UniProtKB - P06685 (AT1A1_RAT)

BLAST

>sp|P06685|AT1A1_RAT Sodium/potassium-transporting ATPase subunit alpha-1 OS=Rattus norvegicus OX=10116 GN=Atp1a1 PE=1 SV=1
MGKGVGRDKYEPAAVSEHGDKKSKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLS
RGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRSA
TEEEPPNDDLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSI
NAEDVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETR
NIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAEEIEHFIHLITGVAV
FLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKN
LEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWFA
LSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIEVCCGSVMEMREKYTKIVEI
PFNSTNKYQLSIHKNPNASEPKHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQN
AYLELGGLGERVLGFCHLLLPDEQFPEGFQFDTDEVNFPVDNLCFVGLISMIDPPRAAVP
DAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNQVNPRDA
KACVVHGSDLKDMTSEELDDILRYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVN
DSPALKKADIGVAMGIVGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTL
TSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPK
TDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPFHLLGIRETWDDRWINDVED
SYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFE
ETALAAFLSYCPGMGAALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKE
TYY

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History
Entry version 193 (12 Sep 2018)
Sequence version 1 (01 Jan 1988)
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Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

Atp1a1

Organism

Rattus norvegicus (Rat)

Status

Reviewed-Annotation score: -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 key	Position(s)	DescriptionActions	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
Inferred from direct assayⁱ
- 12730684
ankyrin binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 8159688
ATP binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 18075585
chaperone binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 18768923
phosphatase activity Source: Ensembl
phosphatidylinositol 3-kinase binding
Source: RGD
Inferred from physical interactionⁱ
- 17728397
potassium ion binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 18075585
protein domain specific binding
Source: RGD
Inferred from physical interactionⁱ
- 16269407
protein kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17939993
sodium:potassium-exchanging ATPase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 17939993
sodium ion binding
Source: RGD
Inferred from direct assayⁱ
- 16269407
steroid hormone binding Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

ATP hydrolysis coupled transmembrane transport
Source: BHF-UCL
Inferred from direct assayⁱ
- 18075585
cardiac muscle contraction
Source: BHF-UCL
Traceable author statementⁱ
- 17442282
cellular potassium ion homeostasis Source: Ensembl
cellular response to mechanical stimulus
Source: RGD
Inferred from direct assayⁱ
- 17458903
cellular response to steroid hormone stimulus Source: Ensembl
cellular sodium ion homeostasis Source: Ensembl
energy coupled proton transmembrane transport, against electrochemical gradient
Source: RGD
Traceable author statementⁱ
- 16269407
establishment or maintenance of transmembrane electrochemical gradient
Source: BHF-UCL
Inferred by curatorⁱ
- 18075585
membrane hyperpolarization
Source: RGD
Inferred from mutant phenotypeⁱ
- 17001300
membrane repolarization Source: Ensembl
negative regulation of glucocorticoid biosynthetic process Source: Ensembl
negative regulation of heart contraction Source: Ensembl
positive regulation of heart contraction Source: Ensembl
positive regulation of striated muscle contraction Source: Ensembl
potassium ion import
Source: RGD
Inferred from direct assayⁱ
- 12531906
potassium ion import across plasma membrane
Source: BHF-UCL
Inferred from direct assayⁱ
- 18075585
potassium ion transport
Source: RGD
Inferred from direct assayⁱ
- 12093728
- 16624992
regulation of blood pressure Source: Ensembl
regulation of cardiac muscle cell contraction
Source: RGD
Inferred from mutant phenotypeⁱ
- 15629895
regulation of sodium ion transport
Source: UniProtKB
Inferred from direct assayⁱ
- 17939993
regulation of the force of heart contraction Source: Ensembl
relaxation of cardiac muscle
Source: BHF-UCL
Traceable author statementⁱ
- 17442282
response to drug Source: Ensembl
response to glycoside Source: Ensembl
sodium ion export across plasma membrane
Source: BHF-UCL
Inferred from direct assayⁱ
- 18075585
sodium ion transport
Source: RGD
Inferred from direct assayⁱ

View the complete GO annotation on QuickGO ...

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	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 2

Organism-specific databases

Rat genome database More...RGDⁱ	2167 Atp1a1

RGDⁱ

2167 Atp1a1

Topology

Feature key	Position(s)	DescriptionActions	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, Membrane

Pathology & 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

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	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, Phosphoprotein

Proteomic databases

PaxDbⁱ	P06685
PRIDEⁱ	P06685

PTM databases

iPTMnetⁱ	P06685
PhosphoSitePlusⁱ	P06685

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSRNOG00000030019 Expressed in 10 organ(s), highest expression level in adult mammalian kidney
Genevisibleⁱ	P06685 RN

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
Inferred from physical interactionⁱ
- 8159688
chaperone binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 18768923
phosphatidylinositol 3-kinase binding
Source: RGD
Inferred from physical interactionⁱ
- 17728397
protein domain specific binding
Source: RGD
Inferred from physical interactionⁱ
- 16269407
protein kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17939993

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	246399, 10 interactors
ELMⁱ	P06685
IntActⁱ	P06685, 4 interactors
Molecular INTeraction database More...MINTⁱ	P06685
STRINGⁱ	10116.ENSRNOP00000045650

Chemistry databases

BindingDBⁱ

P06685

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	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

Show more details

3D structure databases

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 helix

Phylogenomic databases

eggNOGⁱ	KOG0203 Eukaryota COG0474 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00890000139334
HOVERGENⁱ	HBG004298
InParanoidⁱ	P06685
KEGG Orthology (KO) More...KOⁱ	K01539
OMAⁱ	ARIMPEQ
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G01BB
PhylomeDBⁱ	P06685

Family and domain databases

Conserved Domains Database More...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
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P06685-1 [UniParc]FASTA Add to basket

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        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

Length:1,023

Mass (Da):113,054

Last modified:January 1, 1988 - v1

Checksum:ⁱ85E98233EE6C18E9

Experimental Info

Feature key	Position(s)	DescriptionActions	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
NCBI Reference Sequences More...RefSeqⁱ	NP_036636.1, NM_012504.1
UniGeneⁱ	Rn.217534 Rn.2992

Genome annotation databases

Ensemblⁱ	ENSRNOT00000040430; ENSRNOP00000045650; ENSRNOG00000030019
GeneIDⁱ	24211
KEGGⁱ	rno:24211
UCSC genome browser More...UCSCⁱ	RGD:2167 rat

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P06685	Sodium/potassium-transporting ATPase subunit alpha-1		XENLA		1025	UniRef90_P06685
Sodium/potassium-transporting ATPase subunit alpha-1		HUMAN		1023
Sodium/potassium-transporting ATPase subunit alpha-1		MOUSE		1023
Sodium/potassium-transporting ATPase subunit alpha-1		PONAB		1023
Sodium/potassium-transporting ATPase subunit alpha-1		RABIT		1023
+426

Protein	Similar proteins		Species	Score	Length	Source
P06685	Sodium/potassium-transporting ATPase subunit alpha-1		XENLA		1025	UniRef50_P06685
Sodium/potassium-transporting ATPase subunit alpha-1		RHIMB		1023
Sodium/potassium-transporting ATPase subunit alpha-1		PONAB		1023
Sodium/potassium-transporting ATPase subunit alpha-1		MOUSE		1023
Sodium/potassium-transporting ATPase subunit alpha-1		HUMAN		1023
+1375

Cross-referencesⁱ

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

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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...

Protein-protein interaction databases

BioGridⁱ	246399, 10 interactors
ELMⁱ	P06685
IntActⁱ	P06685, 4 interactors
MINTⁱ	P06685
STRINGⁱ	10116.ENSRNOP00000045650

Chemistry databases

BindingDBⁱ	P06685
ChEMBLⁱ	CHEMBL3010

PTM databases

iPTMnetⁱ	P06685
PhosphoSitePlusⁱ	P06685

Proteomic databases

PaxDbⁱ	P06685
PRIDEⁱ	P06685

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSRNOT00000040430; ENSRNOP00000045650; ENSRNOG00000030019
GeneIDⁱ	24211
KEGGⁱ	rno:24211
UCSCⁱ	RGD:2167 rat

Organism-specific databases

CTDⁱ	476
RGDⁱ	2167 Atp1a1

Phylogenomic databases

eggNOGⁱ	KOG0203 Eukaryota COG0474 LUCA
GeneTreeⁱ	ENSGT00890000139334
HOVERGENⁱ	HBG004298
InParanoidⁱ	P06685
KOⁱ	K01539
OMAⁱ	ARIMPEQ
OrthoDBⁱ	EOG091G01BB
PhylomeDBⁱ	P06685

Enzyme and pathway databases

Reactomeⁱ	R-RNO-5578775 Ion homeostasis R-RNO-936837 Ion transport by P-type ATPases
SABIO-RKⁱ	P06685

Miscellaneous databases

EvolutionaryTraceⁱ	P06685
Protein Ontology More...PROⁱ	PR:P06685

Gene expression databases

Bgeeⁱ	ENSRNOG00000030019 Expressed in 10 organ(s), highest expression level in adult mammalian kidney
Genevisibleⁱ	P06685 RN

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
ProtoNetⁱ	Search...

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:	September 12, 2018
	This is version 193 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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Supporting data

UniProtKB - P06685 (AT1A1_RAT)

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Sodium/potassium-transporting ATPase subunit alpha-1

Atp1a1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Endoplasmic reticulum

Endosome

Golgi apparatus

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ