Sodium/potassium-transporting ATPase subunit alpha-3

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Reviewed, UniProtKB/Swiss-Prot P13637 (AT1A3_HUMAN)

Last modified November 24, 2009. Version 115. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Sodium/potassium-transporting ATPase subunit alpha-3
      Short name=Sodium pump subunit alpha-3
    EC=3.6.3.9
Alternative name(s):
    Na(+)/K(+) ATPase alpha-3 subunit
    Na(+)/K(+) ATPase alpha(III) subunit

Gene names

Name:

ATP1A3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	1013 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.
Involvement in disease	Defects in ATP1A3 are the cause of dystonia type 12 (DYT12) [MIM:128235]; also known as rapid-onset dystonia parkinsonism (RDP). DYT12 is an autosomal dominant dystonia-parkinsonism disorder. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. DYT12 patients develop dystonia and parkinsonism between 15 and 45 years of age. The disease is characterized by an unusually rapid evolution of signs and symptoms. The sudden onset of symptoms over hours to a few weeks, often associated with physical or emotional stress, suggests a trigger initiating a nervous system insult resulting in permanent neurologic disability. Ref.8
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IIC subfamily.

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Ontologies

Keywords
Biological process	Ion transport Potassium transport Sodium transport Sodium/potassium transport Transport
Cellular component	Membrane
Disease	Disease mutation Dystonia Parkinsonism
Domain	Transmembrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Sodium
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro potassium ion transport Inferred from electronic annotation. Source: UniProtKB-KW sodium ion transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Ref.8 Inferred from direct assay. Source: UniProtKB endoplasmic reticulum Ref.8 Inferred from direct assay. Source: UniProtKB sodium:potassium-exchanging ATPase complex Ref.8 Inferred by curator. Source: UniProtKB
Molecular function	ATP binding Ref.8 Non-traceable author statement. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW monovalent inorganic cation transmembrane transporter activity Inferred from electronic annotation. Source: InterPro potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW sodium ion binding Inferred from electronic annotation. Source: UniProtKB-KW sodium:potassium-exchanging ATPase activity Ref.8 Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

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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_0000046298

Regions

Topological domain

1 – 77

Cytoplasmic Potential

Transmembrane

78 – 98

Potential

Topological domain

99 – 121

Lumenal Potential

Transmembrane

122 – 142

Potential

Topological domain

143 – 278

136

Cytoplasmic Potential

Transmembrane

279 – 298

Potential

Topological domain

299 – 310

Lumenal Potential

Transmembrane

311 – 328

Potential

Topological domain

329 – 762

434

Cytoplasmic Potential

Transmembrane

763 – 782

Potential

Topological domain

783 – 792

Lumenal Potential

Transmembrane

793 – 813

Potential

Topological domain

814 – 833

Cytoplasmic Potential

Transmembrane

834 – 856

Potential

Topological domain

857 – 908

Lumenal Potential

Transmembrane

909 – 928

Potential

Topological domain

929 – 941

Cytoplasmic Potential

Transmembrane

942 – 960

Potential

Topological domain

961 – 975

Lumenal Potential

Transmembrane

976 – 996

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 By similarity

Modified residue

368

Phosphothreonine By similarity

Modified residue

493

Phosphotyrosine By similarity

Modified residue

548

Phosphotyrosine By similarity

Modified residue

549

Phosphotyrosine By similarity

Modified residue

933

Phosphoserine; by PKA By similarity

Natural variations

Natural variant

274

I → T in DYT12. Ref.8

VAR_026735

Natural variant

277

E → K in DYT12. Ref.8

VAR_026736

Natural variant

613

T → M in DYT12. Ref.8

VAR_026737

Natural variant

758

I → S in DYT12. Ref.8

VAR_026738

Natural variant

780

F → L in DYT12. Ref.8

VAR_026739

Natural variant

801

D → Y in DYT12. Ref.8

VAR_026740

Experimental info

Sequence conflict

1 – 2

MG → MEIH Ref.2

Sequence conflict

336

L → V Ref.1

Sequence conflict

336

L → V Ref.2

Sequence conflict

336

L → V Ref.4

Sequence conflict

336

L → V Ref.6

Sequence conflict

380

H → T in AAA52285. Ref.4

Sequence conflict

421

A → P Ref.6

Sequence conflict

430

I → M in CAA31390. Ref.2

Sequence conflict

555 – 557

FPK → YPQ Ref.1

Sequence conflict

555 – 557

FPK → YPQ Ref.2

Sequence conflict

555 – 557

FPK → YPQ in AAA52286. Ref.4

Sequence conflict

577

G → P in AAA51798. Ref.1

Sequence conflict

583

D → G Ref.1

Sequence conflict

583

D → G Ref.2

Sequence conflict

583

D → G in AAA52286. Ref.4

Sequence conflict

919

V → A in AAA52286. Ref.4

Sequence conflict

944

L → M in AAA52286. Ref.4

Sequence conflict

982

F → S in CAA31390. Ref.2

Sequence conflict

1006

W → S in AAA51798. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P13637-1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: BF28CD9F1E11AF48
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FASTA

1,013

111,749

        10         20         30         40         50         60 
MGDKKDDKDS PKKNKGKERR 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 PERILDRCST 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

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References

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[1]	"Family of human Na+, K+-ATPase genes. Structure of the gene for the catalytic subunit (alpha III-form) and its relationship with structural features of the protein." Ovchinnikov Y.A., Monastyrskaya G.S., Broude N.E., Ushkaryov Y.A., Melkov A.M., Smirnov Y.V., Malyshev I.V., Allikmets R.L., Kostina M.B., Dulubova I.E., Kiyatkin N.I., Grishin A.V., Modyanov N.N., Sverdlov E.D. FEBS Lett. 233:87-94(1988) [PubMed: 2838329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Family of human Na(+),K(+)-ATPase genes. Structure of the gene of isoform alpha-III." Sverdlov E.D., Monastyrskaya G.S., Broude N.E., Ushkarev Y.A., Melkov A.M., Smirnov Y.V., Malyshev I.V., Allikmets R.L., Kostina M.B., Dulubova I.E., Kiyatkin N.I., Grishin A.V., Modyanov N.N., Ovchinnikov Y.A. Dokl. Akad. Nauk SSSR 297:1488-1494(1987) [PubMed: 2834163] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Brain.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"The family of human Na+,K+-ATPase genes. A partial nucleotide sequence related to the alpha-subunit." Ovchinnikov Y.A., Monastyrskaya G.S., Broude N.E., Allikmets R.L., Ushkaryov Y.A., Melkov A.M., Smirnov Y.V., Malyshev I.V., Dulubova I.E., Petrukhin K.E., Gryshin A.V., Sverdlov V.E., Kiyatkin N.I., Kostina M.B., Modyanov N.N., Sverdlov E.D. FEBS Lett. 213:73-80(1987) [PubMed: 3030810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-387; 494-538 AND 545-1013.
[5]	Erratum Ovchinnikov Y.A., Monastyrskaya G.S., Broude N.E., Allikmets R.L., Ushkaryov Y.A., Melkov A.M., Smirnov Y.V., Malyshev I.V., Dulubova I.E., Petrukhin K.E., Gryshin A.V., Sverdlov V.E., Kiyatkin N.I., Kostina M.B., Modyanov N.N., Sverdlov E.D. FEBS Lett. 214:375-375(1987)
[6]	"The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit." Sverdlov E.D., Monastyrskaya G.S., Broude N.E., Ushkaryov Y.A., Allikmets R.L., Melkov A.M., Smirnov Y.V., Malyshev I.V., Dulubova I.E., Petrukhin K.E., Gryshin A.V., Kiyatkin N.I., Kostina M.B., Sverdlov V.E., Modyanov N.N., Ovchinnikov Y.A. FEBS Lett. 217:275-278(1987) [PubMed: 3036582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 243-434.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Mutations in the Na(+)/K(+)-ATPase alpha-3 gene ATP1A3 are associated with rapid-onset dystonia parkinsonism." de Carvalho Aguiar P., Sweadner K.J., Penniston J.T., Zaremba J., Liu L., Caton M., Linazasoro G., Borg M., Tijssen M.A.J., Bressman S.B., Dobyns W.B., Brashear A., Ozelius L.J. Neuron 43:169-175(2004) [PubMed: 15260953] [Abstract] Cited for: VARIANTS DYT12 THR-274; LYS-277; MET-613; SER-758; LEU-780 AND TYR-801.
+	Additional computationally mapped references.

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Web resources

GeneReviews

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Cross-references

Sequence databases
	M37457 M37456 Genomic DNA. Translation: AAA51798.1. X12910 X12923 Genomic DNA. Translation: CAA31390.1. BC009282 mRNA. Translation: AAH09282.1. BC009394 mRNA. Translation: AAH09394.1. BC015566 mRNA. Translation: AAH15566.1. M28286, M28284, M28285 Genomic DNA. Translation: AAA52285.1. M28293 M28292 Genomic DNA. Translation: AAA52286.1. M27577, M27570, M27573 Genomic DNA. Translation: AAA58380.1.
IPI	IPI00302840.
PIR	S00801.
RefSeq	NP_689509.1.
UniGene	Hs.515427
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P13637. 1 interaction.
STRING	P13637.
PTM databases
PhosphoSite	P13637.
Proteomic databases
PRIDE	P13637.
Genome annotation databases
Ensembl	ENST00000302102; ENSP00000302397; ENSG00000105409; Homo sapiens. [Genome view]
GeneID	478.
KEGG	hsa:478.
UCSC	uc002osg.1. human.
Organism-specific databases
CTD	478.
GeneCards	GC19M047162.
HGNC	HGNC:801. ATP1A3.
MIM	128235. phenotype. 182350. gene.
Orphanet	71517. Rapid-onset dystonia-parkinsonism.
PharmGKB	PA64.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P13637.
HOVERGEN	P13637.
OrthoDB	EOG9THZCP
Enzyme and pathway databases
BRENDA	3.6.3.9. 247.
Gene expression databases
ArrayExpress	P13637.
Bgee	P13637.
CleanEx	HS_ATP1A3.
Genevestigator	P13637.
GermOnline	ENSG00000105409. Homo sapiens.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR005775. ATPase_P-typ_cation-ex_asu_euk. IPR006069. ATPase_P-typ_cation-exchng_asu. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 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. PR00121. NAKATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01106. ATPase-IIC_X-K. 1 hit. TIGR01494. ATPase_P-type. 4 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	1981.
SOURCE	Search...

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Entry information

Entry name

AT1A3_HUMAN

Accession

Primary (citable) accession number: P13637
Secondary accession number(s): Q16732, Q16735, Q969K5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	October 17, 2006
Last modified:	November 24, 2009
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents