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UniProtKB - Q5R8A5 (PA24A_PONAB)

Entry version 76 (02 Dec 2020)
Sequence version 1 (21 Dec 2004)
Previous versions | rss
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Protein

Cytosolic phospholipase A2

Gene

PLA2G4A

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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

Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity).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

Activated by cytosolic calcium, which is necessary for binding to membrane lipids. Activated by phosphorylation in response to mitogenic stimuli.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycerophospholipid metabolism

This protein is involved in the pathway glycerophospholipid metabolism, which is part of Membrane lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway glycerophospholipid metabolism and in Membrane lipid metabolism.

Pathwayi: arachidonate metabolism

This protein is involved in the pathway arachidonate metabolism, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway arachidonate metabolism and in Lipid metabolism.

Pathwayi: prostaglandin biosynthesis

This protein is involved in the pathway prostaglandin biosynthesis, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway prostaglandin biosynthesis and in Lipid metabolism.

Pathwayi: leukotriene B4 biosynthesis

This protein is involved in the pathway leukotriene B4 biosynthesis, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway leukotriene B4 biosynthesis and in Lipid metabolism.

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 bindingi40Calcium 1By similarity1
Metal bindingi40Calcium 2By similarity1
Metal bindingi41Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi43Calcium 1By similarity1
Metal bindingi43Calcium 2By similarity1
Metal bindingi65Calcium 1By similarity1
Metal bindingi93Calcium 2By similarity1
Metal bindingi94Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi95Calcium 2By similarity1
<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 sitei228NucleophileBy similarity1
Active sitei549Proton acceptorBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionHydrolase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Glycerol metabolism, Leukotriene biosynthesis, Lipid biosynthesis, Lipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism
LigandCalcium, Lipid-binding, Metal-binding

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00383
UPA00662
UPA00878
UPA00940

<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:
Cytosolic phospholipase A2
Short name:
cPLA2
Alternative name(s):
Phospholipase A2 group IVA
Including the following 2 domains:
Phospholipase A2 (EC:3.1.1.4By similarity)
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
Lysophospholipase (EC:3.1.1.5By similarity)
<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:PLA2G4A
Synonyms:CPLA2, PLA2G4
<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>OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
<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 identifieri9601 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo
<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
  • UP000001595 <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: Unplaced

<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

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane, Nucleus

<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_00003451341 – 749Cytosolic phospholipase A2Add BLAST749

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 residuei2PhosphoserineBy similarity1
Modified residuei268PhosphothreonineBy similarity1
Modified residuei434PhosphoserineBy similarity1
Modified residuei435PhosphoserineBy similarity1
Modified residuei437PhosphoserineBy similarity1
Modified residuei505Phosphoserine; by MAPKBy similarity1
Modified residuei515PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki541Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki606Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei727PhosphoserineBy similarity1
Modified residuei729PhosphoserineBy similarity1

<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

Phosphorylated at both Ser-505 and Ser-727 in response to mitogenic stimuli.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

<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 KAT5.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9601.ENSPPYP00000000461

<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

Biological Magnetic Resonance Data Bank

More...BMRBi		Q5R8A5

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

More...SMRi		Q5R8A5

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini6 – 122C2PROSITE-ProRule annotationAdd BLAST117
Domaini140 – 740PLA2cPROSITE-ProRule annotationAdd BLAST601

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 178Phospholipid bindingBy similarityAdd BLAST178

<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

The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic calcium. In the presence of phosphoinositides, regulates phospholipase A2 and lysophospholipase activities in a calcium-independent way.By similarity

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1012, Eukaryota
KOG1325, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q5R8A5

Database of Orthologous Groups

More...OrthoDBi		302848at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd04036, C2_cPLA2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.150, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR016035, Acyl_Trfase/lysoPLipase
IPR041847, C2_cPLA2
IPR000008, C2_dom
IPR035892, C2_domain_sf
IPR002642, LysoPLipase_cat_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00168, C2, 1 hit
PF01735, PLA2_B, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00239, C2, 1 hit
SM00022, PLAc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52151, SSF52151, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50004, C2, 1 hit
PS51210, PLA2C, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

Q5R8A5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSFIDPYQHI IVEHQYSHKF TVVVLCATKV TKGAFGDMLD TPDPYVELFI 
        60         70         80         90        100
STTPDSRKRT RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE 
       110        120        130        140        150
TLGTATFPVS SMKVGEKKEV PFIFNQVTEM ILEMSLEVCS CPDLRFSMAL 
       160        170        180        190        200
CDQEKTFRQQ RKEHIRESMK KLLGPKNSEG LHSARDVPVV AILGSGGGFR 
       210        220        230        240        250
AMVGFSGVMK ALYESGILDC ATYVAGLSGS TWYMSTLYSH PDFPEKGPEE 
       260        270        280        290        300
INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG 
       310        320        330        340        350
ETLIHNRMNT TLSSLKEKVN TAQCPLPLFT CLHVKPDVSE LMFADWVEFS 
       360        370        380        390        400
PYEIGMAKYG TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL 
       410        420        430        440        450
FNRVLGVSGS QSRGSTMEEE LENITTKHIV SNDSSDSDDE SHEPKGTENE 
       460        470        480        490        500
DAGSDYQSDN QASWIHRMIM ALVSDSALFN TREGRAGKVH NFMLGLNLNT 
       510        520        530        540        550
SYPLSPLSDF ATQDSFDDDE LDAAVADPDE FERIYEPLDV KSKKIHVVDS 
       560        570        580        590        600
GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWAKMN 
       610        620        630        640        650
KLPFPKIDPY VFDREGLKEC YVFKPKNPDM EKDCPTIIHF VLANINFRKY 
       660        670        680        690        700
KAPGVPRETE EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMHFN 
       710        720        730        740 
TLNNIDVIKE AMVESIEYRR QNPSRCSVSL SNVEARRFFN KEFLSKPKA
Length:749
Mass (Da):85,168
Last modified:December 21, 2004 - 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:i70C1D0C9E983BBD4
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
CR859848 mRNA Translation: CAH92005.1

NCBI Reference Sequences

More...RefSeqi		NP_001126164.1, NM_001132692.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		100173125

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		pon:100173125

<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
CR859848 mRNA Translation: CAH92005.1
RefSeqiNP_001126164.1, NM_001132692.1

3D structure databases

BMRBiQ5R8A5
SMRiQ5R8A5
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000000461

Genome annotation databases

GeneIDi100173125
KEGGipon:100173125

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5321

Phylogenomic databases

eggNOGiKOG1012, Eukaryota
KOG1325, Eukaryota
InParanoidiQ5R8A5
OrthoDBi302848at2759

Enzyme and pathway databases

UniPathwayiUPA00383
UPA00662
UPA00878
UPA00940

Family and domain databases

CDDicd04036, C2_cPLA2, 1 hit
Gene3Di2.60.40.150, 1 hit
InterProiView protein in InterPro
IPR016035, Acyl_Trfase/lysoPLipase
IPR041847, C2_cPLA2
IPR000008, C2_dom
IPR035892, C2_domain_sf
IPR002642, LysoPLipase_cat_dom
PfamiView protein in Pfam
PF00168, C2, 1 hit
PF01735, PLA2_B, 1 hit
SMARTiView protein in SMART
SM00239, C2, 1 hit
SM00022, PLAc, 1 hit
SUPFAMiSSF52151, SSF52151, 1 hit
PROSITEiView protein in PROSITE
PS50004, C2, 1 hit
PS51210, PLA2C, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiPA24A_PONAB
<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: Q5R8A5
<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: July 22, 2008
Last sequence update: December 21, 2004
Last modified: December 2, 2020
This is version 76 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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