Sodium/potassium-transporting ATPase subunit alpha-3

Contribute

Send feedback

Read comments (?) or add your own

Q6PIC6 (AT1A3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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-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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1013 AA.
Sequence status	Complete.
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 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	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 adult locomotory behavior Inferred from mutant phenotype PubMed 17234593. Source: MGI ionotropic glutamate receptor signaling pathway Inferred from mutant phenotype PubMed 17234593. Source: MGI memory Inferred from mutant phenotype PubMed 17234593. Source: MGI response to drug Inferred from mutant phenotype PubMed 17234593. Source: MGI visual learning Inferred from mutant phenotype PubMed 17234593. Source: MGI
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay PubMed 10837135. Source: MGI plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB synapse Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP 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 sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1013

1013

Sodium/potassium-transporting ATPase subunit alpha-3

PRO_0000046299

Regions

Topological domain

1 – 77

Cytoplasmic Potential

Transmembrane

78 – 98

Helical; Potential

Topological domain

99 – 121

Extracellular Potential

Transmembrane

122 – 142

Helical; Potential

Topological domain

143 – 278

136

Cytoplasmic Potential

Transmembrane

279 – 298

Helical; Potential

Topological domain

299 – 310

Extracellular Potential

Transmembrane

311 – 328

Helical; Potential

Topological domain

329 – 762

434

Cytoplasmic Potential

Transmembrane

763 – 782

Helical; Potential

Topological domain

783 – 792

Extracellular Potential

Transmembrane

793 – 813

Helical; Potential

Topological domain

814 – 833

Cytoplasmic Potential

Transmembrane

834 – 856

Helical; Potential

Topological domain

857 – 908

Extracellular Potential

Transmembrane

909 – 928

Helical; Potential

Topological domain

929 – 941

Cytoplasmic Potential

Transmembrane

942 – 960

Helical; Potential

Topological domain

961 – 975

Extracellular Potential

Transmembrane

976 – 996

Helical; Potential

Topological domain

997 – 1013

Cytoplasmic Potential

Region

72 – 74

Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site

366

4-aspartylphosphate intermediate By similarity

Metal binding

707

Magnesium By similarity

Metal binding

711

Magnesium By similarity

Amino acid modifications

Modified residue

265

Phosphoserine Ref.3

Modified residue

368

Phosphothreonine Ref.5

Modified residue

493

Phosphotyrosine Ref.4

Modified residue

548

Phosphotyrosine Ref.4

Modified residue

549

Phosphotyrosine Ref.4

Modified residue

933

Phosphoserine; by PKA By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6PIC6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 72F051406284EA8A
Show »

FASTA

1,013

111,692

        10         20         30         40         50         60 
MGDKKDDKSS PKKSKAKERR DLDDLKKEVA MTEHKMSVEE VCRKYNTDCV QGLTHSKAQE 

        70         80         90        100        110        120 
ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SILLWIGAIL CFLAYGIQAG TEDDPSGDNL 

       130        140        150        160        170        180 
YLGIVLAAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIREGEKMQV NAEEVVVGDL 

       190        200        210        220        230        240 
VEIKGGDRVP ADLRIISAHG CKVDNSSLTG ESEPQTRSPD CTHDNPLETR NITFFSTNCV 

       250        260        270        280        290        300 
EGTARGVVVA TGDRTVMGRI ATLASGLEVG KTPIAIEIEH FIQLITGVAV FLGVSFFILS 

       310        320        330        340        350        360 
LILGYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN LEAVETLGST 

       370        380        390        400        410        420 
STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTEDQSGTS FDKSSHTWVA LSHIAGLCNR 

       430        440        450        460        470        480 
AVFKGGQDNI PVLKRDVAGD ASESALLKCI ELSSGSVKLM RERNKKVAEI PFNSTNKYQL 

       490        500        510        520        530        540 
SIHETEDPND NRYLLVMKGA PERILDRCAT ILLQGKEQPL DEEMKEAFQN AYLELGGLGE 

       550        560        570        580        590        600 
RVLGFCHYYL PEEQFPKGFA FDCDDVNFTT DNLCFVGLMS MIDPPRAAVP DAVGKCRSAG 

       610        620        630        640        650        660 
IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA KACVIHGTDL 

       670        680        690        700        710        720 
KDFTSEQIDE ILQNHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN DSPALKKADI 

       730        740        750        760        770        780 
GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF 

       790        800        810        820        830        840 
LLFIMANIPL PLGTITILCI DLGTDMVPAI SLAYEAAESD IMKRQPRNPR TDKLVNERLI 

       850        860        870        880        890        900 
SMAYGQIGMI QALGGFFSYF VILAENGFLP GNLVGIRLNW DDRTVNDLED SYGQQWTYEQ 

       910        920        930        940        950        960 
RKVVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE ETALAAFLSY 

       970        980        990       1000       1010 
CPGMDVALRM YPLKPSWWFC AFPYSFLIFV YDEIRKLILR RNPGGWVEKE TYY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: Eye.
[2]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 21-27; 36-81; 153-163; 168-184; 203-254; 260-271; 350-367; 404-420; 425-434; 436-458; 466-492; 517-557; 587-595; 603-615; 620-648; 652-682; 689-764; 878-901; 931-940; 943-969 AND 1001-1009. Strain: C57BL/6. Tissue: Brain.
[3]	"Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[4]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-493; TYR-548 AND TYR-549, MASS SPECTROMETRY. Tissue: Brain.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-368, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC034645 mRNA. Translation: AAH34645.1. BC037206 mRNA. Translation: AAH37206.1. BC042894 mRNA. Translation: AAH42894.1.
IPI	IPI00122048.
UniGene	Mm.44101.
3D structure databases
ProteinModelPortal	Q6PIC6.
SMR	Q6PIC6. Positions 16-1013.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6PIC6. 4 interactions.
PTM databases
PhosphoSite	Q6PIC6.
Proteomic databases
PaxDb	Q6PIC6.
PRIDE	Q6PIC6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000080882; ENSMUSP00000079691; ENSMUSG00000040907.
UCSC	uc009frf.1. mouse.
Organism-specific databases
MGI	MGI:88107. Atp1a3.
Phylogenomic databases
eggNOG	COG0474.
GeneTree	ENSGT00560000076866.
HOGENOM	HOG000265622.
HOVERGEN	HBG004298.
OrthoDB	EOG46MBHS.
Gene expression databases
ArrayExpress	Q6PIC6.
Bgee	Q6PIC6.
CleanEx	MM_ATP1A3.
Genevestigator	Q6PIC6.
GermOnline	ENSMUSG00000040907. Mus musculus.
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
ChiTaRS	ATP1A3. mouse.
SOURCE	Search...

Entry information

Entry name

AT1A3_MOUSE

Accession

Primary (citable) accession number: Q6PIC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 84 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents