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 TNaK1-alpha
Organism	Taenia solium (Pork tapeworm)
Taxonomic identifier	6204 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Platyhelminthes › Cestoda › Eucestoda › Cyclophyllidea › Taeniidae › Taenia

Protein attributes

Sequence length	1014 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 By similarity.
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 By similarity.
Subcellular location	Membrane; Multi-pass membrane protein Ref.1.
Tissue specificity	Preferentially localized in muscle cells and protonephridial ducts, and in small quantities in the tegument of cysticerci. Ref.1
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 – 1014

1014

Sodium/potassium-transporting ATPase subunit alpha

PRO_0000291569

Regions

Transmembrane

124 – 144

21

Helical; Potential

Transmembrane

281 – 300

20

Helical; Potential

Transmembrane

313 – 330

18

Helical; Potential

Transmembrane

764 – 783

20

Helical; Potential

Transmembrane

794 – 814

21

Helical; Potential

Transmembrane

834 – 856

23

Helical; Potential

Transmembrane

909 – 928

20

Helical; Potential

Transmembrane

942 – 960

19

Helical; Potential

Transmembrane

976 – 996

21

Helical; Potential

Sites

Active site

368

1

4-aspartylphosphate intermediate By similarity

Metal binding

708

1

Magnesium By similarity

Metal binding

712

1

Magnesium By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6RWA9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 595741648A93D5D1
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FASTA

1,014

111,990

        10         20         30         40         50         60 
MGKSRGDKYR DATDGKKDAK KDLNELKQEL AMDEHQISLD ELYARLGTNP DTGLTSEQAK 

        70         80         90        100        110        120 
TRLDRDGPNA LTPPKTTPEW VKFCKNMFGG FSLLLWIGAV LCFIAHGIPC WCAGEPYLYD 

       130        140        150        160        170        180 
NLYLGIVLAA VVVITGCFSY YQESKSSKIM ESFAKLVPQY AVVIRGGQRI DAPAEALVVG 

       190        200        210        220        230        240 
DIIDVKFGDR VPADIRVIKA SSFKVDNSAL TGESEPQTRT AEYTNENPLE TKNLAFFSTN 

       250        260        270        280        290        300 
AVEGTCRGVV VATGDRTVMG RIANLASGLE MGATPIAREI AHFIHIITGV AVFLGVTFFI 

       310        320        330        340        350        360 
IAFILGYYWL DAVIFLIGII VANVPEGLLA TVTVCLTLTA KRMASKNCLV KNLEAVETLG 

       370        380        390        400        410        420 
STSTICSDKT GTLTQNRMTV AHMWFDNKIF EADTSDDQST ANYSRASSTW MALSRIAMLC 

       430        440        450        460        470        480 
NRAEFKPGEE TNPVLKRECN GDASESALLK CVGLSIGGVT GYRTDKPKVA EIPFNSTNKY 

       490        500        510        520        530        540 
QVSVHQTDDG DERYLVVMKG APERILDRCS TVLMEGQELH MDDQWRESFN NAYLELGGIG 

       550        560        570        580        590        600 
ERVLGFCDLR LPADKFPRGF KFDIDEPNFP IEGMPFVGLM SMIDPPRAAV PDAVSKCRSA 

       610        620        630        640        650        660 
GIKVVMVTGD HPITAKAIAK GVGIISDGNK TVEDIAAERG VPVSQVNPRE ASACVVHGSD 

       670        680        690        700        710        720 
LRDMTPAQID EILENHSEIV FARTSPQQKL IIVEGIQRMG AIVAVTGDGV NDSPALKKAD 

       730        740        750        760        770        780 
IGVAMGITGS DVSKQAADMI LLDDNFASIV TGVEEGRIIF DNLKKSIAYT LTSNIPEITP 

       790        800        810        820        830        840 
FLIFILADVP LPLGTITILC IDLGTDMVPA ISLAYEEAED IMKRMPRDPF RDKLVNERLI 

       850        860        870        880        890        900 
SMAYGQIGMI QASGGFFVYF VIMAENGFWP SRLLGLRKQW DSPAINDVAD SYGQEWTYTQ 

       910        920        930        940        950        960 
RKRLEYTCHT AFFASIVIVQ WTDLLICKTR KNSIYQQGMW NHHLTFGLFF ETTLAIFLSY 

       970        980        990       1000       1010 
CPGLEHGLRM MPLRWTWWLP VLPFSVSIFI FDEVRKKFLR TLPPGNWVER ETNY

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References

[1]

"Cloning and expression of a Na(+), K(+)-ATPase alpha-subunit from Taenia solium (TNaK1alpha)."
Willms K., Shoemaker C.B., Skelly P.J., Landa A.
Mol. Biochem. Parasitol. 138:79-82(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY487828 mRNA. Translation: AAS59168.1.
3D structure databases
ProteinModelPortal	Q6RWA9.
SMR	Q6RWA9. Positions 20-1014.
ModBase	Search...
Proteomic databases
PRIDE	Q6RWA9.
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_TAESO

Accession

Primary (citable) accession number: Q6RWA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 52 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