Sodium/potassium-transporting ATPase subunit alpha

Preferred order of sections

Names and origin

Protein names	Recommended 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
Organism	Hydra vulgaris (Hydra) (Hydra attenuata)
Taxonomic identifier	6087 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Cnidaria › Hydrozoa › Hydroida › Anthomedusae › Hydridae › Hydra

Protein attributes

Sequence length	1031 AA.
Sequence status	Complete.
Protein existence	Evidence 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).
Enzyme regulation	This alpha subunit is resistant to ouabain.
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]

Ontologies

Keywords
Biological process	Ion transport Potassium transport Sodium transport Sodium/potassium transport Transport
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Sodium
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological_process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
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 electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1031

1031

Sodium/potassium-transporting ATPase subunit alpha

PRO_0000046308

Regions

Transmembrane

102 – 123

22

Helical; By similarity

Transmembrane

136 – 155

20

Helical; By similarity

Transmembrane

297 – 319

23

Helical; By similarity

Transmembrane

326 – 354

29

Helical; By similarity

Transmembrane

795 – 818

24

Helical; By similarity

Transmembrane

857 – 882

26

Helical; By similarity

Transmembrane

924 – 944

21

Helical; By similarity

Transmembrane

961 – 986

26

Helical; By similarity

Sites

Active site

382

1

4-aspartylphosphate intermediate Probable

Metal binding

725

1

Magnesium By similarity

Metal binding

729

1

Magnesium By similarity

Binding site

512

1

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P35317 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: D2F4A07B811B356F
Show »

FASTA

1,031

114,161

        10         20         30         40         50         60 
MADPGDLESR GKADSYSVAE KKSAPKKISK KNANKAKLED LKKELEMTEH SMKLESLLSM 

        70         80         90        100        110        120 
YETSLEKGLS ENIVARNLER DGLNALTPPK QTPEWVKFCK QMFGGFSMLL WIGAILCFFA 

       130        140        150        160        170        180 
FGIRAVRDTN PNMDELYLGI VLSVVVIITG CFSYYQESKS SKIMESFKKM IPQEALVLRD 

       190        200        210        220        230        240 
GKKITINAEQ CVVGDVVFVK FGDRIPADIR IVECKGLKVD NSSLTGESEP QSRAVDFTHE 

       250        260        270        280        290        300 
NPIETKNLAF FSTNAVEGTA TGIVVRIGDN TVMGRIANLA SGLGSGKTPI ALEIEHFIHI 

       310        320        330        340        350        360 
VTGVAVFLGV SFLIISLAMG YHWLEAIIFL IGIIVANVPE GLLATVTVCL TLTAKKMAKK 

       370        380        390        400        410        420 
NCLVKHLEAV ETLGSTSVIC SDKTGTLTQN RMTVAHMWFD KMIVEADTTE DQSGIAHDKG 

       430        440        450        460        470        480 
SLTWKSLAKV AALCSRAEFK PNQNDVAVLR KECTGDASET AILKFVELSV GNVMDIRAKN 

       490        500        510        520        530        540 
KKVTEIPFNS TNKYQVSVHE QENSSGYLLV MKGAPEKVLE RCSTILINGE EQPLKDDVIE 

       550        560        570        580        590        600 
IYNKAYDELG GLGERVLGFC HYYLPVDQYP KGFLFKTEEE QNFPLEGLCF LGLLSMIDPP 

       610        620        630        640        650        660 
RAAVPDAVSK CRSAGIKVIM VTGDHPITAK AIAKGVGIIS EGNECEEDIA LRLNIPLEDL 

       670        680        690        700        710        720 
SEDQKKSAKA CVIHGAKLKD IKNEELDKIL CDHTEIVFAR TSPQQKLIIV EGCQRQGAIV 

       730        740        750        760        770        780 
AVTGDGVNDS PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL 

       790        800        810        820        830        840 
KKSIVYTLTS NIPEISPFLM FILFGIPLPL GTITILCIDL GTDMVPAISL AYEKAESDIM 

       850        860        870        880        890        900 
KRHPRNPIRD KLVNERLISL AYGQIGMMQA TAGFFTYFII LAENGFLPSY LFGLRSQWDD 

       910        920        930        940        950        960 
MSNNNLLDSF GSEWTYFQRK EIELTCQTAF FTTIVVVQWA DLIISKTRRL SLFQQGMTNW 

       970        980        990       1000       1010       1020 
FLNFGLFFET ALAAFLQYTP GVNTGLRLRP MNFTWWLPGL PFSLLIFVYD EIRRYLLRKN 

      1030 
PGGWVEKETY Y

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References

[1]	"Molecular cloning and characterization of Na,K-ATPase from Hydra vulgaris: implications for enzyme evolution and ouabain sensitivity." Canfield V.A., Xu K.Y., D'Aquila T., Shyjan A.W., Levenson R. New Biol. 4:339-348(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M75140 mRNA. Translation: AAA29207.1.
3D structure databases
ProteinModelPortal	P35317.
SMR	P35317. Positions 38-1031.
ModBase	Search...
Proteomic databases
PRIDE	P35317.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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...

Entry information

Entry name

AT1A_HYDVU

Accession

Primary (citable) accession number: P35317

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents