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Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

ATP1A1

Organism
Oryctolagus cuniculus (Rabbit)
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 (By similarity). May contribute to blood-heart barrier properties of endocardial endothelium and may control cardiac performance via endothelial Na+/H+ exchange.By similarity1 Publication

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 sitei487ATPBy similarity1
Metal bindingi717MagnesiumBy similarity1
Metal bindingi721MagnesiumBy similarity1

GO - Molecular functioni

  • ATPase binding Source: BHF-UCL
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • nitric-oxide synthase binding Source: BHF-UCL
  • sodium:potassium-exchanging ATPase activity Source: UniProtKB-EC

GO - Biological processi

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00003059791 – 5By similarity5
ChainiPRO_00003059806 – 1023Sodium/potassium-transporting ATPase subunit alpha-1By similarityAdd BLAST1018

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9N6-acetyllysineBy similarity1
Modified residuei10PhosphotyrosineBy similarity1
Modified residuei16Phosphoserine; by PKCBy similarity1
Modified residuei21N6-acetyllysineBy similarity1
Modified residuei40PhosphoserineBy similarity1
Modified residuei47PhosphoserineBy similarity1
Modified residuei228PhosphoserineBy similarity1
Modified residuei260PhosphotyrosineBy similarity1
Modified residuei452PhosphoserineBy similarity1
Modified residuei484PhosphoserineBy similarity1
Modified residuei542PhosphotyrosineBy similarity1
Modified residuei661N6-succinyllysineBy similarity1
Modified residuei668PhosphoserineBy similarity1
Modified residuei675PhosphoserineBy similarity1
Modified residuei943Phosphoserine; by PKABy similarity1

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ9N0Z6.

Expressioni

Tissue specificityi

Expressed in endocardial endothelial cells.1 Publication

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ATP1B1Q9TT372EBI-9685690,EBI-9685670

GO - Molecular functioni

  • ATPase binding Source: BHF-UCL
  • nitric-oxide synthase binding Source: BHF-UCL

Protein-protein interaction databases

IntActiQ9N0Z6. 2 interactors.
STRINGi9986.ENSOCUP00000024821.

Structurei

3D structure databases

ProteinModelPortaliQ9N0Z6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni82 – 84Phosphoinositide-3 kinase bindingBy similarity3

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0203. Eukaryota.
COG0474. LUCA.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiQ9N0Z6.
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.
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.
[Graphical view]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
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.

Q9N0Z6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGVGRDKY EPAAVSEHGD KKGKKAKKER DMDELKKEVS MDDHKLSLDE
60 70 80 90 100
LHRKYGTDLS RGLTTARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF
110 120 130 140 150
SMLLWIGAIL CFLAYGILAA TEEDFDNDNL YLGVVLAAVV 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
EGTARGIVIY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV
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 FDKTSATWLA LSRIAGLCNR AVFQANQENL PILKRAVAGD
460 470 480 490 500
ASESALLKCI ELCCGSVKEM RERYTKIVEI PFNSTNKYQL SIHKNLNANE
510 520 530 540 550
PRHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN AYLELGGLGE
560 570 580 590 600
RVLGFCHLLL PDEQFPEGFQ FDTDEVNFPV DNLCFIGLIS MIDPPRAAVP
610 620 630 640 650
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI
660 670 680 690 700
PVSQVNPRDA KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI
710 720 730 740 750
IVEGCQRQGA IVAVTGDGVN DSPALKKADI GVAMGIAGSD 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 FHLLGIRVDW DDRWINDVED
910 920 930 940 950
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK
960 970 980 990 1000
NKILIFGLFE ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV
1010 1020
YDEIRKLIIR RRPGGWVEKE TYY
Length:1,023
Mass (Da):112,994
Last modified:March 1, 2004 - v2
Checksum:iF6BA59C8979F574D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF235024 mRNA. Translation: AAF60310.2.
RefSeqiNP_001156546.1. NM_001163074.1.
UniGeneiOcu.2457.

Genome annotation databases

GeneIDi100302415.
KEGGiocu:100302415.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF235024 mRNA. Translation: AAF60310.2.
RefSeqiNP_001156546.1. NM_001163074.1.
UniGeneiOcu.2457.

3D structure databases

ProteinModelPortaliQ9N0Z6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9N0Z6. 2 interactors.
STRINGi9986.ENSOCUP00000024821.

Proteomic databases

PRIDEiQ9N0Z6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100302415.
KEGGiocu:100302415.

Organism-specific databases

CTDi476.

Phylogenomic databases

eggNOGiKOG0203. Eukaryota.
COG0474. LUCA.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiQ9N0Z6.
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.
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.
[Graphical view]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
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]
ProtoNetiSearch...

Entry informationi

Entry nameiAT1A1_RABIT
AccessioniPrimary (citable) accession number: Q9N0Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 1, 2004
Last modified: October 5, 2016
This is version 96 of the entry and version 2 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

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.