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Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

ATP1A1

Organism
Sus scrofa (Pig)
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 sitei3744-aspartylphosphate intermediateBy similarity1
Binding sitei485ATPBy similarity1
Metal bindingi715MagnesiumBy similarity1
Metal bindingi719MagnesiumBy similarity1

GO - Molecular functioni

  • ATPase binding Source: BHF-UCL
  • ATP binding Source: BHF-UCL
  • potassium ion binding Source: BHF-UCL
  • sodium:potassium-exchanging ATPase activity Source: UniProtKB
  • sodium ion binding Source: AgBase

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: GO_Central
  • ATP hydrolysis coupled transmembrane transport Source: BHF-UCL
  • cellular potassium ion homeostasis Source: BHF-UCL
  • cellular sodium ion homeostasis Source: BHF-UCL
  • establishment or maintenance of transmembrane electrochemical gradient Source: BHF-UCL
  • membrane repolarization Source: BHF-UCL
  • potassium ion import Source: BHF-UCL
  • potassium ion import across plasma membrane Source: BHF-UCL
  • regulation of sodium ion transport Source: UniProtKB
  • sodium ion export from cell Source: BHF-UCL
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

BRENDAi3.6.3.9. 6170.

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 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

  • integral component of membrane Source: UniProtKB
  • intracellular membrane-bounded organelle Source: GO_Central
  • plasma membrane Source: UniProtKB
  • sarcolemma Source: BHF-UCL
  • sodium:potassium-exchanging ATPase complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4131.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000024871 – 55
ChainiPRO_00000024886 – 1021Sodium/potassium-transporting ATPase subunit alpha-1Add 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 residuei659N6-succinyllysineBy similarity1
Modified residuei666PhosphoserineBy similarity1
Modified residuei673PhosphoserineBy 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

PaxDbiP05024.
PeptideAtlasiP05024.
PRIDEiP05024.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • ATPase binding Source: BHF-UCL

Protein-protein interaction databases

DIPiDIP-60365N.
IntActiP05024. 1 interactor.
STRINGi9823.ENSSSCP00000007190.

Chemistry databases

BindingDBiP05024.

Structurei

Secondary structure

11021
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 30Combined sources4
Helixi31 – 33Combined sources3
Beta strandi42 – 44Combined sources3
Helixi46 – 53Combined sources8
Turni57 – 59Combined sources3
Helixi63 – 73Combined sources11
Helixi86 – 94Combined sources9
Turni95 – 97Combined sources3
Helixi98 – 119Combined sources22
Beta strandi120 – 122Combined sources3
Helixi126 – 155Combined sources30
Helixi157 – 159Combined sources3
Beta strandi166 – 169Combined sources4
Beta strandi172 – 174Combined sources3
Beta strandi176 – 179Combined sources4
Helixi180 – 182Combined sources3
Beta strandi185 – 191Combined sources7
Beta strandi193 – 196Combined sources4
Beta strandi199 – 212Combined sources14
Helixi214 – 217Combined sources4
Beta strandi223 – 225Combined sources3
Turni234 – 236Combined sources3
Beta strandi238 – 241Combined sources4
Beta strandi246 – 258Combined sources13
Helixi260 – 262Combined sources3
Helixi264 – 267Combined sources4
Beta strandi272 – 274Combined sources3
Helixi281 – 310Combined sources30
Helixi315 – 328Combined sources14
Helixi333 – 350Combined sources18
Turni351 – 353Combined sources3
Beta strandi354 – 357Combined sources4
Helixi361 – 366Combined sources6
Beta strandi370 – 373Combined sources4
Helixi375 – 379Combined sources5
Beta strandi385 – 391Combined sources7
Beta strandi394 – 397Combined sources4
Beta strandi401 – 403Combined sources3
Helixi414 – 425Combined sources12
Beta strandi436 – 438Combined sources3
Turni440 – 442Combined sources3
Beta strandi445 – 447Combined sources3
Helixi449 – 461Combined sources13
Helixi465 – 471Combined sources7
Beta strandi474 – 478Combined sources5
Turni482 – 484Combined sources3
Beta strandi486 – 492Combined sources7
Beta strandi495 – 497Combined sources3
Beta strandi500 – 507Combined sources8
Helixi509 – 514Combined sources6
Beta strandi516 – 521Combined sources6
Beta strandi524 – 527Combined sources4
Helixi530 – 545Combined sources16
Beta strandi548 – 558Combined sources11
Turni560 – 562Combined sources3
Turni571 – 574Combined sources4
Beta strandi578 – 590Combined sources13
Helixi597 – 605Combined sources9
Turni606 – 608Combined sources3
Beta strandi610 – 614Combined sources5
Helixi619 – 628Combined sources10
Helixi639 – 646Combined sources8
Helixi650 – 652Combined sources3
Helixi655 – 657Combined sources3
Beta strandi659 – 664Combined sources6
Helixi665 – 668Combined sources4
Helixi673 – 681Combined sources9
Beta strandi684 – 689Combined sources6
Helixi693 – 705Combined sources13
Beta strandi710 – 714Combined sources5
Helixi717 – 719Combined sources3
Helixi720 – 725Combined sources6
Beta strandi726 – 732Combined sources7
Turni733 – 735Combined sources3
Helixi738 – 743Combined sources6
Beta strandi745 – 748Combined sources4
Helixi755 – 779Combined sources25
Helixi781 – 793Combined sources13
Helixi802 – 812Combined sources11
Helixi815 – 819Combined sources5
Turni820 – 822Combined sources3
Helixi829 – 831Combined sources3
Turni837 – 839Combined sources3
Beta strandi842 – 844Combined sources3
Helixi845 – 851Combined sources7
Turni852 – 854Combined sources3
Helixi855 – 873Combined sources19
Helixi878 – 881Combined sources4
Turni882 – 884Combined sources3
Helixi885 – 888Combined sources4
Beta strandi895 – 897Combined sources3
Beta strandi899 – 901Combined sources3
Helixi906 – 934Combined sources29
Beta strandi938 – 940Combined sources3
Helixi942 – 945Combined sources4
Helixi950 – 968Combined sources19
Helixi972 – 975Combined sources4
Helixi983 – 988Combined sources6
Helixi990 – 1009Combined sources20
Beta strandi1010 – 1012Combined sources3
Helixi1016 – 1019Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3B8EX-ray3.50A/C24-1021[»]
3KDPX-ray3.50A/C24-1021[»]
3N23X-ray4.60A/C30-1021[»]
3WGUX-ray2.80A/C6-1021[»]
3WGVX-ray2.80A/C6-1021[»]
4HQJX-ray4.30A/C1-1021[»]
4HYTX-ray3.40A/C1-1021[»]
4RESX-ray3.41A/C1-1021[»]
4RETX-ray4.00A/C1-1021[»]
ProteinModelPortaliP05024.
SMRiP05024.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05024.

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.
InParanoidiP05024.
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.

P05024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH
60 70 80 90 100
RKYGTDLSRG LTPARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM
110 120 130 140 150
LLWIGAILCF 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 SDNQIHEADT
410 420 430 440 450
TENQSGVSFD KTSATWLALS RIAGLCNRAV FQANQENLPI LKRAVAGDAS
460 470 480 490 500
ESALLKCIEL CCGSVKEMRE RYTKIVEIPF NSTNKYQLSI HKNPNTAEPR
510 520 530 540 550
HLLVMKGAPE RILDRCSSIL IHGKEQPLDE ELKDAFQNAY LELGGLGERV
560 570 580 590 600
LGFCHLFLPD EQFPEGFQFD TDDVNFPLDN LCFVGLISMI DPPRAAVPDA
610 620 630 640 650
VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISEGNETVE DIAARLNIPV
660 670 680 690 700
SQVNPRDAKA CVVHGSDLKD MTSEQLDDIL KYHTEIVFAR TSPQQKLIIV
710 720 730 740 750
EGCQRQGAIV AVTGDGVNDS PASKKADIGV AMGIAGSDVS KQAADMILLD
760 770 780 790 800
DNFASIVTGV EEGRLIFDNL KKSIAYTLTS NIPEITPFLI FIIANIPLPL
810 820 830 840 850
GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD KLVNEQLISM
860 870 880 890 900
AYGQIGMIQA LGGFFTYFVI LAENGFLPIH LLGLRVNWDD RWINDVEDSY
910 920 930 940 950
GQQWTYEQRK IVEFTCHTPF FVTIVVVQWA DLVICKTRRN SVFQQGMKNK
960 970 980 990 1000
ILIFGLFEET ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD
1010 1020
EVRKLIIRRR PGGWVEKETY Y
Length:1,021
Mass (Da):112,681
Last modified:November 1, 1988 - v1
Checksum:iF369C6273CEB561D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti7R → P no nucleotide entry (PubMed:3032208).Curated1
Sequence conflicti7R → P no nucleotide entry (PubMed:2844194).Curated1
Sequence conflicti391S → F no nucleotide entry (PubMed:3032208).Curated1
Sequence conflicti391S → F no nucleotide entry (PubMed:2844194).Curated1
Sequence conflicti517S → T no nucleotide entry (PubMed:3032208).Curated1
Sequence conflicti517S → T no nucleotide entry (PubMed:2844194).Curated1
Sequence conflicti723S → L no nucleotide entry (PubMed:3032208).Curated1
Sequence conflicti723S → L no nucleotide entry (PubMed:2844194).Curated1
Sequence conflicti835R → Q no nucleotide entry (PubMed:3032208).Curated1
Sequence conflicti835R → Q no nucleotide entry (PubMed:2844194).Curated1
Sequence conflicti919P → A no nucleotide entry (PubMed:3032208).Curated1
Sequence conflicti919P → A no nucleotide entry (PubMed:2844194).Curated1
Sequence conflicti923T → S no nucleotide entry (PubMed:3032208).Curated1
Sequence conflicti923T → S no nucleotide entry (PubMed:2844194).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03938 mRNA. Translation: CAA27576.1.
M38445 mRNA. Translation: AAA31002.1.
M32512 mRNA. Translation: AAA31004.1.
PIRiB24862.
RefSeqiNP_999414.1. NM_214249.1.
UniGeneiSsc.12630.

Genome annotation databases

GeneIDi397481.
KEGGissc:397481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03938 mRNA. Translation: CAA27576.1.
M38445 mRNA. Translation: AAA31002.1.
M32512 mRNA. Translation: AAA31004.1.
PIRiB24862.
RefSeqiNP_999414.1. NM_214249.1.
UniGeneiSsc.12630.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3B8EX-ray3.50A/C24-1021[»]
3KDPX-ray3.50A/C24-1021[»]
3N23X-ray4.60A/C30-1021[»]
3WGUX-ray2.80A/C6-1021[»]
3WGVX-ray2.80A/C6-1021[»]
4HQJX-ray4.30A/C1-1021[»]
4HYTX-ray3.40A/C1-1021[»]
4RESX-ray3.41A/C1-1021[»]
4RETX-ray4.00A/C1-1021[»]
ProteinModelPortaliP05024.
SMRiP05024.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60365N.
IntActiP05024. 1 interactor.
STRINGi9823.ENSSSCP00000007190.

Chemistry databases

BindingDBiP05024.
ChEMBLiCHEMBL4131.

Proteomic databases

PaxDbiP05024.
PeptideAtlasiP05024.
PRIDEiP05024.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397481.
KEGGissc:397481.

Organism-specific databases

CTDi476.

Phylogenomic databases

eggNOGiKOG0203. Eukaryota.
COG0474. LUCA.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiP05024.
KOiK01539.

Enzyme and pathway databases

BRENDAi3.6.3.9. 6170.

Miscellaneous databases

EvolutionaryTraceiP05024.

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_PIG
AccessioniPrimary (citable) accession number: P05024
Secondary accession number(s): P18874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1988
Last modified: November 2, 2016
This is version 146 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.