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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 intermediateBy similarity
Binding sitei485 – 4851ATPBy similarity
Metal bindingi715 – 7151MagnesiumBy similarity
Metal bindingi719 – 7191MagnesiumBy 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

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

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 55By similarityPRO_0000002479
Chaini6 – 10211016Sodium/potassium-transporting ATPase subunit alpha-1PRO_0000002480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysineBy similarity
Modified residuei10 – 101PhosphotyrosineBy similarity
Modified residuei16 – 161Phosphoserine; by PKCBy similarity
Modified residuei21 – 211N6-acetyllysineBy similarity
Modified residuei258 – 2581PhosphotyrosineBy similarity
Modified residuei540 – 5401PhosphotyrosineBy similarity
Modified residuei659 – 6591N6-succinyllysineBy similarity
Modified residuei941 – 9411Phosphoserine; by PKABy 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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP50997.
PRIDEiP50997.

Interactioni

Subunit structurei

Interacts with SIK1 (By similarity). Interacts with SLC35G1 and STIM1 (By similarity). Composed of three subunits: alpha (catalytic), beta and gamma.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000014393.

Structurei

3D structure databases

ProteinModelPortaliP50997.
SMRiP50997. Positions 24-1021.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini4 – 8582CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini107 – 12923ExtracellularSequence AnalysisAdd
BLAST
Topological domaini151 – 286136CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini307 – 31812ExtracellularSequence AnalysisAdd
BLAST
Topological domaini337 – 770434CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini791 – 80010ExtracellularSequence Analysis
Topological domaini822 – 84120CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini865 – 91652ExtracellularSequence AnalysisAdd
BLAST
Topological domaini937 – 94913CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini969 – 98315ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1005 – 102117CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei86 – 10621HelicalSequence AnalysisAdd
BLAST
Transmembranei130 – 15021HelicalSequence AnalysisAdd
BLAST
Transmembranei287 – 30620HelicalSequence AnalysisAdd
BLAST
Transmembranei319 – 33618HelicalSequence AnalysisAdd
BLAST
Transmembranei771 – 79020HelicalSequence AnalysisAdd
BLAST
Transmembranei801 – 82121HelicalSequence AnalysisAdd
BLAST
Transmembranei842 – 86423HelicalSequence AnalysisAdd
BLAST
Transmembranei917 – 93620HelicalSequence AnalysisAdd
BLAST
Transmembranei950 – 96819HelicalSequence AnalysisAdd
BLAST
Transmembranei984 – 100421HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 823Phosphoinositide-3 kinase bindingBy 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

« Hide

        10         20         30         40         50
MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH
60 70 80 90 100
RKYGTDLSRG LTTARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM
110 120 130 140 150
LLWIGAILCF LAYGIQAATE EEPQNDNLYL GVVLSAVVII TGCFSYYQEA
160 170 180 190 200
KSSKIMESFK NMVPQQALVI RNGEKMSINA EEVVIGDLVE VKGGDRIPAD
210 220 230 240 250
LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI AFFSTNCVKG
260 270 280 290 300
TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL
310 320 330 340 350
GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA
360 370 380 390 400
RKNCLVKNLE AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT
410 420 430 440 450
TENQSGVSFD KSSATWLALS RIAGLCNRAV FQANQENLPI LKRAVAGDAS
460 470 480 490 500
ESALLKCIEL CCGSVKEMRD RYAKIVEIPF NSTNKYQLSI HKNPNTSEPR
510 520 530 540 550
HLLVMKGAPE RILDRCSSIL LHGKEQPLDE ELKDALQNAY LELGGLGERV
560 570 580 590 600
LGFRHLFLPD EQFPEGFQFD TDDVNFPVEN LCFVGFISMI GPPRAAVPDA
610 620 630 640 650
VGKCRGAGIK VIMVTGDHPI TAKAIAKGAG IISEGNETVE DIAARLNIPV
660 670 680 690 700
RQVNPRDAKA CVVHGSDLKD MTSEQLDGIL KYHTEIVFAR TSPQQKLIIV
710 720 730 740 750
EGCQRQGAIV AVTGDGVNDS PALKKADIGV AMGIVGSDAS KQAADMILLD
760 770 780 790 800
DNFASIVTGV EEGRLIFDNL KKSIAYTLTS NIPEITPFLI FIIANIPLPL
810 820 830 840 850
GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD KLVNERLISM
860 870 880 890 900
AYGQIGMIQA LGGFFTYFVI LAENGFLPTH LLGLRVDWDD RWINDVEDSY
910 920 930 940 950
GQQWTYEQRK IVEFTCHTAF FVSIVVVQWA DLVICKTRRN SVFQQGMKNK
960 970 980 990 1000
ILIFGLFEET ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD
1010 1020
EVRKLIIRRR PGGWVEKETY Y
Length:1,021
Mass (Da):112,667
Last modified:October 1, 1996 - v1
Checksum:i938A19AA487CBEAA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091C → Y in CAA46950. (PubMed:1316269)Curated
Sequence conflicti185 – 1851I → V in CAA46950. (PubMed:1316269)Curated
Sequence conflicti249 – 2491K → E in CAA46950. (PubMed:1316269)Curated
Sequence conflicti309 – 3091L → F in CAA46950. (PubMed:1316269)Curated

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...
MobiDBi 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: October 29, 2014
This is version 113 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