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Entry version 162 (16 Oct 2019)
Sequence version 1 (01 Jun 1998)
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Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

Gene

ATP2A2

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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 transcript 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 magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform SERCA2A is involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca2+ signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca (2+) signaling cascades that promote osteoclast differentiation and activation.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

Reversibly inhibited by phospholamban (PLN) at low calcium concentrations (By similarity). Inhibited by sarcolipin (SLN) and myoregulin (MRLN) (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 sitei514ATPBy similarity1
Binding sitei559ATPBy similarity1
Binding sitei677ATPBy similarity1
Binding sitei683ATPBy similarity1
Metal bindingi702MagnesiumBy similarity1
Binding sitei705ATPBy similarity1
Metal bindingi767Calcium 2By similarity1
Metal bindingi770Calcium 2By similarity1
Metal bindingi795Calcium 1By similarity1
Metal bindingi798Calcium 2By similarity1
Metal bindingi799Calcium 1By similarity1
Metal bindingi799Calcium 2By similarity1
Metal bindingi907Calcium 2By 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

GO - Biological processi

<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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CFA-418359 Reduction of cytosolic Ca++ levels
R-CFA-5578775 Ion homeostasis
R-CFA-936837 Ion transport by P-type ATPases

<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 2 (EC:7.2.2.10)
Short name:
SERCA2
Short name:
SR Ca(2+)-ATPase 2
Alternative name(s):
Calcium pump 2
Calcium-transporting ATPase sarcoplasmic reticulum type, slow 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:ATP2A2
<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>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
<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 identifieri9615 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
<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
  • UP000002254 <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: Chromosome 26

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:38254 ATP2A2

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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 – 756CytoplasmicCuratedAdd BLAST443
Transmembranei757 – 776Helical; Name=5By similarityAdd BLAST20
Topological domaini777 – 786LumenalCurated10
Transmembranei787 – 807Helical; Name=6By similarityAdd BLAST21
Topological domaini808 – 827CytoplasmicCuratedAdd BLAST20
Transmembranei828 – 850Helical; Name=7By similarityAdd BLAST23
Topological domaini851 – 896LumenalCuratedAdd BLAST46
Transmembranei897 – 916Helical; Name=8By similarityAdd BLAST20
Topological domaini917 – 929CytoplasmicCuratedAdd BLAST13
Transmembranei930 – 948Helical; Name=9By similarityAdd BLAST19
Topological domaini949 – 963LumenalCuratedAdd BLAST15
Transmembranei964 – 984Helical; Name=10By similarityAdd BLAST21
Topological domaini985 – 997CytoplasmicCuratedAdd BLAST13

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000461941 – 997Sarcoplasmic/endoplasmic reticulum calcium ATPase 2Add BLAST997

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 residuei38PhosphoserineBy similarity1
Modified residuei294Nitrated tyrosineBy similarity1
Modified residuei295Nitrated tyrosineBy similarity1
Modified residuei441PhosphothreonineBy similarity1
Modified residuei531PhosphoserineBy similarity1
Modified residuei580PhosphoserineBy similarity1
Modified residuei661PhosphoserineBy similarity1
Modified residuei663PhosphoserineBy similarity1
<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 bondi875 ↔ 887By similarity

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

Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity.By similarity

Keywords - PTMi

Disulfide bond, Nitration, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
O46674

PRoteomics IDEntifications database

More...
PRIDEi
O46674

<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

Isoform 1 is expressed in the heart.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSCAFG00000008434 Expressed in 3 organ(s), highest expression level in prefrontal cortex

<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) (By similarity).

Interacts with DWORF (By similarity).

Isoform 1 interacts with TRAM2 (via C-terminus).

Interacts with HAX1.

Interacts with S100A8 and S100A9 (By similarity).

Interacts with SLC35G1 and STIM1.

Interacts with TMEM203.

Interacts with TMEM64 and PDIA3 (By similarity).

By similarity

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
O46674, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9612.ENSCAFP00000025477

<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
O46674

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>Regioni575 – 594Interaction with HAX1By similarityAdd BLAST20
Regioni787 – 807Interaction with PLNBy similarityAdd BLAST21
Regioni788 – 997Interaction with TMEM64 and PDIA3By similarityAdd BLAST210
Regioni931 – 942Interaction 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 that is situated between the ATP2A2 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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0202 Eukaryota
COG0474 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159986

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000265621

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O46674

KEGG Orthology (KO)

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KOi
K05853

Identification of Orthologs from Complete Genome Data

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OMAi
DPPTPLW

Database of Orthologous Groups

More...
OrthoDBi
100699at2759

TreeFam database of animal gene trees

More...
TreeFami
TF300651

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
IPR030332 SERCA1/2

The PANTHER Classification System

More...
PANTHERi
PTHR42861:SF18 PTHR42861:SF18, 1 hit

Pfam protein domain database

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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

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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: O46674-1) [UniParc]FASTAAdd to basket
Also known as: ATP2A2A, SERCA2a

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL
60 70 80 90 100
ELVIEQFEDL LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA
110 120 130 140 150
NAIVGVWQER NAENAIEALK EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI
160 170 180 190 200
VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL TGESVSVIKH TDPVPDPRAV
210 220 230 240 250
NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV ATEQERTPLQ
260 270 280 290 300
QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV
310 320 330 340 350
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS
360 370 380 390 400
DKTGTLTTNQ MSVCRMFILD RVEGDSCSLN EFTITGSTYA PIGEVHKDDK
410 420 430 440 450
PVKCHQYDGL VELATICALC NDSALDYNEA KGVYEKVGEA TETALTCLVE
460 470 480 490 500
KMNVFDTELK GLSKIERANA CNSVIKQLMK KEFTLEFSRD RKSMSVYCTP
510 520 530 540 550
NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTPGV KQKVMSVIRE
560 570 580 590 600
WGSGSDTLRC LALATHDNPL RREEMNLEDS ANFIKYETNL TFVGCVGMLD
610 620 630 640 650
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK
660 670 680 690 700
AFTGREFDEL SPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT
710 720 730 740 750
GDGVNDAPAL KKSEIGIAMG SGTAVAKTAS EMVLADDNFS TIVAAVEEGR
760 770 780 790 800
AIYNNMKQFI RYLISSNVGE VVCIFLTAAL GFPEALIPVQ LLWVNLVTDG
810 820 830 840 850
LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG CYVGAATVGA
860 870 880 890 900
AAWWFIAADG GPRVSFYQLS HFLQCKDDNP DFEGVDCAIF ESPYPMTMAL
910 920 930 940 950
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE
960 970 980 990
PLPLIFQITP LNLTQWLMVL KISLPVILMD ETLKFVARNY LEPAILE
Length:997
Mass (Da):109,653
Last modified:June 1, 1998 - 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:i266770F599A9E3D3
GO
Isoform 2 (identifier: O46674-2)
Also known as: ATP2A2B, SERCA2b
Sequence is not available
Note: No experimental confirmation available.
Length:
Mass (Da):

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U94345 mRNA Translation: AAC02263.1

Protein sequence database of the Protein Information Resource

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PIRi
A24345

NCBI Reference Sequences

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RefSeqi
NP_001003214.1, NM_001003214.1 [O46674-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSCAFT00000027396; ENSCAFP00000025477; ENSCAFG00000008434 [O46674-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
403878

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cfa:403878

Keywords - Coding sequence diversityi

Alternative splicing

<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
U94345 mRNA Translation: AAC02263.1
PIRiA24345
RefSeqiNP_001003214.1, NM_001003214.1 [O46674-1]

3D structure databases

SMRiO46674
ModBaseiSearch...

Protein-protein interaction databases

IntActiO46674, 1 interactor
STRINGi9612.ENSCAFP00000025477

Proteomic databases

PaxDbiO46674
PRIDEiO46674

Genome annotation databases

EnsembliENSCAFT00000027396; ENSCAFP00000025477; ENSCAFG00000008434 [O46674-1]
GeneIDi403878
KEGGicfa:403878

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
488
VGNCiVGNC:38254 ATP2A2

Phylogenomic databases

eggNOGiKOG0202 Eukaryota
COG0474 LUCA
GeneTreeiENSGT00940000159986
HOGENOMiHOG000265621
InParanoidiO46674
KOiK05853
OMAiDPPTPLW
OrthoDBi100699at2759
TreeFamiTF300651

Enzyme and pathway databases

ReactomeiR-CFA-418359 Reduction of cytosolic Ca++ levels
R-CFA-5578775 Ion homeostasis
R-CFA-936837 Ion transport by P-type ATPases

Gene expression databases

BgeeiENSCAFG00000008434 Expressed in 3 organ(s), highest expression level in prefrontal cortex

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
IPR030332 SERCA1/2
PANTHERiPTHR42861:SF18 PTHR42861:SF18, 1 hit
PfamiView protein in Pfam
PF00689 Cation_ATPase_C, 1 hit
PF00690 Cation_ATPase_N, 1 hit
PRINTSiPR00120 HATPASE
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiAT2A2_CANLF
<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: O46674
<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: June 1, 1998
Last modified: October 16, 2019
This is version 162 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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