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Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

Atp1a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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)DescriptionActionsGraphical viewLength
Active sitei3764-aspartylphosphate intermediateBy similarity1
Binding sitei487ATP1 Publication1
Metal bindingi717MagnesiumBy similarity1
Metal bindingi721MagnesiumBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processIon transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Sodium

Enzyme and pathway databases

ReactomeiR-RNO-5578775 Ion homeostasis
R-RNO-936837 Ion transport by P-type ATPases
SABIO-RKiP06685

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2167 Atp1a1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini6 – 87CytoplasmicSequence analysisAdd BLAST82
Transmembranei88 – 108HelicalSequence analysisAdd BLAST21
Topological domaini109 – 131ExtracellularSequence analysisAdd BLAST23
Transmembranei132 – 152HelicalSequence analysisAdd BLAST21
Topological domaini153 – 288CytoplasmicSequence analysisAdd BLAST136
Transmembranei289 – 308HelicalSequence analysisAdd BLAST20
Topological domaini309 – 320ExtracellularSequence analysisAdd BLAST12
Transmembranei321 – 338HelicalSequence analysisAdd BLAST18
Topological domaini339 – 772CytoplasmicSequence analysisAdd BLAST434
Transmembranei773 – 792HelicalSequence analysisAdd BLAST20
Topological domaini793 – 802ExtracellularSequence analysis10
Transmembranei803 – 823HelicalSequence analysisAdd BLAST21
Topological domaini824 – 843CytoplasmicSequence analysisAdd BLAST20
Transmembranei844 – 866HelicalSequence analysisAdd BLAST23
Topological domaini867 – 918ExtracellularSequence analysisAdd BLAST52
Transmembranei919 – 938HelicalSequence analysisAdd BLAST20
Topological domaini939 – 951CytoplasmicSequence analysisAdd BLAST13
Transmembranei952 – 970HelicalSequence analysisAdd BLAST19
Topological domaini971 – 985ExtracellularSequence analysisAdd BLAST15
Transmembranei986 – 1006HelicalSequence analysisAdd BLAST21
Topological domaini1007 – 1023CytoplasmicSequence analysisAdd BLAST17

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16S → A: Dopamine fails to increase phosphoinositide-3 kinase activity and to promote its interaction with Na(+)/K(+) ATPase. 1 Publication1
Mutagenesisi83P → R: Dopamine fails to increase phosphoinositide-3 kinase activity and to promote its interaction with Na(+)/K(+) ATPase. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3010

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000024891 – 51 Publication5
ChainiPRO_00000024906 – 1023Sodium/potassium-transporting ATPase subunit alpha-1Add BLAST1018

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9N6-acetyllysineBy similarity1
Modified residuei10Phosphotyrosine1 Publication1
Modified residuei16Phosphoserine; by PKC1 Publication1
Modified residuei21N6-acetyllysineBy similarity1
Modified residuei23Phosphoserine; by PKC2 Publications1
Modified residuei40PhosphoserineCombined sources1
Modified residuei47PhosphoserineCombined sources1
Modified residuei228PhosphoserineCombined sources1
Modified residuei260PhosphotyrosineBy similarity1
Modified residuei452PhosphoserineCombined sources1
Modified residuei484PhosphoserineCombined sources1
Modified residuei542PhosphotyrosineBy similarity1
Modified residuei661N6-succinyllysineBy similarity1
Modified residuei668PhosphoserineBy similarity1
Modified residuei675PhosphoserineBy similarity1
Modified residuei943Phosphoserine; by PKA1 Publication1

Post-translational modificationi

Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-943 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.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP06685
PRIDEiP06685

PTM databases

iPTMnetiP06685
PhosphoSitePlusiP06685

Expressioni

Gene expression databases

BgeeiENSRNOG00000030019 Expressed in 10 organ(s), highest expression level in adult mammalian kidney
GenevisibleiP06685 RN

Interactioni

Subunit structurei

The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1 (PubMed:17283221, PubMed:19339511, PubMed:23532852). Interacts with regulatory subunit FXYD3 (PubMed:15743908). Interacts with SLC35G1 and STIM1 (By similarity). Interacts with SIK1 (PubMed:17939993).By similarity5 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi246399, 10 interactors
ELMiP06685
IntActiP06685, 4 interactors
MINTiP06685
STRINGi10116.ENSRNOP00000045650

Chemistry databases

BindingDBiP06685

Structurei

Secondary structure

11023
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP06685
SMRiP06685
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06685

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni82 – 84Phosphoinositide-3 kinase binding3

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0203 Eukaryota
COG0474 LUCA
GeneTreeiENSGT00890000139334
HOVERGENiHBG004298
InParanoidiP06685
KOiK01539
OMAiARIMPEQ
OrthoDBiEOG091G01BB
PhylomeDBiP06685

Family and domain databases

CDDicd02608 P-type_ATPase_Na-K_like, 1 hit
Gene3Di3.40.1110.10, 1 hit
3.40.50.1000, 2 hits
InterProiView protein in InterPro
IPR006068 ATPase_P-typ_cation-transptr_C
IPR004014 ATPase_P-typ_cation-transptr_N
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR005775 P-type_ATPase_IIC
IPR001757 P_typ_ATPase
PfamiView protein in Pfam
PF00689 Cation_ATPase_C, 1 hit
PF00690 Cation_ATPase_N, 1 hit
SMARTiView protein in SMART
SM00831 Cation_ATPase_N, 1 hit
SUPFAMiSSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81660 SSF81660, 1 hit
SSF81665 SSF81665, 3 hits
TIGRFAMsiTIGR01106 ATPase-IIC_X-K, 1 hit
TIGR01494 ATPase_P-type, 2 hits
PROSITEiView protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P06685-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGKGVGRDKY EPAAVSEHGD KKSKKAKKER DMDELKKEVS MDDHKLSLDE
60 70 80 90 100
LHRKYGTDLS RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF
110 120 130 140 150
SMLLWIGAIL CFLAYGIRSA TEEEPPNDDL YLGVVLSAVV IITGCFSYYQ
160 170 180 190 200
EAKSSKIMES FKNMVPQQAL VIRNGEKMSI NAEDVVVGDL VEVKGGDRIP
210 220 230 240 250
ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR NIAFFSTNCV
260 270 280 290 300
EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV
310 320 330 340 350
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR
360 370 380 390 400
MARKNCLVKN LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA
410 420 430 440 450
DTTENQSGVS FDKTSATWFA LSRIAGLCNR AVFQANQENL PILKRAVAGD
460 470 480 490 500
ASESALLKCI EVCCGSVMEM REKYTKIVEI PFNSTNKYQL SIHKNPNASE
510 520 530 540 550
PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN AYLELGGLGE
560 570 580 590 600
RVLGFCHLLL PDEQFPEGFQ FDTDEVNFPV DNLCFVGLIS MIDPPRAAVP
610 620 630 640 650
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI
660 670 680 690 700
PVNQVNPRDA KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI
710 720 730 740 750
IVEGCQRQGA IVAVTGDGVN DSPALKKADI GVAMGIVGSD VSKQAADMIL
760 770 780 790 800
LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LIFIIANIPL
810 820 830 840 850
PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK TDKLVNERLI
860 870 880 890 900
SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRETW DDRWINDVED
910 920 930 940 950
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK
960 970 980 990 1000
NKILIFGLFE ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV
1010 1020
YDEVRKLIIR RRPGGWVEKE TYY
Length:1,023
Mass (Da):113,054
Last modified:January 1, 1988 - v1
Checksum:i85E98233EE6C18E9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti68 – 69AA → PV in AAA41671 (PubMed:2822726).Curated2
Sequence conflicti175G → E in AAA41671 (PubMed:2822726).Curated1
Sequence conflicti188G → V in AAA41671 (PubMed:2822726).Curated1
Sequence conflicti335G → V in AAA41671 (PubMed:2822726).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14511 mRNA Translation: AAA40775.1
X05882 mRNA Translation: CAA29306.1
M28647 mRNA Translation: AAA41671.1
BC061968 mRNA Translation: AAH61968.1
M11733 mRNA Translation: AAA40783.1
X53233 Genomic DNA Translation: CAA37325.1
X53234 Genomic DNA Translation: CAA37326.1
PIRiA24639
RefSeqiNP_036636.1, NM_012504.1
UniGeneiRn.217534
Rn.2992

Genome annotation databases

EnsembliENSRNOT00000040430; ENSRNOP00000045650; ENSRNOG00000030019
GeneIDi24211
KEGGirno:24211
UCSCiRGD:2167 rat

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14511 mRNA Translation: AAA40775.1
X05882 mRNA Translation: CAA29306.1
M28647 mRNA Translation: AAA41671.1
BC061968 mRNA Translation: AAH61968.1
M11733 mRNA Translation: AAA40783.1
X53233 Genomic DNA Translation: CAA37325.1
X53234 Genomic DNA Translation: CAA37326.1
PIRiA24639
RefSeqiNP_036636.1, NM_012504.1
UniGeneiRn.217534
Rn.2992

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MO7NMR-A386-595[»]
1MO8NMR-A386-595[»]
ProteinModelPortaliP06685
SMRiP06685
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246399, 10 interactors
ELMiP06685
IntActiP06685, 4 interactors
MINTiP06685
STRINGi10116.ENSRNOP00000045650

Chemistry databases

BindingDBiP06685
ChEMBLiCHEMBL3010

PTM databases

iPTMnetiP06685
PhosphoSitePlusiP06685

Proteomic databases

PaxDbiP06685
PRIDEiP06685

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000040430; ENSRNOP00000045650; ENSRNOG00000030019
GeneIDi24211
KEGGirno:24211
UCSCiRGD:2167 rat

Organism-specific databases

CTDi476
RGDi2167 Atp1a1

Phylogenomic databases

eggNOGiKOG0203 Eukaryota
COG0474 LUCA
GeneTreeiENSGT00890000139334
HOVERGENiHBG004298
InParanoidiP06685
KOiK01539
OMAiARIMPEQ
OrthoDBiEOG091G01BB
PhylomeDBiP06685

Enzyme and pathway databases

ReactomeiR-RNO-5578775 Ion homeostasis
R-RNO-936837 Ion transport by P-type ATPases
SABIO-RKiP06685

Miscellaneous databases

EvolutionaryTraceiP06685
PROiPR:P06685

Gene expression databases

BgeeiENSRNOG00000030019 Expressed in 10 organ(s), highest expression level in adult mammalian kidney
GenevisibleiP06685 RN

Family and domain databases

CDDicd02608 P-type_ATPase_Na-K_like, 1 hit
Gene3Di3.40.1110.10, 1 hit
3.40.50.1000, 2 hits
InterProiView protein in InterPro
IPR006068 ATPase_P-typ_cation-transptr_C
IPR004014 ATPase_P-typ_cation-transptr_N
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR005775 P-type_ATPase_IIC
IPR001757 P_typ_ATPase
PfamiView protein in Pfam
PF00689 Cation_ATPase_C, 1 hit
PF00690 Cation_ATPase_N, 1 hit
SMARTiView protein in SMART
SM00831 Cation_ATPase_N, 1 hit
SUPFAMiSSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81660 SSF81660, 1 hit
SSF81665 SSF81665, 3 hits
TIGRFAMsiTIGR01106 ATPase-IIC_X-K, 1 hit
TIGR01494 ATPase_P-type, 2 hits
PROSITEiView protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiAT1A1_RAT
AccessioniPrimary (citable) accession number: P06685
Secondary accession number(s): Q64609
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: September 12, 2018
This is version 193 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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