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UniProtKB - P06685 (AT1A1_RAT)

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Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

Atp1a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • ADP binding Source: RGD
  • ankyrin binding Source: BHF-UCL
  • ATP binding Source: BHF-UCL
  • chaperone binding Source: BHF-UCL
  • phosphatase activity Source: Ensembl
  • phosphatidylinositol 3-kinase binding Source: RGD
  • potassium ion binding Source: BHF-UCL
  • protein domain specific binding Source: RGD
  • protein kinase binding Source: UniProtKB
  • sodium:potassium-exchanging ATPase activity Source: UniProtKB
  • sodium ion binding Source: RGD
  • steroid hormone binding Source: Ensembl
Complete GO annotation...

GO - Biological processi

  • ATP hydrolysis coupled transmembrane transport Source: BHF-UCL
  • cardiac muscle contraction Source: BHF-UCL
  • cellular potassium ion homeostasis Source: Ensembl
  • cellular response to mechanical stimulus Source: RGD
  • cellular response to steroid hormone stimulus Source: Ensembl
  • cellular sodium ion homeostasis Source: Ensembl
  • energy coupled proton transmembrane transport, against electrochemical gradient Source: RGD
  • establishment or maintenance of transmembrane electrochemical gradient Source: BHF-UCL
  • membrane hyperpolarization Source: RGD
  • membrane repolarization Source: Ensembl
  • negative regulation of glucocorticoid biosynthetic process Source: Ensembl
  • negative regulation of heart contraction Source: Ensembl
  • positive regulation of heart contraction Source: Ensembl
  • positive regulation of striated muscle contraction Source: Ensembl
  • potassium ion import Source: RGD
  • potassium ion import across plasma membrane Source: BHF-UCL
  • potassium ion transport Source: RGD
  • regulation of blood pressure Source: Ensembl
  • regulation of cardiac muscle cell contraction Source: RGD
  • regulation of sodium ion transport Source: UniProtKB
  • regulation of the force of heart contraction Source: Ensembl
  • relaxation of cardiac muscle Source: BHF-UCL
  • response to drug Source: Ensembl
  • response to glycoside Source: Ensembl
  • sodium ion export from cell Source: BHF-UCL
  • sodium ion transport Source: RGD
Complete GO annotation...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2167. Atp1a1.

Subcellular locationi

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

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • basolateral plasma membrane Source: Ensembl
  • caveola Source: RGD
  • endoplasmic reticulum Source: BHF-UCL
  • endosome Source: RGD
  • extracellular exosome Source: Ensembl
  • Golgi apparatus Source: BHF-UCL
  • integral component of membrane Source: UniProtKB
  • intercalated disc Source: BHF-UCL
  • membrane Source: RGD
  • membrane raft Source: RGD
  • myelin sheath Source: Ensembl
  • plasma membrane Source: BHF-UCL
  • postsynaptic density Source: Ensembl
  • protein complex Source: Ensembl
  • sarcolemma Source: BHF-UCL
  • sodium:potassium-exchanging ATPase complex Source: RGD
  • T-tubule Source: BHF-UCL
Complete GO annotation...

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.
GenevisibleiP06685. RN.

Interactioni

Subunit structurei

Interacts with SLC35G1 and STIM1 (By similarity). Composed of three subunits: alpha (catalytic), beta and gamma. Interacts with SIK1.By similarity2 Publications

GO - Molecular functioni

  • ankyrin binding Source: BHF-UCL
  • chaperone binding Source: BHF-UCL
  • phosphatidylinositol 3-kinase binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein kinase binding Source: UniProtKB
Complete GO annotation...

Protein-protein interaction databases

BioGridi246399. 10 interactors.
IntActiP06685. 2 interactors.
MINTiMINT-3089277.
STRINGi10116.ENSRNOP00000045650.

Chemistry databases

BindingDBiP06685.

Structurei

Secondary structure

11023
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi394 – 396Combined sources3
Beta strandi403 – 405Combined sources3
Helixi416 – 427Combined sources12
Beta strandi431 – 435Combined sources5
Beta strandi438 – 440Combined sources3
Helixi442 – 444Combined sources3
Beta strandi447 – 449Combined sources3
Turni451 – 453Combined sources3
Helixi454 – 461Combined sources8
Turni462 – 464Combined sources3
Helixi467 – 473Combined sources7
Beta strandi478 – 480Combined sources3
Turni483 – 485Combined sources3
Beta strandi489 – 494Combined sources6
Beta strandi496 – 500Combined sources5
Beta strandi502 – 509Combined sources8
Helixi511 – 515Combined sources5
Beta strandi518 – 521Combined sources4
Beta strandi526 – 529Combined sources4
Helixi532 – 546Combined sources15
Beta strandi556 – 558Combined sources3
Turni562 – 564Combined sources3
Turni572 – 574Combined sources3

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...

Miscellaneous databases

EvolutionaryTraceiP06685.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification]Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0203. Eukaryota.
COG0474. LUCA.
GeneTreeiENSGT00880000137885.
HOVERGENiHBG004298.
InParanoidiP06685.
KOiK01539.
OMAiARIMPEQ.
OrthoDBiEOG091G01BB.
PhylomeDBiP06685.

Family and domain databases

Gene3Di3.40.1110.10. 1 hit.
InterProiView protein in InterPro
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

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: June 7, 2017
This is version 183 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