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Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

ATP1A1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

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

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini6 – 8580CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei86 – 10621HelicalSequence AnalysisAdd
BLAST
Topological domaini107 – 12923ExtracellularSequence AnalysisAdd
BLAST
Transmembranei130 – 15021HelicalSequence AnalysisAdd
BLAST
Topological domaini151 – 286136CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei287 – 30620HelicalSequence AnalysisAdd
BLAST
Topological domaini307 – 31812ExtracellularSequence AnalysisAdd
BLAST
Transmembranei319 – 33618HelicalSequence AnalysisAdd
BLAST
Topological domaini337 – 770434CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei771 – 79020HelicalSequence AnalysisAdd
BLAST
Topological domaini791 – 80010ExtracellularSequence Analysis
Transmembranei801 – 82121HelicalSequence AnalysisAdd
BLAST
Topological domaini822 – 84120CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei842 – 86423HelicalSequence AnalysisAdd
BLAST
Topological domaini865 – 91652ExtracellularSequence AnalysisAdd
BLAST
Transmembranei917 – 93620HelicalSequence AnalysisAdd
BLAST
Topological domaini937 – 94913CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei950 – 96819HelicalSequence AnalysisAdd
BLAST
Topological domaini969 – 98315ExtracellularSequence AnalysisAdd
BLAST
Transmembranei984 – 100421HelicalSequence AnalysisAdd
BLAST
Topological domaini1005 – 102117CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 55By similarityPRO_0000305975
Chaini6 – 10211016Sodium/potassium-transporting ATPase subunit alpha-1By similarityPRO_0000305976Add
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 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

PaxDbiQ08DA1.
PRIDEiQ08DA1.

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001646.

Structurei

3D structure databases

ProteinModelPortaliQ08DA1.
SMRiQ08DA1. Positions 24-1021.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ08DA1.
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.
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.

Q08DA1-1 [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
LLWIGAVLCF LAYGIQAATE EEPQNDNLYL GVVLSAVVII TGCFSYYQEA
160 170 180 190 200
KSSKIMESFK NMVPQQALVI RNGEKMSINA EEVVVGDLVE VKGGDRIPAD
210 220 230 240 250
LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI AFFSTNCVEG
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 KTSATWLALS RIAGLCNRAV FQANQDNLPI LKRAVAGDAS
460 470 480 490 500
ESALLKCIEV CCGSVKEMRE RYTKIVEIPF NSTNKYQLSI HKNANAGEPR
510 520 530 540 550
HLLVMKGAPE RILDRCSSIL IHGKEQPLDE ELKDAFQNAY LELGGLGERV
560 570 580 590 600
LGFCHLLLPD EQFPEGFQFD TDDVNFPVDN LCFVGLISMI DPPRAAVPDA
610 620 630 640 650
VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISEGNETVE DIAARLNIPV
660 670 680 690 700
SQVNPRDARA CVVHGSDLKD MTPEQLDDIL KYHTEIVFAR TSPQQKLIIV
710 720 730 740 750
EGCQRQGAIV AVTGDGVNDS PALKKADIGV AMGIAGSDVS KQAADMILLD
760 770 780 790 800
DNFASIVTGV EEGRLIFDNL KKSIAYTLTS NIPEITPFLI FIIANIPLPL
810 820 830 840 850
GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPQTD KLVNERLISM
860 870 880 890 900
AYGQIGMIQA LGGFFTYFVI MAENGFLPNH LLGIRVTWDD 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):112,643
Last modified:October 31, 2006 - v1
Checksum:iE01CAF82B6F1A6FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC123864 mRNA. Translation: AAI23865.1.
RefSeqiNP_001070266.1. NM_001076798.1.
UniGeneiBt.54076.

Genome annotation databases

GeneIDi282144.
KEGGibta:282144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC123864 mRNA. Translation: AAI23865.1.
RefSeqiNP_001070266.1. NM_001076798.1.
UniGeneiBt.54076.

3D structure databases

ProteinModelPortaliQ08DA1.
SMRiQ08DA1. Positions 24-1021.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001646.

Proteomic databases

PaxDbiQ08DA1.
PRIDEiQ08DA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282144.
KEGGibta:282144.

Organism-specific databases

CTDi476.

Phylogenomic databases

eggNOGiCOG0474.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiQ08DA1.
KOiK01539.

Miscellaneous databases

NextBioi20805979.

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. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Basal ganglia.

Entry informationi

Entry nameiAT1A1_BOVIN
AccessioniPrimary (citable) accession number: Q08DA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 31, 2006
Last modified: June 24, 2015
This is version 67 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

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.