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Entry version 172 (02 Dec 2020)
Sequence version 3 (31 Oct 2012)
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Protein

85/88 kDa calcium-independent phospholipase A2

Gene

Pla2g6

Organism
Mus musculus (Mouse)
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

Calcium-independent phospholipase involved in phospholipid remodeling with implications in cellular membrane homeostasis, mitochondrial integrity and signal transduction. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity respectively), producing lysophospholipids that are used in deacylation-reacylation cycles (PubMed:18937505). Hydrolyzes both saturated and unsaturated long fatty acyl chains in various glycerophospholipid classes such as phosphatidylcholines, phosphatidylethanolamines and phosphatidates, with a preference for hydrolysis at sn-2 position. Can further hydrolyze lysophospholipids carrying saturated fatty acyl chains (lysophospholipase activity). Upon oxidative stress, contributes to remodeling of mitochondrial phospholipids in pancreatic beta cells, in a repair mechanism to reduce oxidized lipid content (By similarity). Preferentially hydrolyzes oxidized polyunsaturated fatty acyl chains from cardiolipins, yielding monolysocardiolipins that can be reacylated with unoxidized fatty acyls to regenerate native cardiolipin species. Hydrolyzes oxidized glycerophosphoethanolamines present in pancreatic islets, releasing oxidized polyunsaturated fatty acids such as hydroxyeicosatetraenoates (HETEs) (PubMed:24648512). Has thioesterase activity toward fatty-acyl CoA releasing CoA-SH known to facilitate fatty acid transport and beta-oxidation in mitochondria particularly in skeletal muscle (PubMed:18937505). Plays a role in regulation of membrane dynamics and homeostasis. Selectively hydrolyzes sn-2 arachidonoyl group in plasmalogen phospholipids, structural components of lipid rafts and myelin (By similarity). Regulates F-actin polymerization at the pseudopods, which is required for both speed and directionality of MCP1/CCL2-induced monocyte chemotaxis (By similarity). Targets membrane phospholipids to produce potent lipid signaling messengers. Generates lysophosphatidate (LPA, 1-acyl-glycerol-3-phosphate), which acts via G-protein receptors in various cell types. Has phospholipase A2 activity toward platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), likely playing a role in inactivation of this potent proinflammatory signaling lipid (By similarity). In response to glucose, amplifies calcium influx in pancreatic beta cells to promote INS secretion (PubMed:17895289).By similarity3 Publications

<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

Inhibited by calcium-activated calmodulin (By similarity). Activated by ATP (PubMed:18937505, PubMed:17895289). Inhibited by bromoenol lactone (BEL) (PubMed:18937505, PubMed:17895289).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei520NucleophilePROSITE-ProRule annotation1
Active sitei653Proton acceptorPROSITE-ProRule annotation1

<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 functionCalmodulin-binding, Hydrolase
Biological processChemotaxis, Lipid metabolism, Phospholipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1482788, Acyl chain remodelling of PC
R-MMU-1482839, Acyl chain remodelling of PE
R-MMU-2029485, Role of phospholipids in phagocytosis
R-MMU-6811436, COPI-independent Golgi-to-ER retrograde traffic

<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:
85/88 kDa calcium-independent phospholipase A2 (EC:3.1.1.41 Publication)
Short name:
CaI-PLA2
Alternative name(s):
2-lysophosphatidylcholine acylhydrolase (EC:3.1.1.5By similarity)
Group VI phospholipase A2
Short name:
GVI PLA2
Intracellular membrane-associated calcium-independent phospholipase A2 beta
Short name:
iPLA2-beta
Palmitoyl-CoA hydrolase (EC:3.1.2.21 Publication)
Patatin-like phospholipase domain-containing protein 9
Short name:
PNPLA9
<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:Pla2g6
Synonyms:Pnpla9
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 15

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1859152, Pla2g6

<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%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>Transmembranei481 – 501HelicalSequence analysisAdd BLAST21
Transmembranei512 – 532HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane, Mitochondrion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Knockout mice represent an appropriate model for studying the pathogenesis of neuroaxonal dystrophy in human neurodegenerative diseases (PubMed:18305254, PubMed:18937505). Mutant mice show neuroaxonal dystrophy and significant motor dysfunction from the age of 50 weeks that progressed to ataxia by 2 years (PubMed:18305254). At 55 weeks they display numerous spheroids located in the axons and synapses throughout central and peripheral nervous system, mostly prominent in the tegmentum of the medulla, the lower pons, and the dorsal horns of the spinal cord. Sciatic nerves have reduced numbers of myelinated fibers indicative of neural degeneration (PubMed:18305254). The neuroaxonal dystrophy is associated with deficient remodeling of the mitochondrial inner membrane and presynaptic membrane of axon terminals (PubMed:21813701). Mutant mice gradually lose weight and die earlier than wild-type littermates (PubMed:18305254). Mutant male mice show reduced fertility (PubMed:18305254).3 Publications

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3259503

<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_00000670381 – 80785/88 kDa calcium-independent phospholipase A2Add BLAST807

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 residuei13PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P97819

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P97819

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

More...
PaxDbi
P97819

PeptideAtlas

More...
PeptideAtlasi
P97819

PRoteomics IDEntifications database

More...
PRIDEi
P97819

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P97819

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

More...
PhosphoSitePlusi
P97819

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

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

Expressed in neurons of central and peripheral nervous system (PubMed:18937505, PubMed:18305254). Highly expressed in Purkinje cells in cerebellum and dorsal and ventral horn neurons in the spinal cord (PubMed:18305254). Expressed in testis (at protein level) (PubMed:18305254). Expressed in skeletal muscle (at protein level) (PubMed:18937505).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000042632, Expressed in testis and 289 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P97819, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P97819, MM

<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

Homodimer formed by catalytic domains tightly interacting through a large hydrophobic interface. The contact area involves 3 alpha helices, several loops and a part of the beta sheet from each monomer. Both active sites of the dimer are in close proximity adopting an open conformation that provide sufficient space for phospholipid access and favoring cooperativity in deacylation-reacylation reactions. Each monomer has 9 ankyrin repeats stacked side-by-side in an elongated structure oriented outwards from the catalytic core.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
207296, 1 interactor

Protein interaction database and analysis system

More...
IntActi
P97819, 3 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000132071

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P97819, protein

<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
P97819

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 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati120 – 147ANK 1By similarityAdd BLAST28
Repeati151 – 181ANK 1Sequence analysisAdd BLAST31
Repeati185 – 215ANK 2Sequence analysisAdd BLAST31
Repeati219 – 248ANK 3Sequence analysisAdd BLAST30
Repeati251 – 281ANK 4Sequence analysisAdd BLAST31
Repeati286 – 312ANK 5Sequence analysisAdd BLAST27
Repeati316 – 345ANK 6Sequence analysisAdd BLAST30
Repeati349 – 378ANK 7Sequence analysisAdd BLAST30
Repeati382 – 403ANK 9By similarityAdd BLAST22
<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>Domaini482 – 666PNPLAPROSITE-ProRule annotationAdd BLAST185

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>Regioni678 – 687Calmodulin-binding (1-9-14 motif)By similarity10
Regioni749 – 760Calmodulin-binding (IQ motif)By similarityAdd BLAST12

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi486 – 491GXGXXGPROSITE-ProRule annotation6
Motifi518 – 522GXSXGPROSITE-ProRule annotation5
Motifi653 – 655DGA/GPROSITE-ProRule annotation3

<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

Has two putative calmodulin binding domains, the 1-9-14 and IQ motifs. One calmodulin molecule interacts with PLA2G6 dimer, likely through 1-9-14 motif on each monomer (By similarity). Binds calmodulin in a calcium-dependent way (By similarity).By similarity

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0513, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158756

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_010817_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P97819

Identification of Orthologs from Complete Genome Data

More...
OMAi
DSWTRPY

TreeFam database of animal gene trees

More...
TreeFami
TF319230

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.20, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016035, Acyl_Trfase/lysoPLipase
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR002641, PNPLA_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12796, Ank_2, 2 hits
PF01734, Patatin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01415, ANKYRIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248, ANK, 6 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48403, SSF48403, 1 hit
SSF52151, SSF52151, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 4 hits
PS51635, PNPLA, 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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform Long (identifier: P97819-1) [UniParc]FASTAAdd to basket
Also known as: iPLA2-L

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
MQFFGRLVNT LSSVTNLFSN PFRVKEVSLT DYVSSERVRE EGQLILLQNV
60 70 80 90 100
SNRTWDCVLV SPRNPQSGFR LFQLESEADA LVNFQQFSSQ LPPFYESSVQ
110 120 130 140 150
VLHVEVLQHL TDLIRNHPSW TVTHLAVELG IRECFHHSRI ISCANSTENE
160 170 180 190 200
EGCTPLHLAC RKGDSEILVE LVQYCHAQMD VTDNKGETAF HYAVQGDNPQ
210 220 230 240 250
VLQLLGKNAS AGLNQVNNQG LTPLHLACKM GKQEMVRVLL LCNARCNIMG
260 270 280 290 300
PGGFPIHTAM KFSQKGCAEM IISMDSNQIH SKDPRYGASP LHWAKNAEMA
310 320 330 340 350
RMLLKRGCDV DSTSSSGNTA LHVAVMRNRF DCVMVLLTYG ANAGARGEHG
360 370 380 390 400
NTPLHLAMSK DNMEMVKALI VFGAEVDTPN DFGETPALIA SKISKLITRK
410 420 430 440 450
ALLTLLKTVG ADHHFPIIQG VSTEQGSAAA THPLFSLDRT QPPAISLNNL
460 470 480 490 500
ELQDLMPISR ARKPAFILSS MRDEKRSHDH LLCLDGGGVK GLVIIQLLIA
510 520 530 540 550
IEKASGVATK DLFDWVAGTS TGGILALAIL HSKSMAYMRG VYFRMKDEVF
560 570 580 590 600
RGSRPYESGP LEEFLKREFG EHTKMTDVKK PKVMLTGTLS DRQPAELHLF
610 620 630 640 650
RNYDAPEAVR EPRCNQNINL KPPTQPADQL VWRAARSSGA APTYFRPNGR
660 670 680 690 700
FLDGGLLANN PTLDAMTEIH EYNQDMIRKG QGNKVKKLSI VVSLGTGKSP
710 720 730 740 750
QVPVTCVDVF RPSNPWELAK TVFGAKELGK MVVDCCTDPD GRAVDRARAW
760 770 780 790 800
CEMVGIQYFR LNPQLGSDIM LDEVSDAVLV NALWETEVYI YEHREEFQKL

VQLLLSP
Length:807
Mass (Da):89,560
Last modified:October 31, 2012 - v3
<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:i3838889731100294
GO
Isoform Short (identifier: P97819-2) [UniParc]FASTAAdd to basket
Also known as: iPLA2-S

The sequence of this isoform differs from the canonical sequence as follows:
     396-451: LITRKALLTLLKTVGADHHFPIIQGVSTEQGSAAATHPLFSLDRTQPPAISLNNLE → Q

Show »
Length:752
Mass (Da):83,702
Checksum:iAAC3347B0E1292E9
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3UX52G3UX52_MOUSE
85/88 kDa calcium-independent phosp...
Pla2g6
199Annotation score:

Annotation score:1 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>
G3UY97G3UY97_MOUSE
85/88 kDa calcium-independent phosp...
Pla2g6
204Annotation score:

Annotation score:1 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>
G3UX73G3UX73_MOUSE
85/88 kDa calcium-independent phosp...
Pla2g6
33Annotation score:

Annotation score:1 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_044364396 – 451LITRK…LNNLE → Q in isoform Short. 2 PublicationsAdd BLAST56

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

More...
DDBJi
Links Updated
U88624 mRNA Translation: AAB48511.2
AF259401 mRNA Translation: AAF72651.1
BC003487 mRNA Translation: AAH03487.1
BC057209 mRNA Translation: AAH57209.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS27637.1 [P97819-2]
CCDS56991.1 [P97819-1]

NCBI Reference Sequences

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RefSeqi
NP_001185952.1, NM_001199023.1 [P97819-1]
NP_001185953.1, NM_001199024.1 [P97819-2]
NP_001185954.1, NM_001199025.1 [P97819-2]
NP_058611.1, NM_016915.4 [P97819-2]
XP_006521215.1, XM_006521152.2 [P97819-1]
XP_006521216.1, XM_006521153.3 [P97819-1]
XP_006521217.1, XM_006521154.1 [P97819-1]
XP_006521218.1, XM_006521155.2 [P97819-1]
XP_006521219.1, XM_006521156.3 [P97819-1]
XP_006521220.1, XM_006521157.3 [P97819-1]
XP_006521221.1, XM_006521158.2 [P97819-1]
XP_006521222.1, XM_006521159.3 [P97819-1]
XP_006521223.1, XM_006521160.2 [P97819-1]
XP_017172187.1, XM_017316698.1 [P97819-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000047816; ENSMUSP00000044234; ENSMUSG00000042632 [P97819-2]
ENSMUST00000166977; ENSMUSP00000132071; ENSMUSG00000042632 [P97819-2]
ENSMUST00000172403; ENSMUSP00000131081; ENSMUSG00000042632 [P97819-2]
ENSMUST00000173163; ENSMUSP00000134456; ENSMUSG00000042632 [P97819-2]
ENSMUST00000174021; ENSMUSP00000134672; ENSMUSG00000042632 [P97819-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
53357

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:53357

UCSC genome browser

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UCSCi
uc007wtd.2, mouse [P97819-1]

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
U88624 mRNA Translation: AAB48511.2
AF259401 mRNA Translation: AAF72651.1
BC003487 mRNA Translation: AAH03487.1
BC057209 mRNA Translation: AAH57209.1
CCDSiCCDS27637.1 [P97819-2]
CCDS56991.1 [P97819-1]
RefSeqiNP_001185952.1, NM_001199023.1 [P97819-1]
NP_001185953.1, NM_001199024.1 [P97819-2]
NP_001185954.1, NM_001199025.1 [P97819-2]
NP_058611.1, NM_016915.4 [P97819-2]
XP_006521215.1, XM_006521152.2 [P97819-1]
XP_006521216.1, XM_006521153.3 [P97819-1]
XP_006521217.1, XM_006521154.1 [P97819-1]
XP_006521218.1, XM_006521155.2 [P97819-1]
XP_006521219.1, XM_006521156.3 [P97819-1]
XP_006521220.1, XM_006521157.3 [P97819-1]
XP_006521221.1, XM_006521158.2 [P97819-1]
XP_006521222.1, XM_006521159.3 [P97819-1]
XP_006521223.1, XM_006521160.2 [P97819-1]
XP_017172187.1, XM_017316698.1 [P97819-2]

3D structure databases

SMRiP97819
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi207296, 1 interactor
IntActiP97819, 3 interactors
STRINGi10090.ENSMUSP00000132071

Chemistry databases

ChEMBLiCHEMBL3259503

PTM databases

iPTMnetiP97819
PhosphoSitePlusiP97819

Proteomic databases

EPDiP97819
MaxQBiP97819
PaxDbiP97819
PeptideAtlasiP97819
PRIDEiP97819

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
225, 237 antibodies

Genome annotation databases

EnsembliENSMUST00000047816; ENSMUSP00000044234; ENSMUSG00000042632 [P97819-2]
ENSMUST00000166977; ENSMUSP00000132071; ENSMUSG00000042632 [P97819-2]
ENSMUST00000172403; ENSMUSP00000131081; ENSMUSG00000042632 [P97819-2]
ENSMUST00000173163; ENSMUSP00000134456; ENSMUSG00000042632 [P97819-2]
ENSMUST00000174021; ENSMUSP00000134672; ENSMUSG00000042632 [P97819-1]
GeneIDi53357
KEGGimmu:53357
UCSCiuc007wtd.2, mouse [P97819-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8398
MGIiMGI:1859152, Pla2g6

Phylogenomic databases

eggNOGiKOG0513, Eukaryota
GeneTreeiENSGT00940000158756
HOGENOMiCLU_010817_0_0_1
InParanoidiP97819
OMAiDSWTRPY
TreeFamiTF319230

Enzyme and pathway databases

ReactomeiR-MMU-1482788, Acyl chain remodelling of PC
R-MMU-1482839, Acyl chain remodelling of PE
R-MMU-2029485, Role of phospholipids in phagocytosis
R-MMU-6811436, COPI-independent Golgi-to-ER retrograde traffic

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
53357, 0 hits in 17 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Pla2g6, mouse

Protein Ontology

More...
PROi
PR:P97819
RNActiP97819, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000042632, Expressed in testis and 289 other tissues
ExpressionAtlasiP97819, baseline and differential
GenevisibleiP97819, MM

Family and domain databases

Gene3Di1.25.40.20, 2 hits
InterProiView protein in InterPro
IPR016035, Acyl_Trfase/lysoPLipase
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR002641, PNPLA_dom
PfamiView protein in Pfam
PF12796, Ank_2, 2 hits
PF01734, Patatin, 1 hit
PRINTSiPR01415, ANKYRIN
SMARTiView protein in SMART
SM00248, ANK, 6 hits
SUPFAMiSSF48403, SSF48403, 1 hit
SSF52151, SSF52151, 1 hit
PROSITEiView protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 4 hits
PS51635, PNPLA, 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 nameiPLPL9_MOUSE
<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: P97819
Secondary accession number(s): Q99LA9, Q9JK61
<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: May 30, 2000
Last sequence update: October 31, 2012
Last modified: December 2, 2020
This is version 172 of the entry and version 3 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

Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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