UniProtKB - P06685 (AT1A1_RAT)
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Protein
Sodium/potassium-transporting ATPase subunit alpha-1
Gene
Atp1a1
Organism
Rattus norvegicus (Rat)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 376 | 4-aspartylphosphate intermediateBy similarity | 1 | |
Binding sitei | 487 | ATP1 Publication | 1 | |
Metal bindingi | 717 | MagnesiumBy similarity | 1 | |
Metal bindingi | 721 | MagnesiumBy similarity | 1 |
GO - Molecular functioni
- ADP binding Source: RGD
- ankyrin binding Source: BHF-UCL
- ATP binding Source: BHF-UCL
- chaperone binding Source: BHF-UCL
- phosphatase activity Source: RGD
- phosphatidylinositol 3-kinase binding Source: RGD
- potassium ion binding Source: BHF-UCL
- protein domain specific binding Source: RGD
- protein kinase binding Source: UniProtKB
- sodium:potassium-exchanging ATPase activity Source: UniProtKB
- sodium ion binding Source: RGD
- steroid hormone binding Source: RGD
GO - Biological processi
- ATP hydrolysis coupled transmembrane transport Source: BHF-UCL
- cardiac muscle contraction Source: BHF-UCL
- cellular potassium ion homeostasis Source: RGD
- cellular response to mechanical stimulus Source: RGD
- cellular response to steroid hormone stimulus Source: RGD
- cellular sodium ion homeostasis Source: RGD
- energy coupled proton transmembrane transport, against electrochemical gradient Source: RGD
- establishment or maintenance of transmembrane electrochemical gradient Source: BHF-UCL
- membrane hyperpolarization Source: RGD
- membrane repolarization Source: RGD
- negative regulation of glucocorticoid biosynthetic process Source: RGD
- negative regulation of heart contraction Source: RGD
- positive regulation of heart contraction Source: RGD
- positive regulation of striated muscle contraction Source: RGD
- potassium ion import Source: RGD
- potassium ion import across plasma membrane Source: BHF-UCL
- potassium ion transport Source: RGD
- regulation of blood pressure Source: RGD
- regulation of cardiac muscle cell contraction Source: RGD
- regulation of sodium ion transport Source: UniProtKB
- regulation of the force of heart contraction Source: RGD
- relaxation of cardiac muscle Source: BHF-UCL
- response to drug Source: RGD
- response to glycoside Source: RGD
- sodium ion export across plasma membrane Source: BHF-UCL
- sodium ion transport Source: RGD
Keywordsi
Molecular function | Hydrolase |
Biological process | Ion transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Sodium |
Enzyme and pathway databases
Reactomei | R-RNO-5578775. Ion homeostasis. R-RNO-936837. Ion transport by P-type ATPases. |
SABIO-RKi | P06685. |
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 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2167. Atp1a1. |
Subcellular locationi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 6 – 87 | CytoplasmicSequence analysisAdd BLAST | 82 | |
Transmembranei | 88 – 108 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 109 – 131 | ExtracellularSequence analysisAdd BLAST | 23 | |
Transmembranei | 132 – 152 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 153 – 288 | CytoplasmicSequence analysisAdd BLAST | 136 | |
Transmembranei | 289 – 308 | HelicalSequence analysisAdd BLAST | 20 | |
Topological domaini | 309 – 320 | ExtracellularSequence analysisAdd BLAST | 12 | |
Transmembranei | 321 – 338 | HelicalSequence analysisAdd BLAST | 18 | |
Topological domaini | 339 – 772 | CytoplasmicSequence analysisAdd BLAST | 434 | |
Transmembranei | 773 – 792 | HelicalSequence analysisAdd BLAST | 20 | |
Topological domaini | 793 – 802 | ExtracellularSequence analysis | 10 | |
Transmembranei | 803 – 823 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 824 – 843 | CytoplasmicSequence analysisAdd BLAST | 20 | |
Transmembranei | 844 – 866 | HelicalSequence analysisAdd BLAST | 23 | |
Topological domaini | 867 – 918 | ExtracellularSequence analysisAdd BLAST | 52 | |
Transmembranei | 919 – 938 | HelicalSequence analysisAdd BLAST | 20 | |
Topological domaini | 939 – 951 | CytoplasmicSequence analysisAdd BLAST | 13 | |
Transmembranei | 952 – 970 | HelicalSequence analysisAdd BLAST | 19 | |
Topological domaini | 971 – 985 | ExtracellularSequence analysisAdd BLAST | 15 | |
Transmembranei | 986 – 1006 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1007 – 1023 | CytoplasmicSequence analysisAdd BLAST | 17 |
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 16 | S → A: Dopamine fails to increase phosphoinositide-3 kinase activity and to promote its interaction with Na(+)/K(+) ATPase. 1 Publication | 1 | |
Mutagenesisi | 83 | P → R: Dopamine fails to increase phosphoinositide-3 kinase activity and to promote its interaction with Na(+)/K(+) ATPase. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3010. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
PropeptideiPRO_0000002489 | 1 – 5 | 1 Publication | 5 | |
ChainiPRO_0000002490 | 6 – 1023 | Sodium/potassium-transporting ATPase subunit alpha-1Add BLAST | 1018 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 9 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 10 | Phosphotyrosine1 Publication | 1 | |
Modified residuei | 16 | Phosphoserine; by PKC1 Publication | 1 | |
Modified residuei | 21 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 23 | Phosphoserine; by PKC2 Publications | 1 | |
Modified residuei | 40 | PhosphoserineCombined sources | 1 | |
Modified residuei | 47 | PhosphoserineCombined sources | 1 | |
Modified residuei | 228 | PhosphoserineCombined sources | 1 | |
Modified residuei | 260 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 452 | PhosphoserineCombined sources | 1 | |
Modified residuei | 484 | PhosphoserineCombined sources | 1 | |
Modified residuei | 542 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 661 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 668 | PhosphoserineBy similarity | 1 | |
Modified residuei | 675 | PhosphoserineBy similarity | 1 | |
Modified residuei | 943 | Phosphoserine; by PKA1 Publication | 1 |
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.5 Publications
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
PaxDbi | P06685. |
PRIDEi | P06685. |
PTM databases
iPTMneti | P06685. |
PhosphoSitePlusi | P06685. |
Interactioni
Subunit structurei
The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1 (PubMed:17283221, PubMed:19339511, PubMed:23532852). Interacts with regulatory subunit FXYD3 (PubMed:15743908). Interacts with SLC35G1 and STIM1 (By similarity). Interacts with SIK1 (PubMed:17939993).By similarity5 Publications
GO - Molecular functioni
- ankyrin binding Source: BHF-UCL
- chaperone binding Source: BHF-UCL
- phosphatidylinositol 3-kinase binding Source: RGD
- protein domain specific binding Source: RGD
- protein kinase binding Source: UniProtKB
Protein-protein interaction databases
BioGridi | 246399. 10 interactors. |
ELMi | P06685. |
IntActi | P06685. 4 interactors. |
MINTi | P06685. |
STRINGi | 10116.ENSRNOP00000045650. |
Chemistry databases
BindingDBi | P06685. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 394 – 396 | Combined sources | 3 | |
Beta strandi | 403 – 405 | Combined sources | 3 | |
Helixi | 416 – 427 | Combined sources | 12 | |
Beta strandi | 431 – 435 | Combined sources | 5 | |
Beta strandi | 438 – 440 | Combined sources | 3 | |
Helixi | 442 – 444 | Combined sources | 3 | |
Beta strandi | 447 – 449 | Combined sources | 3 | |
Turni | 451 – 453 | Combined sources | 3 | |
Helixi | 454 – 461 | Combined sources | 8 | |
Turni | 462 – 464 | Combined sources | 3 | |
Helixi | 467 – 473 | Combined sources | 7 | |
Beta strandi | 478 – 480 | Combined sources | 3 | |
Turni | 483 – 485 | Combined sources | 3 | |
Beta strandi | 489 – 494 | Combined sources | 6 | |
Beta strandi | 496 – 500 | Combined sources | 5 | |
Beta strandi | 502 – 509 | Combined sources | 8 | |
Helixi | 511 – 515 | Combined sources | 5 | |
Beta strandi | 518 – 521 | Combined sources | 4 | |
Beta strandi | 526 – 529 | Combined sources | 4 | |
Helixi | 532 – 546 | Combined sources | 15 | |
Beta strandi | 556 – 558 | Combined sources | 3 | |
Turni | 562 – 564 | Combined sources | 3 | |
Turni | 572 – 574 | Combined sources | 3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1MO7 | NMR | - | A | 386-595 | [»] | |
1MO8 | NMR | - | A | 386-595 | [»] | |
ProteinModelPortali | P06685. | |||||
SMRi | P06685. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P06685. |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 82 – 84 | Phosphoinositide-3 kinase binding | 3 |
Sequence similaritiesi
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification]Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0203. Eukaryota. COG0474. LUCA. |
GeneTreei | ENSGT00890000139334. |
HOVERGENi | HBG004298. |
InParanoidi | P06685. |
KOi | K01539. |
OMAi | ARIMPEQ. |
OrthoDBi | EOG091G01BB. |
PhylomeDBi | P06685. |
Family and domain databases
CDDi | cd02608. P-type_ATPase_Na-K_like. 1 hit. |
Gene3Di | 3.40.1110.10. 1 hit. 3.40.50.1000. 2 hits. |
InterProi | View protein in InterPro IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023299. ATPase_P-typ_cyto_dom_N. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom_sf. IPR008250. ATPase_P-typ_transduc_dom_A_sf. IPR036412. HAD-like_sf. IPR023214. HAD_sf. IPR005775. P-type_ATPase_IIC. IPR001757. P_typ_ATPase. |
Pfami | View protein in Pfam PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. |
SMARTi | View protein in SMART SM00831. Cation_ATPase_N. 1 hit. |
SUPFAMi | SSF56784. SSF56784. 1 hit. SSF81653. SSF81653. 1 hit. SSF81660. SSF81660. 1 hit. SSF81665. SSF81665. 3 hits. |
TIGRFAMsi | TIGR01106. ATPase-IIC_X-K. 1 hit. TIGR01494. ATPase_P-type. 2 hits. |
PROSITEi | View protein in PROSITE PS00154. ATPASE_E1_E2. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P06685-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGKGVGRDKY EPAAVSEHGD KKSKKAKKER DMDELKKEVS MDDHKLSLDE
60 70 80 90 100
LHRKYGTDLS RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF
110 120 130 140 150
SMLLWIGAIL CFLAYGIRSA TEEEPPNDDL YLGVVLSAVV 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
EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV
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 FDKTSATWFA LSRIAGLCNR AVFQANQENL PILKRAVAGD
460 470 480 490 500
ASESALLKCI EVCCGSVMEM REKYTKIVEI PFNSTNKYQL SIHKNPNASE
510 520 530 540 550
PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN AYLELGGLGE
560 570 580 590 600
RVLGFCHLLL PDEQFPEGFQ FDTDEVNFPV DNLCFVGLIS MIDPPRAAVP
610 620 630 640 650
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI
660 670 680 690 700
PVNQVNPRDA KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI
710 720 730 740 750
IVEGCQRQGA IVAVTGDGVN DSPALKKADI GVAMGIVGSD 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 FHLLGIRETW DDRWINDVED
910 920 930 940 950
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK
960 970 980 990 1000
NKILIFGLFE ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV
1010 1020
YDEVRKLIIR RRPGGWVEKE TYY
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 68 – 69 | AA → PV in AAA41671 (PubMed:2822726).Curated | 2 | |
Sequence conflicti | 175 | G → E in AAA41671 (PubMed:2822726).Curated | 1 | |
Sequence conflicti | 188 | G → V in AAA41671 (PubMed:2822726).Curated | 1 | |
Sequence conflicti | 335 | G → V in AAA41671 (PubMed:2822726).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M14511 mRNA. Translation: AAA40775.1. X05882 mRNA. Translation: CAA29306.1. M28647 mRNA. Translation: AAA41671.1. BC061968 mRNA. Translation: AAH61968.1. M11733 mRNA. Translation: AAA40783.1. X53233 Genomic DNA. Translation: CAA37325.1. X53234 Genomic DNA. Translation: CAA37326.1. |
PIRi | A24639. |
RefSeqi | NP_036636.1. NM_012504.1. |
UniGenei | Rn.217534. Rn.2992. |
Genome annotation databases
Ensembli | ENSRNOT00000040430; ENSRNOP00000045650; ENSRNOG00000030019. |
GeneIDi | 24211. |
KEGGi | rno:24211. |
UCSCi | RGD:2167. rat. |
Similar proteinsi
Entry informationi
Entry namei | AT1A1_RAT | |
Accessioni | P06685Primary (citable) accession number: P06685 Secondary accession number(s): Q64609 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | January 1, 1988 | |
Last modified: | February 28, 2018 | |
This is version 189 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |