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P58312 (AT1A3_OREMO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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-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
OrganismOreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica)
Taxonomic identifier8127 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataOvalentariaCichlomorphaeCichliformesCichlidaeAfrican cichlidsPseudocrenilabrinaeOreochrominiOreochromis

Protein attributes

Sequence length1010 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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

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]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10101010Sodium/potassium-transporting ATPase subunit alpha-3
PRO_0000046302

Regions

Topological domain1 – 7474Cytoplasmic Potential
Transmembrane75 – 9521Helical; Potential
Topological domain96 – 11823Extracellular Potential
Transmembrane119 – 13921Helical; Potential
Topological domain140 – 275136Cytoplasmic Potential
Transmembrane276 – 29520Helical; Potential
Topological domain296 – 30712Extracellular Potential
Transmembrane308 – 32518Helical; Potential
Topological domain326 – 759434Cytoplasmic Potential
Transmembrane760 – 77920Helical; Potential
Topological domain780 – 78910Extracellular Potential
Transmembrane790 – 81021Helical; Potential
Topological domain811 – 83020Cytoplasmic Potential
Transmembrane831 – 85323Helical; Potential
Topological domain854 – 90552Extracellular Potential
Transmembrane906 – 92520Helical; Potential
Topological domain926 – 93813Cytoplasmic Potential
Transmembrane939 – 95719Helical; Potential
Topological domain958 – 97215Extracellular Potential
Transmembrane973 – 99321Helical; Potential
Topological domain994 – 101017Cytoplasmic Potential
Region69 – 713Interaction with phosphoinositide-3 kinase By similarity
Compositional bias10 – 134Poly-Lys

Sites

Active site36314-aspartylphosphate intermediate By similarity
Metal binding7041Magnesium By similarity
Metal binding7081Magnesium By similarity

Amino acid modifications

Modified residue9301Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
P58312 [UniParc].

Last modified October 18, 2001. Version 1.
Checksum: 9FEDB07C7547F0D1

FASTA1,010111,507
        10         20         30         40         50         60 
MGDKDDRFPK KKKGGTKDMD ALKKEVPITE HKMSVEEVCR KFQTDVVQGL TNAKAAEFLL 

        70         80         90        100        110        120 
RDGPNALTPP PTTPEWVKFC RQLFGGFSIL LWTGAILCFL AYAIQAATED EPAGDNLYLG 

       130        140        150        160        170        180 
IVLTAVVVIT GCFSYFQEAK SSKIMESFKN MVPQQALVIR EGEKVQVNAE EVMAGDLIEV 

       190        200        210        220        230        240 
KGGDRIPADI RVTSAHGCKV DNSSLTGESE PQSRSPDCTH DNPLETRNIA FFSTNCVEGT 

       250        260        270        280        290        300 
ARGIVICTGD RTVMGRIATL TSGLETGKTP IAVEIEHFIH IITGVAVFLG VTFFILAIIL 

       310        320        330        340        350        360 
GYTWLKAVIF LIGIIVANVP EGLLATVTVC LTLTAKRMAK KNCLVKNLEA VETLGSTSTI 

       370        380        390        400        410        420 
CSDKTGTLTQ NRMTVAHMWF DNQIHEADTT EDQSGAAFDK SSVTWLSLSR VAPLCNRAQF 

       430        440        450        460        470        480 
KPRQDSVSIL KRDVAGDASE SALLKCIELS CGSVRMMRDK NKKVAEIPFN PTNKYQLSIH 

       490        500        510        520        530        540 
ETEDPNDNRY LLVMKGALER ILDRCSTIML QGKEQPMDEE MKEAFQNAYM ELGGLGERVL 

       550        560        570        580        590        600 
GFRHLLLPED QYPKGFAFDT DDVNFQTDNL CFVGLMSMID PPRAAVPDAV GKCRSAGIKV 

       610        620        630        640        650        660 
IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPVS QVNPRDAKAC VIHGSDLKDL 

       670        680        690        700        710        720 
SQDQMDDILR NHTEIVFART SPQQKLIIVE GCQRLGAIVA VTGDGVNDSP ALKKADIGVA 

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

       790        800        810        820        830        840 
IIVNIPLALG TITILCIDLG TDMGSAISLA YETAESDIMK RQPRNPCRDK LVNERLISIA 

       850        860        870        880        890        900 
YGQIGMIQAL GGFFSYFVIL AENGFLPSQL VGIRLNWDDR SLNDLEDSYG QQWTYEQRKI 

       910        920        930        940        950        960 
VEFTCHTAFF VSIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLFEETA LAAFLSYCPG 

       970        980        990       1000       1010 
MDVALRMYPL KPTWWFWAFP YSFLIFVYDE ARKLILCRNP GGWVEKETYY 

« Hide

References

[1]Feng H.H., Leu J.H., Huang C.J., Hwang P.P.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF109409 mRNA. Translation: AAF75108.1.

3D structure databases

ProteinModelPortalP58312.
SMRP58312. Positions 17-1010.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP58312.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004298.

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. 3 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...

Entry information

Entry nameAT1A3_OREMO
AccessionPrimary (citable) accession number: P58312
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 18, 2001
Last modified: June 11, 2014
This is version 81 of the entry and version 1 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