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UniProtKB - Q64578 (AT2A1_RAT)

Entry version 181 (29 Sep 2021)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
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Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Gene

Atp2a1

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

Key regulator of striated muscle performance by acting as the major Ca2+ ATPase responsible for the reuptake of cytosolic Ca2+ into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By similarity). Reversibly inhibited by phospholamban (PLN) at low calcium concentrations (By similarity). Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN (By similarity). Enhanced by DWORF; DWORF increases activity by displacing sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi304Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi305Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi307Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi309Calcium 1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei3514-aspartylphosphate intermediateBy similarity1
Metal bindingi351MagnesiumBy similarity1
Metal bindingi353Magnesium; via carbonyl oxygenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei353ATPBy similarity1
Binding sitei442ATPBy similarity1
Binding sitei489ATPBy similarity1
Binding sitei515ATPBy similarity1
Binding sitei560ATPBy similarity1
Binding sitei678ATPBy similarity1
Binding sitei684ATPBy similarity1
Metal bindingi703MagnesiumBy similarity1
Binding sitei706ATPBy similarity1
Metal bindingi768Calcium 2By similarity1
Metal bindingi771Calcium 2By similarity1
Metal bindingi796Calcium 1By similarity1
Metal bindingi799Calcium 2By similarity1
Metal bindingi800Calcium 1By similarity1
Metal bindingi800Calcium 2By similarity1
Metal bindingi908Calcium 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi625 – 627ATPBy similarity3

<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 processCalcium transport, Ion transport, Transport
LigandATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

<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_and_taxonomy_section">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:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (EC:7.2.2.10By similarity)
Short name:
SERCA1
Short name:
SR Ca(2+)-ATPase 1
Alternative name(s):
Calcium pump 1
Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
Endoplasmic reticulum class 1/2 Ca(2+) ATPase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Atp2a1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		621293, Atp2a1

<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_location_section">'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 domaini1 – 48CytoplasmicCuratedAdd BLAST48
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei49 – 69Helical; Name=1By similarityAdd BLAST21
Topological domaini70 – 89LumenalCuratedAdd BLAST20
Transmembranei90 – 110Helical; Name=2By similarityAdd BLAST21
Topological domaini111 – 253CytoplasmicCuratedAdd BLAST143
Transmembranei254 – 273Helical; Name=3By similarityAdd BLAST20
Topological domaini274 – 295LumenalCuratedAdd BLAST22
Transmembranei296 – 313Helical; Name=4By similarityAdd BLAST18
Topological domaini314 – 757CytoplasmicCuratedAdd BLAST444
Transmembranei758 – 777Helical; Name=5By similarityAdd BLAST20
Topological domaini778 – 787LumenalCurated10
Transmembranei788 – 808Helical; Name=6By similarityAdd BLAST21
Topological domaini809 – 828CytoplasmicCuratedAdd BLAST20
Transmembranei829 – 851Helical; Name=7By similarityAdd BLAST23
Topological domaini852 – 897LumenalCuratedAdd BLAST46
Transmembranei898 – 917Helical; Name=8By similarityAdd BLAST20
Topological domaini918 – 930CytoplasmicCuratedAdd BLAST13
Transmembranei931 – 949Helical; Name=9By similarityAdd BLAST19
Topological domaini950 – 964LumenalCuratedAdd BLAST15
Transmembranei965 – 985Helical; Name=10By similarityAdd BLAST21
Topological domaini986 – 994CytoplasmicCurated9

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3585236

DrugCentral

More...DrugCentrali		Q64578

<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 '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_00000461901 – 994Sarcoplasmic/endoplasmic reticulum calcium ATPase 1Add BLAST994

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 residuei441PhosphothreonineCombined sources1
Modified residuei569PhosphothreonineCombined sources1
Modified residuei581PhosphoserineCombined sources1
Modified residuei643PhosphoserineCombined sources1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi876 ↔ 888By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q64578

PRoteomics IDEntifications database

More...PRIDEi		Q64578

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q64578

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

More...PhosphoSitePlusi		Q64578

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q64578

<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

Skeletal muscle, fast twitch muscle (type II) fibers.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Increased contractile activity leads to a decrease in SERCA1 expression, while decreased contractile activity leads to an increase in SERCA1 expression.1 Publication

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with sarcolipin (SLN) (By similarity).

Interacts with phospholamban (PLN) (By similarity).

Interacts with myoregulin (MRLN).

Interacts with DWORF (By similarity). Interacts VMP1 (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		250515, 1 interactor

Protein interaction database and analysis system

More...IntActi		Q64578, 1 interactor

Molecular INTeraction database

More...MINTi		Q64578

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000067246

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q64578

<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

3D structure databases

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

More...SMRi		Q64578

Database of comparative protein structure models

More...ModBasei		Search...

<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>Regioni788 – 808Interaction with PLNBy similarityAdd BLAST21
Regioni932 – 943Interaction with PLNBy similarityAdd BLAST12

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Ca2+ and ATP binding cause major rearrangements of the cytoplasmic and transmembrane domains. According to the E1-E2 model, Ca2+ binding to the cytosolic domain of the pump in the high-affinity E1 conformation is followed by the ATP-dependent phosphorylation of the active site Asp, giving rise to E1P. A conformational change of the phosphoenzyme gives rise to the low-affinity E2P state that exposes the Ca2+ ions to the lumenal side and promotes Ca2+ release. Dephosphorylation of the active site Asp mediates the subsequent return to the E1 conformation.By similarity
PLN and SLN both have a single transmembrane helix; both occupy a similar binding site on ATP2A1 that is situated between the ATP2A1 transmembrane helices.By similarity

<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 IIA subfamily. [View classification]Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0202, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q64578

Identification of Orthologs from Complete Genome Data

More...OMAi		DPPTPLW

Database of Orthologous Groups

More...OrthoDBi		100699at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q64578

Family and domain databases

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
IPR005782, P-type_ATPase_IIA
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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00120, HATPASE

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		TIGR01116, ATPase-IIA1_Ca, 1 hit
TIGR01494, ATPase_P-type, 3 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q64578-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEAAHSKSTE ECLSYFGVSE TTGLTPDQVK RHLEKYGPNE LPAEEGKSLW 
        60         70         80         90        100
ELVVEQFEDL LVRILLLAAC ISFVLAWFEE GEETVTAFVE PFVILLILIA 
       110        120        130        140        150
NAIVGVWQER NAENAIEALK EYEPEMGKVY RADRKSVQRI KARDIVPGDI 
       160        170        180        190        200
VEVAVGDKVP ADIRILSIKS TTLRVDQSIL TGESVSVIKH TDPVPDPRAV 
       210        220        230        240        250
NQDKKNMLFS GTNIAAGKAV GIVATTGVST EIGKIRDQMA ATEQDKTPLQ 
       260        270        280        290        300
QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWFR GAIYYFKIAV 
       310        320        330        340        350
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS 
       360        370        380        390        400
DKTGTLTTNQ MSVCKMFIID KVDGDICSLN EFSITGSTYA PEGEVLKNDK 
       410        420        430        440        450
PVRAGQYDGL VELATICALC NDSSLDFNET KGVYEKVGEA TETALTTLVE 
       460        470        480        490        500
KMNVFNTEVR SLSKVERANA CNSVIRQLMK KEFTLEFSRD RKSMSVYCSP 
       510        520        530        540        550
AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPLTGP VKEKIMSVIK 
       560        570        580        590        600
EWGTGRDTLR CLALATRDTP PKREEMVLDD SAKFMEYEMD LTFVGVVGML 
       610        620        630        640        650
DPPRKEVTGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFSENEEVAD 
       660        670        680        690        700
RAYTGREFDD LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM 
       710        720        730        740        750
TGDGVNDAPA LKKAEIGIAM GSGTAVAKTA SEMVLADDNF STIVAAVEEG 
       760        770        780        790        800
RAIYNNMKQF IRYLISSNVG EVVCIFLTAA LGLPEALIPV QLLWVNLVTD 
       810        820        830        840        850
GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI GGYVGAATVG 
       860        870        880        890        900
AAAWWFLYAE DGPHVSYHQL THFMQCTEHN PEFDGLDCEV FEAPEPMTMA 
       910        920        930        940        950
LSVLVTIEMC NALNSLSENQ SLLRMPPWVN IWLLGSICLS MSLHFLILYV 
       960        970        980        990 
DPLPMIFKLR ALDFTQWLMV LKISLPVIGL DELLKFIARN YLEG
Length:994
Mass (Da):109,409
Last modified:November 1, 1996 - 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:i899F91AD8038A47A
GO

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
M99223 mRNA Translation: AAA40991.1
AF091853 Genomic DNA Translation: AAD17802.1
AF091852 Genomic DNA Translation: AAD17801.1

Protein sequence database of the Protein Information Resource

More...PIRi		A48849

NCBI Reference Sequences

More...RefSeqi		NP_478120.1, NM_058213.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		116601

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:116601

<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
M99223 mRNA Translation: AAA40991.1
AF091853 Genomic DNA Translation: AAD17802.1
AF091852 Genomic DNA Translation: AAD17801.1
PIRiA48849
RefSeqiNP_478120.1, NM_058213.1

3D structure databases

SMRiQ64578
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi250515, 1 interactor
IntActiQ64578, 1 interactor
MINTiQ64578
STRINGi10116.ENSRNOP00000067246

Chemistry databases

BindingDBiQ64578
ChEMBLiCHEMBL3585236
DrugCentraliQ64578

PTM databases

iPTMnetiQ64578
PhosphoSitePlusiQ64578
SwissPalmiQ64578

Proteomic databases

jPOSTiQ64578
PRIDEiQ64578

Genome annotation databases

GeneIDi116601
KEGGirno:116601

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		487
RGDi621293, Atp2a1

Phylogenomic databases

eggNOGiKOG0202, Eukaryota
InParanoidiQ64578
OMAiDPPTPLW
OrthoDBi100699at2759
PhylomeDBiQ64578

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q64578

Family and domain databases

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
IPR005782, P-type_ATPase_IIA
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
PRINTSiPR00120, HATPASE
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
TIGRFAMsiTIGR01116, ATPase-IIA1_Ca, 1 hit
TIGR01494, ATPase_P-type, 3 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 nameiAT2A1_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: Q64578
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: September 29, 2021
This is version 181 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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