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Q9WV27 (AT1A4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-4

Short name=Na(+)/K(+) ATPase alpha-4 subunit
EC=3.6.3.9
Alternative name(s):
Sodium pump subunit alpha-4
Gene names
Name:Atp1a4
Synonyms:Atp1al2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1032 AA.
Sequence statusComplete.
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 ions, providing the energy for active transport of various nutrients. Plays a role in sperm motility By similarity.

Catalytic activity

ATP + H2O + Na+(In) + K+(Out) = ADP + phosphate + Na+(Out) + K+(In).

Enzyme regulation

Specifically inhibited by an endogenous cardiac glycoside, ouabain By similarity.

Subunit structure

Composed of three subunits: alpha (catalytic), beta and gamma.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Expressed at high levels in the testis and at low levels in the epididymis.

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 termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

fertilization

Inferred from mutant phenotype PubMed 21187400. Source: MGI

regulation of cellular pH

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of membrane potential

Inferred from mutant phenotype PubMed 21187400. Source: MGI

sodium ion transmembrane transport

Inferred from mutant phenotype PubMed 21187400. Source: GOC

sodium ion transport

Inferred from mutant phenotype PubMed 21187400. Source: MGI

sperm motility

Inferred from sequence or structural similarity. Source: UniProtKB

spermatogenesis

Inferred from mutant phenotype PubMed 21187400. Source: MGI

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 mutant phenotype PubMed 21187400. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10321032Sodium/potassium-transporting ATPase subunit alpha-4
PRO_0000046304

Regions

Topological domain1 – 9696Cytoplasmic Potential
Transmembrane97 – 11721Helical; Potential
Topological domain118 – 14124Extracellular Potential
Transmembrane142 – 16221Helical; Potential
Topological domain163 – 298136Cytoplasmic Potential
Transmembrane299 – 31820Helical; Potential
Topological domain319 – 33012Extracellular Potential
Transmembrane331 – 34818Helical; Potential
Topological domain349 – 781433Cytoplasmic Potential
Transmembrane782 – 80120Helical; Potential
Topological domain802 – 81110Extracellular Potential
Transmembrane812 – 83221Helical; Potential
Topological domain833 – 85220Cytoplasmic Potential
Transmembrane853 – 87523Helical; Potential
Topological domain876 – 92752Extracellular Potential
Transmembrane928 – 94720Helical; Potential
Topological domain948 – 96013Cytoplasmic Potential
Transmembrane961 – 97919Helical; Potential
Topological domain980 – 99415Extracellular Potential
Transmembrane995 – 101521Helical; Potential
Topological domain1016 – 103217Cytoplasmic Potential
Region91 – 933Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site38614-aspartylphosphate intermediate By similarity
Metal binding7261Magnesium By similarity
Metal binding7301Magnesium By similarity

Amino acid modifications

Modified residue9521Phosphoserine; by PKA By similarity

Experimental info

Sequence conflict741I → V in AAD43812. Ref.1
Sequence conflict4761N → S in AAD43813. Ref.1
Sequence conflict5461M → T in AAD43813. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9WV27 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 5B97565BA67AA08C

FASTA1,032114,887
        10         20         30         40         50         60 
MEPGKEKEVE APGELNQKPR PSTRSSTTNR QPKMKRRKKD LEELKKEVVM DDHKLTLDEL 

        70         80         90        100        110        120 
SAKYSVDLTK GLSILEAQDI LFQNGPNVLT PPPTTPEWVK FCRQLFGGFS LLLWTGACLC 

       130        140        150        160        170        180 
FLAYGIHVNY YKENANKDNL YLGIVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL 

       190        200        210        220        230        240 
VIRDGEKMQI NVRDVVLGDL VEVKGGDQIP ADIRVISAQG CKVDNSSLTG ESEPQSRCPD 

       250        260        270        280        290        300 
CTHENPLETR NIIFFSTNCV EGTARGIVIA TGDYTVMGRI ASLTSGLQMG KTPIATEIEH 

       310        320        330        340        350        360 
FIHLITAVAV FLGVSFFWLS IILGYTWLDA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR 

       370        380        390        400        410        420 
MARKNCLVKN LEAVETLGST STICSDKTGT LTQNRMTVAH LWFDKTVYEA DTSEEQTTGK 

       430        440        450        460        470        480 
TFPKSSDTWF YLARIAGLCN RADFKPHQES VPIAKRATTG DASESALLKF IEQSYNPVSE 

       490        500        510        520        530        540 
MRQKNPKVAE IPFNSTNKYQ MSIHLLEDNS EAHVLLMKGA PERIFDFCSS FLLNGQEYPM 

       550        560        570        580        590        600 
DEEMKMDFQN AYIELGGLGE RVLGFCFLNL PSNFSKGFQF NTDELNFPME NLCFAGLISM 

       610        620        630        640        650        660 
IDPPRTAVPD AVSKCRSAGI KVIMVTGDHP ITAKAIAKSV GIISEGNDTA EDIAARLNIP 

       670        680        690        700        710        720 
ISQVNNKSVK AIVVHGSELK DMESQQLDDI LKSYKEIVFA RTSPQQKLII VEGCQRLGAI 

       730        740        750        760        770        780 
VAVTGDGVND SPALKKADIG IAMGITGSDV SKQAADMILL DDNFASIVTG VEEGRLIFDN 

       790        800        810        820        830        840 
LKKSIAYTLT SNIPEITPFL LFIILSIPLP LGTITILCID LGTDMVPAIS LAYESPESDI 

       850        860        870        880        890        900 
MKRLPRNPKT DNLVNNRLIG MAYGQIGMIQ ALAGFFTYFV ILAENGFKPL DLLGIRLYWD 

       910        920        930        940        950        960 
DTQLNDLEDS YGQQWTYEQR KVVEFTCQTA FFISIVIVQW ADLIICKTRR NSLFKQGMKN 

       970        980        990       1000       1010       1020 
KILIFGLLEE TVLAAFLSYV PGMDVSLRMY PLKINWWFCA LPYSVLIFVY DEIRKLIIRR 

      1030 
RPGGWLEKET YY 

« Hide

References

« Hide 'large scale' references
[1]"The Na,K-ATPase alpha4 gene (Atp1a4) encodes a ouabain-resistant alpha subunit and is tightly linked to the alpha2 gene (Atp1a2) on mouse chromosome 1."
Underhill D.A., Canfield V.A., Dahl J.P., Gros P., Levenson R.
Biochemistry 38:14746-14751(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C57BL/6J and CD-1.
Tissue: Mammary gland and Testis.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 173-183; 370-387; 488-498; 606-634; 708-716 AND 736-783, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF164348 Genomic DNA. Translation: AAD43812.1.
AF164349 Genomic DNA. Translation: AAD43813.1.
AF164350 Genomic DNA. Translation: AAD43814.1.
AC074310 Genomic DNA. No translation available.
AC087061 Genomic DNA. No translation available.
RefSeqNP_038762.1. NM_013734.1.
UniGeneMm.482392.

3D structure databases

ProteinModelPortalQ9WV27.
SMRQ9WV27. Positions 39-1032.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9WV27. 4 interactions.
MINTMINT-4088554.

PTM databases

PhosphoSiteQ9WV27.

Proteomic databases

PaxDbQ9WV27.
PRIDEQ9WV27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000111243; ENSMUSP00000106874; ENSMUSG00000007107.
GeneID27222.
KEGGmmu:27222.
UCSCuc011wwk.1. mouse.

Organism-specific databases

CTD480.
MGIMGI:1351335. Atp1a4.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00560000076866.
HOGENOMHOG000265622.
HOVERGENHBG004298.
InParanoidQ9WV27.
KOK01539.
OMAKSSDTWF.
OrthoDBEOG7327N0.
TreeFamTF312838.

Gene expression databases

BgeeQ9WV27.
GenevestigatorQ9WV27.

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...

Other

NextBio305134.
PROQ9WV27.
SOURCESearch...

Entry information

Entry nameAT1A4_MOUSE
AccessionPrimary (citable) accession number: Q9WV27
Secondary accession number(s): E9QKL5, Q9R173, Q9WV28
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 120 of the entry and version 3 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

MGD cross-references

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