Atp1a1

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

Complete GO annotation...

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
- 16624992
- 12093728
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 from cell
Source: BHF-UCL
Inferred from direct assayⁱ
- 18075585
sodium ion transport
Source: RGD
Inferred from direct assayⁱ

Complete GO annotation...

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.

Subcellular locationⁱ

Cell membrane
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P05023 (AT1A1_HUMAN)
; Multi-pass membrane protein Sequence analysis

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

GO - Cellular componentⁱ

apical plasma membrane Source: Ensembl
basolateral plasma membrane Source: Ensembl
caveola
Source: RGD
Inferred from direct assayⁱ
- 16624992
endoplasmic reticulum
Source: BHF-UCL
Inferred from direct assayⁱ
- 18768923
endosome
Source: RGD
Inferred from direct assayⁱ
- 16893515
extracellular exosome Source: Ensembl
Golgi apparatus
Source: BHF-UCL
Inferred from direct assayⁱ
- 18768923
integral component of membrane Source: UniProtKB
intercalated disc
Source: BHF-UCL
Inferred from direct assayⁱ
- 17442282
membrane
Source: RGD
Inferred from direct assayⁱ
- 16893515
membrane raft
Source: RGD
Inferred from direct assayⁱ
- 18178552
myelin sheath Source: Ensembl
plasma membrane
Source: BHF-UCL
Inferred from direct assayⁱ
- 18768923
postsynaptic density Source: Ensembl
protein complex Source: Ensembl
sarcolemma
Source: BHF-UCL
Inferred from direct assayⁱ
- 17442282
sodium:potassium-exchanging ATPase complex
Source: RGD
Inferred from direct assayⁱ
T-tubule
Source: BHF-UCL
Inferred from direct assayⁱ
- 17442282

Complete GO annotation...

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.
Genevisibleⁱ	P06685. RN.

Interactionⁱ

Subunit structureⁱ

Interacts with SLC35G1 and STIM1 (By similarity). Composed of three subunits: alpha (catalytic), beta and gamma. Interacts with SIK1.By similarity2 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

Complete GO annotation...

Protein-protein interaction databases

BioGridⁱ	246399. 10 interactors.
IntActⁱ	P06685. 2 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-3089277.
STRINGⁱ	10116.ENSRNOP00000045650.

Chemistry databases

BindingDBⁱ

P06685.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

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

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...

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	ENSGT00880000137885.
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

Gene3Dⁱ	3.40.1110.10. 1 hit.
InterProⁱ	View protein in InterPro IPR006068. 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.
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

« Hide

        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

GO

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.

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.
NCBI Reference Sequences More...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.
IntActⁱ	P06685. 2 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-3089277.
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.
UCSC genome browser More...UCSCⁱ	RGD:2167. rat.

Organism-specific databases

CTDⁱ	476.
Rat genome database More...RGDⁱ	2167. Atp1a1.

Phylogenomic databases

eggNOGⁱ	KOG0203. Eukaryota. COG0474. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00880000137885.
HOVERGENⁱ	HBG004298.
InParanoidⁱ	P06685.
KEGG Orthology (KO) More...KOⁱ	K01539.
OMAⁱ	ARIMPEQ.
Database of Orthologous Groups More...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.
Genevisibleⁱ	P06685. RN.

Family and domain databases

Gene3Dⁱ	3.40.1110.10. 1 hit.
InterProⁱ	View protein in InterPro IPR006068. 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.
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.
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:	June 7, 2017
	This is version 183 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P06685 (AT1A1_RAT)

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Sodium/potassium-transporting ATPase subunit alpha-1

Select a section on the left to see content.

<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

<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 - 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

Topology

<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 - 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

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

<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

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

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ