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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 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).By similarity

Catalytic activityi

ATP + H2O + Na+(In) + K+(Out) = ADP + phosphate + Na+(Out) + K+(In).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei3744-aspartylphosphate intermediateBy similarity1
Binding sitei485ATPBy similarity1
Metal bindingi715MagnesiumBy similarity1
Metal bindingi719MagnesiumBy similarity1

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
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini6 – 85CytoplasmicSequence analysisAdd BLAST80
Transmembranei86 – 106HelicalSequence analysisAdd BLAST21
Topological domaini107 – 129ExtracellularSequence analysisAdd BLAST23
Transmembranei130 – 150HelicalSequence analysisAdd BLAST21
Topological domaini151 – 286CytoplasmicSequence analysisAdd BLAST136
Transmembranei287 – 306HelicalSequence analysisAdd BLAST20
Topological domaini307 – 318ExtracellularSequence analysisAdd BLAST12
Transmembranei319 – 336HelicalSequence analysisAdd BLAST18
Topological domaini337 – 770CytoplasmicSequence analysisAdd BLAST434
Transmembranei771 – 790HelicalSequence analysisAdd BLAST20
Topological domaini791 – 800ExtracellularSequence analysis10
Transmembranei801 – 821HelicalSequence analysisAdd BLAST21
Topological domaini822 – 841CytoplasmicSequence analysisAdd BLAST20
Transmembranei842 – 864HelicalSequence analysisAdd BLAST23
Topological domaini865 – 916ExtracellularSequence analysisAdd BLAST52
Transmembranei917 – 936HelicalSequence analysisAdd BLAST20
Topological domaini937 – 949CytoplasmicSequence analysisAdd BLAST13
Transmembranei950 – 968HelicalSequence analysisAdd BLAST19
Topological domaini969 – 983ExtracellularSequence analysisAdd BLAST15
Transmembranei984 – 1004HelicalSequence analysisAdd BLAST21
Topological domaini1005 – 1021CytoplasmicSequence analysisAdd BLAST17

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00003059751 – 5By similarity5
ChainiPRO_00003059766 – 1021Sodium/potassium-transporting ATPase subunit alpha-1By similarityAdd BLAST1016

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 residuei38PhosphoserineBy similarity1
Modified residuei45PhosphoserineBy similarity1
Modified residuei226PhosphoserineBy similarity1
Modified residuei258PhosphotyrosineBy similarity1
Modified residuei450PhosphoserineBy similarity1
Modified residuei482PhosphoserineBy similarity1
Modified residuei540PhosphotyrosineBy similarity1
Modified residuei666PhosphoserineBy similarity1
Modified residuei941Phosphoserine; by PKABy similarity1

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.
PeptideAtlasiQ08DA1.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XE5X-ray3.90A1-1021[»]
ProteinModelPortaliQ08DA1.
SMRiQ08DA1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni80 – 82Phosphoinositide-3 kinase bindingBy similarity3

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0203. Eukaryota.
COG0474. LUCA.
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.
[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.

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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XE5X-ray3.90A1-1021[»]
ProteinModelPortaliQ08DA1.
SMRiQ08DA1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001646.

Proteomic databases

PaxDbiQ08DA1.
PeptideAtlasiQ08DA1.
PRIDEiQ08DA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282144.
KEGGibta:282144.

Organism-specific databases

CTDi476.

Phylogenomic databases

eggNOGiKOG0203. Eukaryota.
COG0474. LUCA.
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.
[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_BOVIN
AccessioniPrimary (citable) accession number: Q08DA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 31, 2006
Last modified: November 2, 2016
This is version 78 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.