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UniProtKB - P11607 (AT2A2_PIG)

Entry version 181 (25 May 2022)
Sequence version 1 (01 Oct 1989)
Previous versions | rss
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Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

Gene

ATP2A2

Organism
Sus scrofa (Pig)
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 magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation. Also modulates ER contacts with lipid droplets, mitochondria and endosomes.

By similarity

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 Ca2+ spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca2+ signaling cascades that promote osteoclast differentiation and activation.

By similarity

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Has different conformational states with differential Ca2+ affinity. The E1 conformational state (active form) shows high Ca2+ affinity, while the E2 state exhibits low Ca2+ affinity. Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. Inhibited by sarcolipin (SLN) and myoregulin (MRLN). The inhibition is blocked by VMP1 (By similarity). Enhanced by DWORF; DWORF increases activity by displacing sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By similarity). Stabilizes SERCA2 in its E2 state (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi304Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi305Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi307Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi309Calcium 1Combined sources1 Publication1
<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 sitei3514-aspartylphosphate intermediateBy similarity1
Metal bindingi351MagnesiumCombined sources1 Publication1
Metal bindingi353Magnesium; via carbonyl oxygenCombined sources1 Publication1
<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 sitei353ATPCombined sources1 Publication1
Binding sitei442ATPCombined sources1 Publication1
Binding sitei489ATPCombined sources1 Publication1
Binding sitei514ATPCombined sources1 Publication1
Binding sitei559ATPBy similarity1
Binding sitei677ATPCombined sources1 Publication1
Binding sitei683ATPBy similarity1
Metal bindingi702MagnesiumCombined sources1 Publication1
Binding sitei705ATPCombined sources1 Publication1
Metal bindingi767Calcium 2Combined sources1 Publication1
Metal bindingi770Calcium 2Combined sources1 Publication1
Metal bindingi795Calcium 1Combined sources1 Publication1
Metal bindingi798Calcium 2Combined sources1 Publication1
Metal bindingi799Calcium 1Combined sources1 Publication1
Metal bindingi799Calcium 2Combined sources1 Publication1
Metal bindingi907Calcium 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi624 – 626ATPCombined sources1 Publication3

<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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SSC-418359, Reduction of cytosolic Ca++ levels
R-SSC-5578775, Ion homeostasis
R-SSC-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%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:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (EC:7.2.2.101 Publication)
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%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:ATP2A2
<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>OrganismiSus scrofa (Pig)
<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 identifieri9823 [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 › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus
<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
  • UP000314985 <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 14
  • UP000008227 Componenti: Chromosome 14

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...VGNCi		VGNC:85647, 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

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 domaini1 – 48CytoplasmicCuratedAdd BLAST48
<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>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 – 1042CytoplasmicCuratedAdd BLAST58

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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000461981 – 1042Sarcoplasmic/endoplasmic reticulum calcium ATPase 2Add BLAST1042

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 residuei2943'-nitrotyrosineBy similarity1
Modified residuei2953'-nitrotyrosineBy similarity1
Modified residuei441PhosphothreonineBy similarity1
Modified residuei531PhosphoserineBy similarity1
Modified residuei580PhosphoserineBy 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 ↔ 887Combined sources1 Publication

<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

Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity.By similarity
Serotonylated on Gln residues by TGM2 in response to hypoxia, leading to its inactivation.By similarity

Keywords - PTMi

Disulfide bond, Nitration, Phosphoprotein

Proteomic databases

PeptideAtlas

More...PeptideAtlasi		P11607

PRoteomics IDEntifications database

More...PRIDEi		P11607

<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

Detected in heart left ventricle (at protein level) (PubMed:30777856). Isoform 2 is highly expressed in heart and slow twitch skeletal muscle. Isoform 1 is widely expressed.2 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P11607, baseline and differential

<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

Interacts with sarcolipin (SLN); the interaction inhibits ATP2A2 Ca2+ affinity.

Interacts with phospholamban (PLN); the interaction inhibits ATP2A2 Ca2+ affinity (By similarity).

Interacts with myoregulin (MRLN) (By similarity).

Interacts with DWORF (By similarity).

Interacts with HAX1 (By similarity).

Interacts with S100A8 and S100A9 (By similarity).

Interacts with SLC35G1 and STIM1.

Interacts with TMEM203 (By similarity).

Interacts with TMEM64 and PDIA3 (By similarity).

Interacts with TMX2 (By similarity).

Interacts with VMP1; VMP1 competes with PLN and SLN to prevent them from forming an inhibitory complex with ATP2A2.

Interacts with ULK1 (By similarity).

Interacts with S100A1 in a Ca2+-dependent manner (By similarity).

Interacts with TUNAR (By similarity).

By similarity

Interacts with TRAM2 (via C-terminus).

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		1149018, 1 interactor

Protein interaction database and analysis system

More...IntActi		P11607, 2 interactors

Molecular INTeraction database

More...MINTi		P11607

STRING: functional protein association networks

More...STRINGi		9823.ENSSSCP00000019348

<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

11042
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P11607

Biological Magnetic Resonance Data Bank

More...BMRBi		P11607

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

More...SMRi		P11607

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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 – 1042Interaction with TMEM64 and PDIA3By similarityAdd BLAST255
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

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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159986

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P11607

Identification of Orthologs from Complete Genome Data

More...OMAi		PLWNNMM

Database of Orthologous Groups

More...OrthoDBi		100699at2759

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, 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>Sequences (2+)i

<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.

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

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P11607-1) [UniParc]FASTAAdd to basket
Also known as: ATP2A2B, SERCA2b

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><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 KVEGDTCSLN 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 KQKIMSVIRE 
       560        570        580        590        600
WGSGSDTLRC LALATHDNPM RREEMNLEDS ANFIKYETNL TFVGCVGMLD 
       610        620        630        640        650
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK 
       660        670        680        690        700
AFTGREFDEL NPSAQREACL 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 GPRVTFYQLS HFLQCKEDNP DFEGVDCAVF ESPYPMTMAL 
       910        920        930        940        950
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE 
       960        970        980        990       1000
PLPLIFQITP LNLTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP 
      1010       1020       1030       1040 
ATKSCSFSAC TDGISWPFVL LIMPLVIWVY STDTNFSDMF WS
Length:1,042
Mass (Da):114,792
Last modified:October 1, 1989 - 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:iA68EC9E41494D532
GO
Isoform 2 (identifier: P11607-2) [UniParc]FASTAAdd to basket
Also known as: ATP2A2A, SERCA2a

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → AILE

Show »
Length:997
Mass (Da):109,726
Checksum:i66697619E312CA3E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A5S6HET4A0A5S6HET4_PIG
Calcium-transporting ATPase
ATP2A2
1,007Annotation score:

Annotation score:3 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>
A0A5S6HSJ6A0A5S6HSJ6_PIG
Calcium-transporting ATPase
ATP2A2
1,005Annotation score:

Annotation score:3 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>

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_000360994 – 1042GKECV…DMFWS → AILE in isoform 2. 1 PublicationAdd BLAST49

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
X15074 mRNA Translation: CAA33170.1
X15073 mRNA Translation: CAA33169.1
X53754 Genomic DNA Translation: CAA37783.1
X53754 Genomic DNA Translation: CAA37784.1

Protein sequence database of the Protein Information Resource

More...PIRi		S04651
S04652

NCBI Reference Sequences

More...RefSeqi		NP_999030.1, NM_213865.1 [P11607-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSSSCT00000045994; ENSSSCP00000037774; ENSSSCG00000034386 [P11607-1]
ENSSSCT00015008195; ENSSSCP00015003301; ENSSSCG00015006148 [P11607-1]
ENSSSCT00025020640; ENSSSCP00025008478; ENSSSCG00025015273 [P11607-1]
ENSSSCT00030063269; ENSSSCP00030028946; ENSSSCG00030045278 [P11607-1]
ENSSSCT00035043363; ENSSSCP00035017345; ENSSSCG00035032729 [P11607-1]
ENSSSCT00040006183; ENSSSCP00040002459; ENSSSCG00040004634 [P11607-1]
ENSSSCT00045030557; ENSSSCP00045021173; ENSSSCG00045017876 [P11607-1]
ENSSSCT00055035587; ENSSSCP00055028270; ENSSSCG00055017945 [P11607-1]
ENSSSCT00060108150; ENSSSCP00060048139; ENSSSCG00060078303 [P11607-1]
ENSSSCT00065011829; ENSSSCP00065004850; ENSSSCG00065008853 [P11607-1]
ENSSSCT00070027936; ENSSSCP00070023256; ENSSSCG00070014188 [P11607-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		396875

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ssc:396875

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
X15074 mRNA Translation: CAA33170.1
X15073 mRNA Translation: CAA33169.1
X53754 Genomic DNA Translation: CAA37783.1
X53754 Genomic DNA Translation: CAA37784.1
PIRiS04651
S04652
RefSeqiNP_999030.1, NM_213865.1 [P11607-1]

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
5MPMX-ray3.30A1-993[»]
6HXBX-ray4.00A1-993[»]
AlphaFoldDBiP11607
BMRBiP11607
SMRiP11607
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi1149018, 1 interactor
IntActiP11607, 2 interactors
MINTiP11607
STRINGi9823.ENSSSCP00000019348

Proteomic databases

PeptideAtlasiP11607
PRIDEiP11607

Genome annotation databases

EnsembliENSSSCT00000045994; ENSSSCP00000037774; ENSSSCG00000034386 [P11607-1]
ENSSSCT00015008195; ENSSSCP00015003301; ENSSSCG00015006148 [P11607-1]
ENSSSCT00025020640; ENSSSCP00025008478; ENSSSCG00025015273 [P11607-1]
ENSSSCT00030063269; ENSSSCP00030028946; ENSSSCG00030045278 [P11607-1]
ENSSSCT00035043363; ENSSSCP00035017345; ENSSSCG00035032729 [P11607-1]
ENSSSCT00040006183; ENSSSCP00040002459; ENSSSCG00040004634 [P11607-1]
ENSSSCT00045030557; ENSSSCP00045021173; ENSSSCG00045017876 [P11607-1]
ENSSSCT00055035587; ENSSSCP00055028270; ENSSSCG00055017945 [P11607-1]
ENSSSCT00060108150; ENSSSCP00060048139; ENSSSCG00060078303 [P11607-1]
ENSSSCT00065011829; ENSSSCP00065004850; ENSSSCG00065008853 [P11607-1]
ENSSSCT00070027936; ENSSSCP00070023256; ENSSSCG00070014188 [P11607-1]
GeneIDi396875
KEGGissc:396875

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		488
VGNCiVGNC:85647, ATP2A2

Phylogenomic databases

GeneTreeiENSGT00940000159986
InParanoidiP11607
OMAiPLWNNMM
OrthoDBi100699at2759

Enzyme and pathway databases

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

Gene expression databases

ExpressionAtlasiP11607, baseline and differential

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, 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 nameiAT2A2_PIG
<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: P11607
Secondary accession number(s): P11606, P79426, P79427
<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: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 25, 2022
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

3D-structure, 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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