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P50997

- AT1A1_CANFA

UniProt

P50997 - AT1A1_CANFA

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Protein
Sodium/potassium-transporting ATPase subunit alpha-1
Gene
ATP1A1
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

ATP + H2O + Na+(In) + K+(Out) = ADP + phosphate + Na+(Out) + K+(In).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei374 – 37414-aspartylphosphate intermediate By similarity
Binding sitei485 – 4851ATP By similarity
Metal bindingi715 – 7151Magnesium By similarity
Metal bindingi719 – 7191Magnesium By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. sodium:potassium-exchanging ATPase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. ATP biosynthetic process Source: InterPro
  2. regulation of sodium ion transport Source: UniProtKB
  3. sodium ion transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Ion transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Sodium

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium/potassium-transporting ATPase subunit alpha-1 (EC:3.6.3.9)
Short name:
Na(+)/K(+) ATPase alpha-1 subunit
Alternative name(s):
Sodium pump subunit alpha-1
Gene namesi
Name:ATP1A1
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini4 – 8582Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei86 – 10621Helical; Reviewed prediction
Add
BLAST
Topological domaini107 – 12923Extracellular Reviewed prediction
Add
BLAST
Transmembranei130 – 15021Helical; Reviewed prediction
Add
BLAST
Topological domaini151 – 286136Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei287 – 30620Helical; Reviewed prediction
Add
BLAST
Topological domaini307 – 31812Extracellular Reviewed prediction
Add
BLAST
Transmembranei319 – 33618Helical; Reviewed prediction
Add
BLAST
Topological domaini337 – 770434Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei771 – 79020Helical; Reviewed prediction
Add
BLAST
Topological domaini791 – 80010Extracellular Reviewed prediction
Transmembranei801 – 82121Helical; Reviewed prediction
Add
BLAST
Topological domaini822 – 84120Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei842 – 86423Helical; Reviewed prediction
Add
BLAST
Topological domaini865 – 91652Extracellular Reviewed prediction
Add
BLAST
Transmembranei917 – 93620Helical; Reviewed prediction
Add
BLAST
Topological domaini937 – 94913Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei950 – 96819Helical; Reviewed prediction
Add
BLAST
Topological domaini969 – 98315Extracellular Reviewed prediction
Add
BLAST
Transmembranei984 – 100421Helical; Reviewed prediction
Add
BLAST
Topological domaini1005 – 102117Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. melanosome Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 55 By similarity
PRO_0000002479
Chaini6 – 10211016Sodium/potassium-transporting ATPase subunit alpha-1
PRO_0000002480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysine By similarity
Modified residuei10 – 101Phosphotyrosine By similarity
Modified residuei16 – 161Phosphoserine; by PKC By similarity
Modified residuei21 – 211N6-acetyllysine By similarity
Modified residuei258 – 2581Phosphotyrosine By similarity
Modified residuei540 – 5401Phosphotyrosine By similarity
Modified residuei659 – 6591N6-succinyllysine By similarity
Modified residuei941 – 9411Phosphoserine; by PKA By similarity

Post-translational modificationi

Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-941 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP50997.
PRIDEiP50997.

Interactioni

Subunit structurei

Interacts with SIK1 By similarity. Composed of three subunits: alpha (catalytic), beta and gamma.

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000014393.

Structurei

3D structure databases

ProteinModelPortaliP50997.
SMRiP50997. Positions 24-1021.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 823Phosphoinositide-3 kinase binding By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiP50997.
KOiK01539.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. 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]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P50997-1 [UniParc]FASTAAdd to Basket

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MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH     50
RKYGTDLSRG LTTARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM 100
LLWIGAILCF LAYGIQAATE EEPQNDNLYL GVVLSAVVII TGCFSYYQEA 150
KSSKIMESFK NMVPQQALVI RNGEKMSINA EEVVIGDLVE VKGGDRIPAD 200
LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI AFFSTNCVKG 250
TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL 300
GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA 350
RKNCLVKNLE AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT 400
TENQSGVSFD KSSATWLALS RIAGLCNRAV FQANQENLPI LKRAVAGDAS 450
ESALLKCIEL CCGSVKEMRD RYAKIVEIPF NSTNKYQLSI HKNPNTSEPR 500
HLLVMKGAPE RILDRCSSIL LHGKEQPLDE ELKDALQNAY LELGGLGERV 550
LGFRHLFLPD EQFPEGFQFD TDDVNFPVEN LCFVGFISMI GPPRAAVPDA 600
VGKCRGAGIK VIMVTGDHPI TAKAIAKGAG IISEGNETVE DIAARLNIPV 650
RQVNPRDAKA CVVHGSDLKD MTSEQLDGIL KYHTEIVFAR TSPQQKLIIV 700
EGCQRQGAIV AVTGDGVNDS PALKKADIGV AMGIVGSDAS KQAADMILLD 750
DNFASIVTGV EEGRLIFDNL KKSIAYTLTS NIPEITPFLI FIIANIPLPL 800
GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD KLVNERLISM 850
AYGQIGMIQA LGGFFTYFVI LAENGFLPTH LLGLRVDWDD RWINDVEDSY 900
GQQWTYEQRK IVEFTCHTAF FVSIVVVQWA DLVICKTRRN SVFQQGMKNK 950
ILIFGLFEET ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD 1000
EVRKLIIRRR PGGWVEKETY Y 1021
Length:1,021
Mass (Da):112,667
Last modified:October 1, 1996 - v1
Checksum:i938A19AA487CBEAA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091C → Y in CAA46950. 1 Publication
Sequence conflicti185 – 1851I → V in CAA46950. 1 Publication
Sequence conflicti249 – 2491K → E in CAA46950. 1 Publication
Sequence conflicti309 – 3091L → F in CAA46950. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42173 mRNA. Translation: AAA67372.1.
X66174 mRNA. Translation: CAA46950.1.
RefSeqiNP_001003306.1. NM_001003306.1.
UniGeneiCfa.3039.

Genome annotation databases

GeneIDi403992.
KEGGicfa:403992.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42173 mRNA. Translation: AAA67372.1 .
X66174 mRNA. Translation: CAA46950.1 .
RefSeqi NP_001003306.1. NM_001003306.1.
UniGenei Cfa.3039.

3D structure databases

ProteinModelPortali P50997.
SMRi P50997. Positions 24-1021.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9615.ENSCAFP00000014393.

Chemistry

BindingDBi P50997.
ChEMBLi CHEMBL4838.

Proteomic databases

PaxDbi P50997.
PRIDEi P50997.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 403992.
KEGGi cfa:403992.

Organism-specific databases

CTDi 476.

Phylogenomic databases

eggNOGi COG0474.
HOGENOMi HOG000265622.
HOVERGENi HBG004298.
InParanoidi P50997.
KOi K01539.

Miscellaneous databases

NextBioi 20817480.

Family and domain databases

Gene3Di 1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProi 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 ]
Pfami PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
SMARTi SM00831. Cation_ATPase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsi TIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiAT1A1_CANFA
AccessioniPrimary (citable) accession number: P50997
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi