3.40.1110.10. 1 hit.
InterPro	IPR006068. 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]
PANTHER	PTHR24093. PTHR24093. 1 hit.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01106. ATPase-IIC_X-K. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL2491.
NextBio	602621.

Entry information

Entry name

AT1A2_RAT

Accession

Primary (citable) accession number: P06686

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents