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Protein

Sodium/potassium-transporting ATPase subunit alpha-3

Gene

Atp1a3

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei366 – 36614-aspartylphosphate intermediateBy similarity
Metal bindingi707 – 7071MagnesiumBy similarity
Metal bindingi711 – 7111MagnesiumBy similarity

GO - Molecular functioni

  • ATP binding Source: RGD
  • cation-transporting ATPase activity Source: RGD
  • D1 dopamine receptor binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • sodium:potassium-exchanging ATPase activity Source: UniProtKB

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

Enzyme and pathway databases

ReactomeiREACT_345620. Ion transport by P-type ATPases.
SABIO-RKP06687.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium/potassium-transporting ATPase subunit alpha-3 (EC:3.6.3.9)
Short name:
Na(+)/K(+) ATPase alpha-3 subunit
Alternative name(s):
Na(+)/K(+) ATPase alpha(III) subunit
Sodium pump subunit alpha-3
Gene namesi
Name:Atp1a3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2169. Atp1a3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7777CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei78 – 9821HelicalSequence AnalysisAdd
BLAST
Topological domaini99 – 12123ExtracellularSequence AnalysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence AnalysisAdd
BLAST
Topological domaini143 – 278136CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei279 – 29820HelicalSequence AnalysisAdd
BLAST
Topological domaini299 – 31012ExtracellularSequence AnalysisAdd
BLAST
Transmembranei311 – 32818HelicalSequence AnalysisAdd
BLAST
Topological domaini329 – 762434CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei763 – 78220HelicalSequence AnalysisAdd
BLAST
Topological domaini783 – 79210ExtracellularSequence Analysis
Transmembranei793 – 81321HelicalSequence AnalysisAdd
BLAST
Topological domaini814 – 83320CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei834 – 85623HelicalSequence AnalysisAdd
BLAST
Topological domaini857 – 90852ExtracellularSequence AnalysisAdd
BLAST
Transmembranei909 – 92820HelicalSequence AnalysisAdd
BLAST
Topological domaini929 – 94113CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei942 – 96019HelicalSequence AnalysisAdd
BLAST
Topological domaini961 – 97515ExtracellularSequence AnalysisAdd
BLAST
Transmembranei976 – 99621HelicalSequence AnalysisAdd
BLAST
Topological domaini997 – 101317CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • axon Source: RGD
  • dendritic spine head Source: RGD
  • dendritic spine neck Source: RGD
  • endoplasmic reticulum Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • myelin sheath Source: UniProtKB
  • nucleus Source: Ensembl
  • plasma membrane Source: UniProtKB
  • sodium:potassium-exchanging ATPase complex Source: RGD
  • synapse Source: UniProtKB
  • vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10131013Sodium/potassium-transporting ATPase subunit alpha-3PRO_0000046300Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651PhosphoserineBy similarity
Modified residuei548 – 5481PhosphotyrosineBy similarity
Modified residuei933 – 9331Phosphoserine; by PKABy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP06687.
PRIDEiP06687.

PTM databases

PhosphoSiteiP06687.

Expressioni

Gene expression databases

GenevestigatoriP06687.

Interactioni

Subunit structurei

Composed of three subunits: alpha (catalytic), beta and gamma.

Protein-protein interaction databases

BioGridi246401. 5 interactions.
IntActiP06687. 2 interactions.
MINTiMINT-7138201.

Structurei

3D structure databases

ProteinModelPortaliP06687.
SMRiP06687. Positions 20-1013.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni72 – 743Interaction with phosphoinositide-3 kinaseBy similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00760000119003.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiP06687.
KOiK01539.
OMAiFCDFMLP.
OrthoDBiEOG7327N0.

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.
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.

P06687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDKKDDKSS PKKSKAKERR DLDDLKKEVA MTEHKMSVEE VCRKYNTDCV
60 70 80 90 100
QGLTHSKAQE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SILLWIGAIL
110 120 130 140 150
CFLAYGIQAG TEDDPSGDNL YLGIVLAAVV IITGCFSYYQ EAKSSKIMES
160 170 180 190 200
FKNMVPQQAL VIREGEKMQV NAEEVVVGDL VEIKGGDRVP ADLRIISAHG
210 220 230 240 250
CKVDNSSLTG ESEPQTRSPD CTHDNPLETR NITFFSTNCV EGTARGVVVA
260 270 280 290 300
TGDRTVMGRI ATLASGLEVG KTPIAIEIEH FIQLITGVAV FLGVSFFILS
310 320 330 340 350
LILGYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
360 370 380 390 400
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTEDQSGTS
410 420 430 440 450
FDKSSHTWVA LSHIAGLCNR AVFKGGQDNI PVLKRDVAGD ASESALLKCI
460 470 480 490 500
ELSSGSVKLM RERNKKVAEI PFNSTNKYQL SIHETEDPND NRYLLVMKGA
510 520 530 540 550
PERILDRCAT ILLQGKEQPL DEEMKEAFQN AYLELGGLGE RVLGFCHYYL
560 570 580 590 600
PEEQFPKGFA FDCDDVNFTT DNLCFVGLMS MIDPPRAAVP DAVGKCRSAG
610 620 630 640 650
IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA
660 670 680 690 700
KACVIHGTDL KDFTSEQIDE ILQNHTEIVF ARTSPQQKLI IVEGCQRQGA
710 720 730 740 750
IVAVTGDGVN DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT
760 770 780 790 800
GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LLFIMANIPL PLGTITILCI
810 820 830 840 850
DLGTDMVPAI SLAYEAAESD IMKRQPRNPR TDKLVNERLI SMAYGQIGMI
860 870 880 890 900
QALGGFFSYF VILAENGFLP GNLVGIRLNW DDRTVNDLED SYGQQWTYEQ
910 920 930 940 950
RKVVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE
960 970 980 990 1000
ETALAAFLSY CPGMDVALRM YPLKPSWWFC AFPYSFLIFV YDEIRKLILR
1010
RNPGGWVEKE TYY
Length:1,013
Mass (Da):111,692
Last modified:October 18, 2001 - v2
Checksum:i72F051406284EA8A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 33MGD → MNL in AAA41672 (PubMed:2822726).Curated
Sequence conflicti104 – 1041A → R in AAA41672 (PubMed:2822726).Curated
Sequence conflicti114 – 1141D → E in AAA41672 (PubMed:2822726).Curated
Sequence conflicti128 – 1281A → G in AAA41672 (PubMed:2822726).Curated
Sequence conflicti149 – 1491E → Q in AAA41672 (PubMed:2822726).Curated
Sequence conflicti152 – 1521K → T in AAA41672 (PubMed:2822726).Curated
Sequence conflicti166 – 1661E → D in AAA41672 (PubMed:2822726).Curated
Sequence conflicti192 – 1943DLR → ELG in AAA41672 (PubMed:2822726).Curated
Sequence conflicti200 – 2001G → R in AAA41672 (PubMed:2822726).Curated
Sequence conflicti339 – 3391Missing in AAA41672 (PubMed:2822726).Curated
Sequence conflicti621 – 6211V → K in AAA41672 (PubMed:2822726).Curated
Sequence conflicti807 – 8093VPA → DPT in AAA41672 (PubMed:2822726).Curated
Sequence conflicti908 – 9081C → F in AAA40777 (PubMed:3028470).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14513 mRNA. Translation: AAA40777.1.
X05883 mRNA. Translation: CAA29307.1.
M28648 mRNA. Translation: AAA41672.1.
PIRiC24639.
RefSeqiNP_036638.1. NM_012506.1.
UniGeneiRn.87329.

Genome annotation databases

EnsembliENSRNOT00000027497; ENSRNOP00000027497; ENSRNOG00000020263.
GeneIDi24213.
KEGGirno:24213.
UCSCiRGD:2169. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14513 mRNA. Translation: AAA40777.1.
X05883 mRNA. Translation: CAA29307.1.
M28648 mRNA. Translation: AAA41672.1.
PIRiC24639.
RefSeqiNP_036638.1. NM_012506.1.
UniGeneiRn.87329.

3D structure databases

ProteinModelPortaliP06687.
SMRiP06687. Positions 20-1013.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246401. 5 interactions.
IntActiP06687. 2 interactions.
MINTiMINT-7138201.

PTM databases

PhosphoSiteiP06687.

Proteomic databases

PaxDbiP06687.
PRIDEiP06687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027497; ENSRNOP00000027497; ENSRNOG00000020263.
GeneIDi24213.
KEGGirno:24213.
UCSCiRGD:2169. rat.

Organism-specific databases

CTDi478.
RGDi2169. Atp1a3.

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00760000119003.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiP06687.
KOiK01539.
OMAiFCDFMLP.
OrthoDBiEOG7327N0.

Enzyme and pathway databases

ReactomeiREACT_345620. Ion transport by P-type ATPases.
SABIO-RKP06687.

Miscellaneous databases

NextBioi602625.
PROiP06687.

Gene expression databases

GenevestigatoriP06687.

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.
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]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of three distinct forms of the Na+,K+-ATPase alpha-subunit from rat brain."
    Shull G.E., Greeb J., Lingrel J.B.
    Biochemistry 25:8125-8132(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Primary structures of two types of alpha-subunit of rat brain Na+,K+,-ATPase deduced from cDNA sequences."
    Hara Y., Urayama O., Kawakami K., Nojima H., Nagamune H., Kojima T., Ohta T., Nagano K., Nakao M.
    J. Biochem. 102:43-58(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Three differentially expressed Na,K-ATPase alpha subunit isoforms: structural and functional implications."
    Herrera V.L.M., Emanuel J.R., Ruiz-Opazo N., Levenson R., Nadal-Ginard B.
    J. Cell Biol. 105:1855-1865(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-930.
    Tissue: Brain and Liver.
  4. Lubec G., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 58-64; 147-152; 246-254; 260-271; 425-434; 436-448; 517-525; 587-595; 620-648; 734-763 AND 878-883, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.

Entry informationi

Entry nameiAT1A3_RAT
AccessioniPrimary (citable) accession number: P06687
Secondary accession number(s): Q16732, Q9Z1G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 18, 2001
Last modified: May 27, 2015
This is version 149 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.