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UniProtKB - P06685 (AT1A1_RAT)

Entry version 215 (23 Feb 2022)
Sequence version 1 (01 Jan 1988)
Previous versions | rss
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Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

Atp1a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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.

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei3764-aspartylphosphate intermediateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei487ATP1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi717MagnesiumBy similarity1
Metal bindingi721MagnesiumBy similarity1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTranslocase
Biological processIon transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Sodium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-5578775, Ion homeostasis
R-RNO-936837, Ion transport by P-type ATPases

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P06685

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Sodium/potassium-transporting ATPase subunit alpha-1 (EC:7.2.2.132 Publications)
Short name:
Na(+)/K(+) ATPase alpha-1 subunit
Alternative name(s):
Sodium pump subunit alpha-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Atp1a1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Rat genome database

More...RGDi		2167, Atp1a1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini6 – 87CytoplasmicSequence analysisAdd BLAST82
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei88 – 108HelicalSequence analysisAdd BLAST21
Topological domaini109 – 131ExtracellularSequence analysisAdd BLAST23
Transmembranei132 – 152HelicalSequence analysisAdd BLAST21
Topological domaini153 – 288CytoplasmicSequence analysisAdd BLAST136
Transmembranei289 – 308HelicalSequence analysisAdd BLAST20
Topological domaini309 – 320ExtracellularSequence analysisAdd BLAST12
Transmembranei321 – 338HelicalSequence analysisAdd BLAST18
Topological domaini339 – 772CytoplasmicSequence analysisAdd BLAST434
Transmembranei773 – 792HelicalSequence analysisAdd BLAST20
Topological domaini793 – 802ExtracellularSequence analysis10
Transmembranei803 – 823HelicalSequence analysisAdd BLAST21
Topological domaini824 – 843CytoplasmicSequence analysisAdd BLAST20
Transmembranei844 – 866HelicalSequence analysisAdd BLAST23
Topological domaini867 – 918ExtracellularSequence analysisAdd BLAST52
Transmembranei919 – 938HelicalSequence analysisAdd BLAST20
Topological domaini939 – 951CytoplasmicSequence analysisAdd BLAST13
Transmembranei952 – 970HelicalSequence analysisAdd BLAST19
Topological domaini971 – 985ExtracellularSequence analysisAdd BLAST15
Transmembranei986 – 1006HelicalSequence analysisAdd BLAST21
Topological domaini1007 – 1023CytoplasmicSequence analysisAdd BLAST17

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi16S → A: Dopamine fails to increase phosphoinositide-3 kinase activity and to promote its interaction with Na(+)/K(+) ATPase. 1 Publication1
Mutagenesisi83P → R: Dopamine fails to increase phosphoinositide-3 kinase activity and to promote its interaction with Na(+)/K(+) ATPase. 1 Publication1
Mutagenesisi302L → R: Results in altered sodium and potassium transport. 1 Publication1
Mutagenesisi303G → R: Results in altered sodium and potassium transport. 1 Publication1
Mutagenesisi314E → K: Abolishes targeting to the basolateral plasma membrane. 1 Publication1
Mutagenesisi859M → R: Results in altered sodium and potassium transport. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3010

DrugCentral

More...DrugCentrali		P06685

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000024891 – 51 Publication5
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000024906 – 1023Sodium/potassium-transporting ATPase subunit alpha-1Add BLAST1018

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei9N6-acetyllysineBy similarity1
Modified residuei10Phosphotyrosine1 Publication1
Modified residuei16Phosphoserine; by PKC1 Publication1
Modified residuei21N6-acetyllysineBy similarity1
Modified residuei23Phosphoserine; by PKC2 Publications1
Modified residuei40PhosphoserineCombined sources1
Modified residuei47PhosphoserineCombined sources1
Modified residuei228PhosphoserineCombined sources1
Modified residuei260PhosphotyrosineBy similarity1
Modified residuei452PhosphoserineCombined sources1
Modified residuei484PhosphoserineCombined sources1
Modified residuei542PhosphotyrosineBy similarity1
Modified residuei661N6-succinyllysineBy similarity1
Modified residuei668PhosphoserineBy similarity1
Modified residuei675PhosphoserineBy similarity1
Modified residuei943Phosphoserine; by PKA1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P06685

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P06685

PRoteomics IDEntifications database

More...PRIDEi		P06685

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P06685

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P06685

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the central nervous system, in most motor and sensory axons of the ventral and dorsal roots, as well as in the large motor neurons of the ventral horn (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000030019, Expressed in adult mammalian kidney and 20 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P06685, RN

<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>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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).

Interacts with CLN3; this interaction regulates the sodium/potassium-transporting ATPase complex localization at the plasma membrane (By similarity).

By similarity5 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		246399, 18 interactors

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P06685

Protein interaction database and analysis system

More...IntActi		P06685, 7 interactors

Molecular INTeraction database

More...MINTi		P06685

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000045650

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P06685

<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

11023
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P06685

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P06685

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P06685

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 38DisorderedSequence analysisAdd BLAST38
Regioni82 – 84Phosphoinositide-3 kinase binding3
Regioni216 – 235DisorderedSequence analysisAdd BLAST20

<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

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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0203, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154840

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_002360_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06685

Identification of Orthologs from Complete Genome Data

More...OMAi		FINLVTD

Database of Orthologous Groups

More...OrthoDBi		100699at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P06685

Family and domain databases

Conserved Domains Database

More...CDDi		cd02608, P-type_ATPase_Na-K_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.1110.10, 1 hit
3.40.50.1000, 1 hit

Integrated resource of protein families, domains and functional sites

More...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
IPR044492, P_typ_ATPase_HD_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00689, Cation_ATPase_C, 1 hit
PF00690, Cation_ATPase_N, 1 hit

Structure-Function Linkage Database

More...SFLDi		SFLDF00027, p-type_atpase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00831, Cation_ATPase_N, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56784, SSF56784, 1 hit
SSF81653, SSF81653, 1 hit
SSF81660, SSF81660, 1 hit
SSF81665, SSF81665, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01106, ATPase-IIC_X-K, 1 hit
TIGR01494, ATPase_P-type, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00154, ATPASE_E1_E2, 1 hit

<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 <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P06685-1 [UniParc]FASTAAdd 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i85E98233EE6C18E9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti68 – 69AA → PV in AAA41671 (PubMed:2822726).Curated2
Sequence conflicti175G → E in AAA41671 (PubMed:2822726).Curated1
Sequence conflicti188G → V in AAA41671 (PubMed:2822726).Curated1
Sequence conflicti335G → V in AAA41671 (PubMed:2822726).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

Protein sequence database of the Protein Information Resource

More...PIRi		A24639

NCBI Reference Sequences

More...RefSeqi		NP_036636.1, NM_012504.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000040430; ENSRNOP00000045650; ENSRNOG00000030019

Database of genes from NCBI RefSeq genomes

More...GeneIDi		24211

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:24211

UCSC genome browser

More...UCSCi		RGD:2167, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

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
PIRiA24639
RefSeqiNP_036636.1, NM_012504.1

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 entryMethodResolution (Å)ChainPositionsPDBsum
1MO7NMR-A386-595[»]
1MO8NMR-A386-595[»]
BMRBiP06685
SMRiP06685
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi246399, 18 interactors
ELMiP06685
IntActiP06685, 7 interactors
MINTiP06685
STRINGi10116.ENSRNOP00000045650

Chemistry databases

BindingDBiP06685
ChEMBLiCHEMBL3010
DrugCentraliP06685

PTM databases

iPTMnetiP06685
PhosphoSitePlusiP06685

Proteomic databases

jPOSTiP06685
PaxDbiP06685
PRIDEiP06685

Genome annotation databases

EnsembliENSRNOT00000040430; ENSRNOP00000045650; ENSRNOG00000030019
GeneIDi24211
KEGGirno:24211
UCSCiRGD:2167, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		476
RGDi2167, Atp1a1

Phylogenomic databases

eggNOGiKOG0203, Eukaryota
GeneTreeiENSGT00940000154840
HOGENOMiCLU_002360_3_0_1
InParanoidiP06685
OMAiFINLVTD
OrthoDBi100699at2759
PhylomeDBiP06685

Enzyme and pathway databases

ReactomeiR-RNO-5578775, Ion homeostasis
R-RNO-936837, Ion transport by P-type ATPases
SABIO-RKiP06685

Miscellaneous databases

EvolutionaryTraceiP06685

Protein Ontology

More...PROi		PR:P06685

Gene expression databases

BgeeiENSRNOG00000030019, Expressed in adult mammalian kidney and 20 other tissues
GenevisibleiP06685, RN

Family and domain databases

CDDicd02608, P-type_ATPase_Na-K_like, 1 hit
Gene3Di3.40.1110.10, 1 hit
3.40.50.1000, 1 hit
InterProiView 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
IPR044492, P_typ_ATPase_HD_dom
PfamiView protein in Pfam
PF00689, Cation_ATPase_C, 1 hit
PF00690, Cation_ATPase_N, 1 hit
SFLDiSFLDF00027, p-type_atpase, 1 hit
SMARTiView protein in SMART
SM00831, Cation_ATPase_N, 1 hit
SUPFAMiSSF56784, SSF56784, 1 hit
SSF81653, SSF81653, 1 hit
SSF81660, SSF81660, 1 hit
SSF81665, SSF81665, 1 hit
TIGRFAMsiTIGR01106, ATPase-IIC_X-K, 1 hit
TIGR01494, ATPase_P-type, 2 hits
PROSITEiView protein in PROSITE
PS00154, ATPASE_E1_E2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAT1A1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06685
Secondary accession number(s): Q64609
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: February 23, 2022
This is version 215 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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