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UniProtKB - Q8VEB4 (PAG15_MOUSE)

Entry version 145 (02 Dec 2020)
Sequence version 1 (01 Mar 2002)
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Protein

Phospholipase A2 group XV

Gene

Pla2g15

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

Has dual calcium-independent phospholipase and O-acyltransferase activities with a potential role in glycerophospholipid homeostasis and remodeling of acyl groups of lipophilic alcohols present in acidic cellular compartments (PubMed:16837646, PubMed:17626977, PubMed:11790796, PubMed:16106046, PubMed:16880524, PubMed:19017977, PubMed:20410020). Catalyzes hydrolysis of the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 or A2 activity) and transfer it to the hydroxyl group at the first carbon of lipophilic alcohols (O-acyltransferase activity). Among preferred fatty acyl donors are phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols and phosphatidylserines (PubMed:20410020). Favors sn-2 over sn-1 deacylation of unsaturated fatty acyl groups of phosphatidylcholines and phosphatidylethanolamines (PubMed:16837646, PubMed:17626977). Among preferred fatty acyl acceptors are natural lipophilic alcohols including short-chain ceramide N-acetyl-sphingosine (C2 ceramide), alkylacylglycerols, monoacylglycerols, and acylethanolamides such as anandamide and oleoylethanolamide (PubMed:16837646, PubMed:17626977). Selectively hydrolyzes the sn-1 fatty acyl group of truncated oxidized phospholipids and may play a role in detoxification of reactive oxidized phospholipids during oxidative stress (PubMed:27993948). Required for normal phospholipid degradation in alveolar macrophages with potential implications in pulmonary surfactant clearance (PubMed:16880524, PubMed:19017977). At neutral pH, hydrolyzes the sn-1 fatty acyl group of the lysophosphatidylcholines (By similarity).By similarity8 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

Phospholipase sn-2 versus sn-1 positional specificity is affected by the phospholipid composition of membranes. Phospholipase A2 activity toward 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine (PAPE) is enhanced in the presence of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), which promotes lipid bilayer formation (PubMed:16837646). O-acyltransferase activity is inhibited by antiarrhythmic drug amiodarone (PubMed:27993948).2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=171 µM for 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine (O-acyltransferase activity)1 Publication
  1. Vmax=5.55 µmol/min/mg enzyme toward 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine (O-acyltransferase activity)1 Publication

pH dependencei

Optimum pH is 4.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei46Substrate; via amide nitrogenBy 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 sitei198Acyl-ester intermediateSequence analysis2 Publications1
Binding sitei199Substrate; via amide nitrogenBy similarity1
Active sitei360Charge relay systemBy similarity1 Publication1
Active sitei392Charge relay systemBy similarity1 Publication1

<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 functionAcyltransferase, Hydrolase, Transferase
Biological processFatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-1483115, Hydrolysis of LPC

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...ESTHERi		mouse-C87498, PC-sterol_acyltransferase

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000352

<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:
Phospholipase A2 group XV
Alternative name(s):
1-O-acylceramide synthase1 Publication
Short name:
ACS
LCAT-like lysophospholipase (EC:3.1.1.5By similarity)
Short name:
LLPL
Lysophospholipase 3
Lysosomal phospholipase A and acyltransferase (EC:2.3.1.-7 Publications, EC:3.1.1.322 Publications, EC:3.1.1.41 Publication)
Lysosomal phospholipase A22 Publications
Short name:
LPLA21 Publication
<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:Pla2g15Imported
Synonyms:Lypla3
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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 8

Organism-specific databases

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

More...MGIi		MGI:2178076, Pla2g15

<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

Keywords - Cellular componenti

Lysosome, Membrane, Secreted

<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

Mice are born at the expected Mendelian rate, are viable and fertile. They display strongly reduced transacylase activity in lung alveolar macrophages and in peritoneal macrophages, leading to the accumulation of pulmonary surfactant phospholipids with phosphatidylethanolamine and phosphatidylcholine headgroups. Mice display higher numers of alveolar macrophages in the lung, together with a mononuclear cell infiltrate in airways and blood vessels. Alveolar nmacrophages are larger than normal and present lamellar inclusion bodies, indicative of cellular phospholipidosis. Besides, mutant mice display splenomegaly.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi65C → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi89C → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi198S → A: Abolishes enzyme activity. 2 Publications1
Mutagenesisi360D → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi392H → A: Abolishes enzyme activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3259497

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 33By similarityAdd BLAST33
<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_000001780934 – 412Phospholipase A2 group XVAdd BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi65 ↔ 89By similarity1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi99N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi273N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi289N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi398N-linked (GlcNAc...) asparagineSequence analysis1

<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

N-glycosylated (PubMed:11790796). N-glycosylation is important for maturation of the enzyme and normal subcellular location (By similarity).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q8VEB4

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q8VEB4

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

More...PaxDbi		Q8VEB4

PeptideAtlas

More...PeptideAtlasi		Q8VEB4

PRoteomics IDEntifications database

More...PRIDEi		Q8VEB4

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		2363, 7 N-Linked glycans (4 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q8VEB4, 4 sites

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

More...PhosphoSitePlusi		Q8VEB4

<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 blood plasma (PubMed:20410020). Detected in alveolar macrophages (at protein level) (PubMed:16106046, PubMed:16880524, PubMed:19017977). Detected in heart, liver, spleen, kidney, thymus, brain and lung (PubMed:16880524).4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000031903, Expressed in stroma of bone marrow and 261 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q8VEB4, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q8VEB4, 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		228695, 19 interactors

Protein interaction database and analysis system

More...IntActi		Q8VEB4, 2 interactors

Molecular INTeraction database

More...MINTi		Q8VEB4

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000034377

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q8VEB4, 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		Q8VEB4

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

<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 AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2369, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157499

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_037070_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q8VEB4

Identification of Orthologs from Complete Genome Data

More...OMAi		IPGWGDP

Database of Orthologous Groups

More...OrthoDBi		828056at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q8VEB4

TreeFam database of animal gene trees

More...TreeFami		TF313258

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029058, AB_hydrolase
IPR003386, LACT/PDAT_acylTrfase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02450, LCAT, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53474, SSF53474, 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>Sequence (1+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q8VEB4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDRHLCTCRE TQLRSGLLLP LFLLMMLADL TLPAQRHPPV VLVPGDLGNQ 
        60         70         80         90        100
LEAKLDKPKV VHYLCSKKTD SYFTLWLNLE LLLPVIIDCW IDNIRLVYNR 
       110        120        130        140        150
TSRATQFPDG VDVRVPGFGE TFSMEFLDPS KRNVGSYFYT MVESLVGWGY 
       160        170        180        190        200
TRGEDVRGAP YDWRRAPNEN GPYFLALREM IEEMYQMYGG PVVLVAHSMG 
       210        220        230        240        250
NVYMLYFLQR QPQVWKDKYI HAFVSLGAPW GGVAKTLRVL ASGDNNRIPV 
       260        270        280        290        300
IGPLKIREQQ RSAVSTSWLL PYNHTWSHEK VFVYTPTTNY TLRDYHRFFR 
       310        320        330        340        350
DIGFEDGWFM RQDTEGLVEA MTPPGVELHC LYGTGVPTPN SFYYESFPDR 
       360        370        380        390        400
DPKICFGDGD GTVNLESVLQ CQAWQSRQEH RVSLQELPGS EHIEMLANAT 
       410 
TLAYLKRVLL EP
Length:412
Mass (Da):47,307
Last modified:March 1, 2002 - 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:i6544369410C46C9A
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1D5RLZ5A0A1D5RLZ5_MOUSE
Phospholipase A2 group XV
Pla2g15
236Annotation 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>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti342F → S in BAE32987 (PubMed:16141072).Curated1

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
AF468958 mRNA Translation: AAL78651.1
AY179884 Genomic DNA Translation: AAO49009.1
AK085194 mRNA Translation: BAC39387.1
AK155004 mRNA Translation: BAE32987.1
AK163111 mRNA Translation: BAE37197.1
AK170814 mRNA Translation: BAE42046.1
BC019373 mRNA Translation: AAH19373.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS22630.1

NCBI Reference Sequences

More...RefSeqi		NP_598553.1, NM_133792.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000034377; ENSMUSP00000034377; ENSMUSG00000031903

Database of genes from NCBI RefSeq genomes

More...GeneIDi		192654

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:192654

UCSC genome browser

More...UCSCi		uc009nfj.1, mouse

<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
AF468958 mRNA Translation: AAL78651.1
AY179884 Genomic DNA Translation: AAO49009.1
AK085194 mRNA Translation: BAC39387.1
AK155004 mRNA Translation: BAE32987.1
AK163111 mRNA Translation: BAE37197.1
AK170814 mRNA Translation: BAE42046.1
BC019373 mRNA Translation: AAH19373.1
CCDSiCCDS22630.1
RefSeqiNP_598553.1, NM_133792.2

3D structure databases

SMRiQ8VEB4
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi228695, 19 interactors
IntActiQ8VEB4, 2 interactors
MINTiQ8VEB4
STRINGi10090.ENSMUSP00000034377

Chemistry databases

ChEMBLiCHEMBL3259497
SwissLipidsiSLP:000000352

Protein family/group databases

ESTHERimouse-C87498, PC-sterol_acyltransferase

PTM databases

GlyConnecti2363, 7 N-Linked glycans (4 sites)
GlyGeniQ8VEB4, 4 sites
PhosphoSitePlusiQ8VEB4

Proteomic databases

EPDiQ8VEB4
MaxQBiQ8VEB4
PaxDbiQ8VEB4
PeptideAtlasiQ8VEB4
PRIDEiQ8VEB4

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		29747, 104 antibodies

Genome annotation databases

EnsembliENSMUST00000034377; ENSMUSP00000034377; ENSMUSG00000031903
GeneIDi192654
KEGGimmu:192654
UCSCiuc009nfj.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		23659
MGIiMGI:2178076, Pla2g15

Phylogenomic databases

eggNOGiKOG2369, Eukaryota
GeneTreeiENSGT00940000157499
HOGENOMiCLU_037070_1_1_1
InParanoidiQ8VEB4
OMAiIPGWGDP
OrthoDBi828056at2759
PhylomeDBiQ8VEB4
TreeFamiTF313258

Enzyme and pathway databases

ReactomeiR-MMU-1483115, Hydrolysis of LPC

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		192654, 3 hits in 19 CRISPR screens

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

More...ChiTaRSi		Pla2g15, mouse

Protein Ontology

More...PROi		PR:Q8VEB4
RNActiQ8VEB4, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000031903, Expressed in stroma of bone marrow and 261 other tissues
ExpressionAtlasiQ8VEB4, baseline and differential
GenevisibleiQ8VEB4, MM

Family and domain databases

InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR003386, LACT/PDAT_acylTrfase
PfamiView protein in Pfam
PF02450, LCAT, 1 hit
SUPFAMiSSF53474, SSF53474, 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 nameiPAG15_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: Q8VEB4
Secondary accession number(s): Q3TCB1, Q3U303
<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: March 1, 2004
Last sequence update: March 1, 2002
Last modified: December 2, 2020
This is version 145 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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