Sodium/potassium-transporting ATPase subunit alpha-1 precursor

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P50997 (AT1A1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sodium/potassium-transporting ATPase subunit alpha-1
Short name=Na(+)/K(+) ATPase alpha-1 subunit
EC=3.6.3.9

Alternative name(s):
Sodium pump subunit alpha-1

Gene names

Name:

ATP1A1

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length	1021 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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).
Subunit structure	Interacts with SIK1 By similarity. Composed of three subunits: alpha (catalytic), beta and gamma.
Subcellular location	Cell membrane; Multi-pass membrane protein. Melanosome By similarity.
Post-translational modification	Phosphorylation on Tyr-10 modulates pumping activity. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity By similarity.
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	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Sodium
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro regulation of sodium ion transport Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	integral to membrane Inferred from sequence or structural similarity. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
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 sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 5

By similarity

PRO_0000002479

Chain

6 – 1021

1016

Sodium/potassium-transporting ATPase subunit alpha-1

PRO_0000002480

Regions

Topological domain

4 – 85

Cytoplasmic Potential

Transmembrane

86 – 106

Helical; Potential

Topological domain

107 – 129

Extracellular Potential

Transmembrane

130 – 150

Helical; Potential

Topological domain

151 – 286

136

Cytoplasmic Potential

Transmembrane

287 – 306

Helical; Potential

Topological domain

307 – 318

Extracellular Potential

Transmembrane

319 – 336

Helical; Potential

Topological domain

337 – 770

434

Cytoplasmic Potential

Transmembrane

771 – 790

Helical; Potential

Topological domain

791 – 800

Extracellular Potential

Transmembrane

801 – 821

Helical; Potential

Topological domain

822 – 841

Cytoplasmic Potential

Transmembrane

842 – 864

Helical; Potential

Topological domain

865 – 916

Extracellular Potential

Transmembrane

917 – 936

Helical; Potential

Topological domain

937 – 949

Cytoplasmic Potential

Transmembrane

950 – 968

Helical; Potential

Topological domain

969 – 983

Extracellular Potential

Transmembrane

984 – 1004

Helical; Potential

Topological domain

1005 – 1021

Cytoplasmic Potential

Region

80 – 82

Phosphoinositide-3 kinase binding By similarity

Sites

Active site

374

4-aspartylphosphate intermediate By similarity

Metal binding

715

Magnesium By similarity

Metal binding

719

Magnesium By similarity

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphoserine; by PKC By similarity

Modified residue

Phosphoserine By similarity

Modified residue

215

Phosphoserine By similarity

Modified residue

217

Phosphothreonine By similarity

Modified residue

226

Phosphoserine By similarity

Modified residue

258

Phosphotyrosine By similarity

Modified residue

450

Phosphoserine By similarity

Modified residue

540

Phosphotyrosine By similarity

Modified residue

941

Phosphoserine; by PKA By similarity

Experimental info

Sequence conflict

109

C → Y in CAA46950. Ref.2

Sequence conflict

185

I → V in CAA46950. Ref.2

Sequence conflict

249

K → E in CAA46950. Ref.2

Sequence conflict

309

L → F in CAA46950. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P50997 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 938A19AA487CBEAA
Show »

FASTA

1,021

112,667

        10         20         30         40         50         60 
MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH RKYGTDLSRG 

        70         80         90        100        110        120 
LTTARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM LLWIGAILCF LAYGIQAATE 

       130        140        150        160        170        180 
EEPQNDNLYL GVVLSAVVII TGCFSYYQEA KSSKIMESFK NMVPQQALVI RNGEKMSINA 

       190        200        210        220        230        240 
EEVVIGDLVE VKGGDRIPAD LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI 

       250        260        270        280        290        300 
AFFSTNCVKG TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL 

       310        320        330        340        350        360 
GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE 

       370        380        390        400        410        420 
AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TENQSGVSFD KSSATWLALS 

       430        440        450        460        470        480 
RIAGLCNRAV FQANQENLPI LKRAVAGDAS ESALLKCIEL CCGSVKEMRD RYAKIVEIPF 

       490        500        510        520        530        540 
NSTNKYQLSI HKNPNTSEPR HLLVMKGAPE RILDRCSSIL LHGKEQPLDE ELKDALQNAY 

       550        560        570        580        590        600 
LELGGLGERV LGFRHLFLPD EQFPEGFQFD TDDVNFPVEN LCFVGFISMI GPPRAAVPDA 

       610        620        630        640        650        660 
VGKCRGAGIK VIMVTGDHPI TAKAIAKGAG IISEGNETVE DIAARLNIPV RQVNPRDAKA 

       670        680        690        700        710        720 
CVVHGSDLKD MTSEQLDGIL KYHTEIVFAR TSPQQKLIIV EGCQRQGAIV AVTGDGVNDS 

       730        740        750        760        770        780 
PALKKADIGV AMGIVGSDAS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS 

       790        800        810        820        830        840 
NIPEITPFLI FIIANIPLPL GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD 

       850        860        870        880        890        900 
KLVNERLISM AYGQIGMIQA LGGFFTYFVI LAENGFLPTH LLGLRVDWDD RWINDVEDSY 

       910        920        930        940        950        960 
GQQWTYEQRK IVEFTCHTAF FVSIVVVQWA DLVICKTRRN SVFQQGMKNK ILIFGLFEET 

       970        980        990       1000       1010       1020 
ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD EVRKLIIRRR PGGWVEKETY 


Y

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References

[1]	"Cloning of the dog Na/K-ATPase alpha 1 subunit." Xie Z., Li H., Liu G., Wang Y., Askari A., Mercer R.W. (In) Bamberg E., Schoner W. (eds.); The sodium pump, pp.49-52, Springer-Verlag, New York (1994) Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Mutation of a cysteine in the first transmembrane segment of Na,K-ATPase alpha subunit confers ouabain resistance." Canessa C.M., Horisberger J.-D., Louvard D., Rossier B.C. EMBO J. 11:1681-1687(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 92-311. Strain: Cocker spaniel. Tissue: Kidney.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42173 mRNA. Translation: AAA67372.1. X66174 mRNA. Translation: CAA46950.1.
RefSeq	NP_001003306.1. NM_001003306.1.
UniGene	Cfa.3039.
3D structure databases
ProteinModelPortal	P50997.
SMR	P50997. Positions 24-1021.
ModBase	Search...
Protein-protein interaction databases
STRING	9615.ENSCAFP00000014393.
Proteomic databases
PaxDb	P50997.
PRIDE	P50997.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	403992.
KEGG	cfa:403992.
Organism-specific databases
CTD	476.
Phylogenomic databases
eggNOG	COG0474.
HOGENOM	HOG000265622.
HOVERGEN	HBG004298.
InParanoid	P50997.
KO	K01539.
OrthoDB	EOG46MBHS.
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...
Other
BindingDB	P50997.
ChEMBL	CHEMBL4838.
NextBio	20817480.

Entry information

Entry name

AT1A1_CANFA

Accession

Primary (citable) accession number: P50997

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents