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P05025 (AT1A_TORCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sodium/potassium-transporting ATPase subunit alpha
Short name=Na(+)/K(+) ATPase alpha subunit
EC=3.6.3.9
Alternative name(s):
Sodium pump subunit alpha
OrganismTorpedo californica (Pacific electric ray)
Taxonomic identifier7787 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Batoidea › Torpediniformes › Torpedinidae › Torpedo

Protein attributes

Sequence length1022 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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.

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

Propeptide1 – 55
PRO_0000002509
Chain6 – 10221017Sodium/potassium-transporting ATPase subunit alpha
PRO_0000002510

Regions

Topological domain6 – 8782Cytoplasmic Potential
Transmembrane88 – 10821Helical; Potential
Topological domain109 – 13123Lumenal Potential
Transmembrane132 – 15221Helical; Potential
Topological domain153 – 288136Cytoplasmic Potential
Transmembrane289 – 30820Helical; Potential
Topological domain309 – 32012Lumenal Potential
Transmembrane321 – 33818Helical; Potential
Topological domain339 – 771433Cytoplasmic Potential
Transmembrane772 – 79120Helical; Potential
Topological domain792 – 80110Lumenal Potential
Transmembrane802 – 82221Helical; Potential
Topological domain823 – 84220Cytoplasmic Potential
Transmembrane843 – 86523Helical; Potential
Topological domain866 – 91752Lumenal Potential
Transmembrane918 – 93720Helical; Potential
Topological domain938 – 95013Cytoplasmic Potential
Transmembrane951 – 96919Helical; Potential
Topological domain970 – 98415Lumenal Potential
Transmembrane985 – 100521Helical; Potential
Topological domain1006 – 102217Cytoplasmic Potential
Region82 – 843Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site37614-aspartylphosphate intermediate By similarity
Metal binding7161Magnesium By similarity
Metal binding7201Magnesium By similarity

Amino acid modifications

Modified residue161Phosphoserine; by PKC By similarity
Modified residue9421Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
P05025 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: D92FE737847D73C2

FASTA1,022112,430
        10         20         30         40         50         60 
MGKGAASEKY QPAATSENAK NSKKSKSKTT DLDELKKEVS LDDHKLNLDE LHQKYGTDLT 

        70         80         90        100        110        120 
QGLTPARAKE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF SILLWTGAIL CFLAYGIQVA 

       130        140        150        160        170        180 
TVDNPANDNL YLGVVLSTVV IITGCFSYYQ EAKSSKIMDS FKNMVPQQAL VIRDGEKSSI 

       190        200        210        220        230        240 
NAEQVVVGDL VEVKGGDRIP ADLRIISACS CKVDNSSLTG ESEPQSRSPE YSSENPLETK 

       250        260        270        280        290        300 
NIAFFSTNCV EGTARGIVIN IGDHTVMGRI ATLASGLEVG QTPIAAEIEH FIHIITGVAV 

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

       370        380        390        400        410        420 
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGIS FDKTSLSWNA 

       430        440        450        460        470        480 
LSRIAALCNR AVFQAGQDSV PILKRSVAGD ASESALLKCI ELCCGSVSQM RDRNPKIVEI 

       490        500        510        520        530        540 
PFNSTNKYQL SIHENDKADS RYLLVMKGAP ERILDRCSTI LLNGEDKPLN EEMKEAFQNA 

       550        560        570        580        590        600 
YLELGGLGER VLGFCHLKLS TSKFPEGYPF DVEEPNFPIT DLCFVGLMSM IDPPRAAVPD 

       610        620        630        640        650        660 
AVGKCRSAGI KVIMVTGDHP ITAKAIAKGV GIISEGNETV EDIAARLNIP VNQVNPRDAK 

       670        680        690        700        710        720 
ACVVHGTDLK DLSHENLDDI LHYHTEIVFA RTSPQQKLII VEGCQRQGAI VAVTGDGVND 

       730        740        750        760        770        780 
SPALKKADIG VAMGIAGSDV SKQAADMILL DDNFASIVTG VEEGRLIFDN LKKSIAYTLT 

       790        800        810        820        830        840 
SNIPEITPFL VFIIANVPLP LGTVTILCID LGTDMVPAIS LAYERAESDI MKRQPRNPKT 

       850        860        870        880        890        900 
DKLVNERLIS MAYGQIGMIQ ALGGFFSYFV ILAENGFLPI DLIGIREKWD ELWTQDLEDS 

       910        920        930        940        950        960 
YGQQWTYEQR KIVEYTCHTS FFVSIVIVQW ADLIICKTRR NSIFQQGMKN KILIFGLFEE 

       970        980        990       1000       1010       1020 
TALAAFLSYT PGTDIALRMY PLKPSWWFCA FPYSLIIFLY DEARRFILRR NPGGWVEQET 


YY

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References

[1]"Primary structure of the alpha-subunit of Torpedo californica (Na+ + K+)ATPase deduced from cDNA sequence."
Kawakami K., Noguchi S., Noda M., Takahashi H., Ohta T., Kawamura M., Nojima H., Nagano K., Hirose T., Inayama S., Hayashida H., Miyata T., Numa S.
Nature 316:733-736(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"The active site structure of Na+/K+-transporting ATPase: location of the 5'-(p-fluorosulfonyl)benzoyladenosine binding site and soluble peptides released by trypsin."
Ohta T., Nagano K., Yoshida M.
Proc. Natl. Acad. Sci. U.S.A. 83:2071-2075(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 386-402; 502-512; 671-689 AND 887-906.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X02810 mRNA. Translation: CAA26578.1.
PIRS00503.

3D structure databases

ProteinModelPortalP05025.
SMRP05025. Positions 28-1022.
ModBaseSearch...

Proteomic databases

PRIDEP05025.

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]
PANTHERPTHR24093. PTHR24093. 1 hit.
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]
SUPFAMSSF81660. ATPase_cation_domN. 1 hit.
SSF56784. HAD-like_dom. 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 nameAT1A_TORCA
AccessionPrimary (citable) accession number: P05025
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 1, 2013
This is version 104 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

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