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UniProtKB - Q9NZ20 (PA2G3_HUMAN)

Entry version 165 (07 Apr 2021)
Sequence version 2 (11 Jan 2011)
Previous versions | rss
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Protein

Group 3 secretory phospholipase A2

Gene

PLA2G3

Organism
Homo sapiens (Human)
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

Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids without apparent head group selectivity (PubMed:12522102, PubMed:18801741, PubMed:15863501, PubMed:28947740). Contributes to phospholipid remodeling of low-density lipoprotein (LDL) and high-density lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells (PubMed:18801741). May act in an autocrine and paracrine manner (PubMed:23624557). Secreted by immature mast cells, acts on nearby fibroblasts upstream to PTDGS to synthesize prostaglandin D2 (PGD2), which in turn promotes mast cell maturation and degranulation via PTGDR (PubMed:23624557). Secreted by epididymal epithelium, acts on immature sperm cells within the duct, modulating the degree of unsaturation of the fatty acyl components of phosphatidylcholines required for acrosome assembly and sperm cell motility. Facilitates the replacement of fatty acyl chains in phosphatidylcholines in sperm membranes from omega-6 and omega-9 to omega-3 polyunsaturated fatty acids (PUFAs). Coupled to lipoxygenase pathway, may process omega-6 PUFAs to generate oxygenated lipid mediators in the male reproductive tract (By similarity). At pericentrosomal preciliary compartment, negatively regulates ciliogenesis likely by regulating endocytotic recycling of ciliary membrane protein (PubMed:20393563). Coupled to cyclooxygenase pathway provides arachidonate to generate prostaglandin E2 (PGE2), a potent immunomodulatory lipid in inflammation and tumorigenesis (PubMed:12522102, PubMed:15863501). At colonic epithelial barrier, preferentially hydrolyzes phospholipids having arachidonate and docosahexaenoate at sn-2 position, contributing to the generation of oxygenated metabolites involved in colonic stem cell homeostasis (PubMed:28947740). Releases C16:0 and C18:0 lysophosphatidylcholine subclasses from neuron plasma membranes and promotes neurite outgrowth and neuron survival (PubMed:17868035).By similarity7 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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion.By similarity

<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

Arachidonic acid release is markedly increased by glypican, a glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan.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 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 bindingi158Calcium; via carbonyl oxygenBy similarity1
Metal bindingi160Calcium; via carbonyl oxygenBy similarity1
Metal bindingi162Calcium; via carbonyl oxygenBy 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 sitei184PROSITE-ProRule annotation1
Metal bindingi185CalciumBy similarity1
Active sitei214By 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 processCilium biogenesis/degradation, Lipid metabolism, Mast cell degranulation, Phospholipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q9NZ20

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1482788, Acyl chain remodelling of PC
R-HSA-1482839, Acyl chain remodelling of PE
R-HSA-1482925, Acyl chain remodelling of PG

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001086

<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:
Group 3 secretory phospholipase A2 (EC:3.1.1.42 Publications)
Alternative name(s):
Group III secretory phospholipase A2
Short name:
GIII sPLA2
Short name:
sPLA2-III
Phosphatidylcholine 2-acylhydrolase 3
<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:PLA2G3Imported
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 › Homo
<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
  • UP000005640 <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 22

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:17934, PLA2G3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		611651, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9NZ20

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000100078.3

<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

Cell membrane, Cytoplasm, Cytoskeleton, Endosome, 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

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>Mutagenesisi167N → S: Loss of glycosylation. 1 Publication1
Mutagenesisi184H → Q: Impairs PGE2 synthesis. Impairs PGD2 synthesis. Impairs mast cell degranulation. Impairs neurite outgrowth. 4 Publications1
Mutagenesisi280N → S: Loss of glycosylation. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		50487

Open Targets

More...OpenTargetsi		ENSG00000100078

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA38267

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9NZ20, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4667

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PLA2G3

Domain mapping of disease mutations (DMDM)

More...DMDMi		317373314

<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 – 19Sequence analysisAdd BLAST19
<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_000002299220 – 509Group 3 secretory phospholipase A2Sequence analysisAdd BLAST490

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 bondi159 ↔ 181By similarity
<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>Glycosylationi167N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi180 ↔ 220By similarity
Disulfide bondi187 ↔ 213By similarity
Disulfide bondi211 ↔ 244By similarity
Glycosylationi280N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi325N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi396N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi439N-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-glycosylation does not affect the catalytic activity, but is required for proper secretion. A nonglycosylated form is observed in several cell types.1 Publication
In several cell types, the N- and C-termini are cleaved off.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9NZ20

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9NZ20

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

More...PaxDbi		Q9NZ20

PeptideAtlas

More...PeptideAtlasi		Q9NZ20

PRoteomics IDEntifications database

More...PRIDEi		Q9NZ20

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		83316

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q9NZ20, 5 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9NZ20

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

More...PhosphoSitePlusi		Q9NZ20

<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 kidney, heart, liver, and skeletal muscle. Also present in placenta and peripheral blood leukocytes. Not detected in colon, thymus, spleen and small intestine. In lung, expressed in bronchial epithelial cells and alveolar macrophages, but scarcely detected in alveolar epithelium, arterial walls and interstitial fibroblasts (at protein level). In joints of osteoarthritis and rheumatoid arthritis, expressed in endothelial cells (at protein level). In normal heart, detected in some vessels. In myocardial tissues with acute infarction, expressed in vascular endothelial cells adjacent to cardiomyocytes and those in lesions with granulation. Expression in cardiomyocytes is scarce (at protein level). In uterus, breast and colon cancers, detected in tumor cells and neighboring microvascular endothelium, but not in normal glandular tissues (at protein level) (PubMed:15863501). Expressed in dermal resting mast cells (at protein level) and pulmonary mast cells (PubMed:23624557). Expressed in neuronal fibers (at protein level) (PubMed:17868035). Highly expressed in dorsal root ganglia neurons (at protein level) (PubMed:17868035). Expressed in Purkinje cells in cerebellum (at protein level) (PubMed:17868035). In stomach is preferentially expressed in neuronal fibers and in microvascular endothelium (PubMed:17868035). Sparsely expressed in normal aorta (at protein level). Highly expressed in macrophages and smooth muscle cells in aorta with atheroma (PubMed:18801741).4 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By IL1B/interleukin-1 beta and TNF in microvascular endothelial cells (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000100078, Expressed in ectocervix and 97 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9NZ20, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000100078, Tissue enhanced (esophagus, skin, tongue)

<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		119074, 2 interactors

Protein interaction database and analysis system

More...IntActi		Q9NZ20, 2 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000215885

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9NZ20, 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		Q9NZ20

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni150 – 291Phospholipase A2-like3 PublicationsAdd BLAST142

<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 phospholipase A2-like domain represents the fully processed form after N- and C-termini are cleaved off. It is the secreted mature form found in biological fluids.3 Publications

<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 phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QTYI, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000161662

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_535922_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9NZ20

Identification of Orthologs from Complete Genome Data

More...OMAi		CPQNISP

Database of Orthologous Groups

More...OrthoDBi		893757at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9NZ20

TreeFam database of animal gene trees

More...TreeFami		TF324679

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.90.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR016090, PLipase_A2_dom
IPR036444, PLipase_A2_dom_sf
IPR033113, PLipase_A2_His_AS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF05826, Phospholip_A2_2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48619, SSF48619, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00118, PA2_HIS, 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.

<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.

Q9NZ20-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGVQAGLFGM LGFLGVALGG SPALRWYRTS CHLTKAVPGN PLGYLSFLAK 
        60         70         80         90        100
DAQGLALIHA RWDAHRRLQS CSWEDEPELT AAYGALCAHE TAWGSFIHTP 
       110        120        130        140        150
GPELQRALAT LQSQWEACRA LEESPAGARK KRAAGQSGVP GGGHQREKRG 
       160        170        180        190        200
WTMPGTLWCG VGDSAGNSSE LGVFQGPDLC CREHDRCPQN ISPLQYNYGI 
       210        220        230        240        250
RNYRFHTISH CDCDTRFQQC LQNQHDSISD IVGVAFFNVL EIPCFVLEEQ 
       260        270        280        290        300
EACVAWYWWG GCRMYGTVPL ARLQPRTFYN ASWSSRATSP TPSSRSPAPP 
       310        320        330        340        350
KPRQKQHLRK GPPHQKGSKR PSKANTTALQ DPMVSPRLDV APTGLQGPQG 
       360        370        380        390        400
GLKPQGARWV CRSFRRHLDQ CEHQIGPREI EFQLLNSAQE PLFHCNCTRR 
       410        420        430        440        450
LARFLRLHSP PEVTNMLWEL LGTTCFKLAP PLDCVEGKNC SRDPRAIRVS 
       460        470        480        490        500
ARHLRRLQQR RHQLQDKGTD ERQPWPSEPL RGPMSFYNQC LQLTQAARRP 

DRQQKSWSQ
Length:509
Mass (Da):57,167
Last modified:January 11, 2011 - v2
<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:iED03BED129B0BC9F
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD15617 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02455570S → A2 PublicationsCorresponds to variant dbSNP:rs2232176Ensembl.1
Natural variantiVAR_024556116E → Q. Corresponds to variant dbSNP:rs2074734Ensembl.1
Natural variantiVAR_020288157L → V. Corresponds to variant dbSNP:rs2074735Ensembl.1
Natural variantiVAR_056581307H → Y. Corresponds to variant dbSNP:rs2232180Ensembl.1
Natural variantiVAR_024557322S → R. Corresponds to variant dbSNP:rs2072193Ensembl.1
Natural variantiVAR_034366378R → Q. Corresponds to variant dbSNP:rs2232183Ensembl.1

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
AF220490 mRNA Translation: AAF44746.1
AC005005 Genomic DNA Translation: AAD15617.1 Sequence problems.
BC025316 mRNA Translation: AAH25316.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS13889.1

NCBI Reference Sequences

More...RefSeqi		NP_056530.2, NM_015715.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000215885; ENSP00000215885; ENSG00000100078

Database of genes from NCBI RefSeq genomes

More...GeneIDi		50487

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:50487

UCSC genome browser

More...UCSCi		uc003aka.4, human

<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
AF220490 mRNA Translation: AAF44746.1
AC005005 Genomic DNA Translation: AAD15617.1 Sequence problems.
BC025316 mRNA Translation: AAH25316.1
CCDSiCCDS13889.1
RefSeqiNP_056530.2, NM_015715.4

3D structure databases

SMRiQ9NZ20
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi119074, 2 interactors
IntActiQ9NZ20, 2 interactors
STRINGi9606.ENSP00000215885

Chemistry databases

ChEMBLiCHEMBL4667
SwissLipidsiSLP:000001086

PTM databases

GlyGeniQ9NZ20, 5 sites
iPTMnetiQ9NZ20
PhosphoSitePlusiQ9NZ20

Genetic variation databases

BioMutaiPLA2G3
DMDMi317373314

Proteomic databases

EPDiQ9NZ20
MassIVEiQ9NZ20
PaxDbiQ9NZ20
PeptideAtlasiQ9NZ20
PRIDEiQ9NZ20
ProteomicsDBi83316

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		11027, 184 antibodies

The DNASU plasmid repository

More...DNASUi		50487

Genome annotation databases

EnsembliENST00000215885; ENSP00000215885; ENSG00000100078
GeneIDi50487
KEGGihsa:50487
UCSCiuc003aka.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		50487
DisGeNETi50487

GeneCards: human genes, protein and diseases

More...GeneCardsi		PLA2G3
HGNCiHGNC:17934, PLA2G3
HPAiENSG00000100078, Tissue enhanced (esophagus, skin, tongue)
MIMi611651, gene
neXtProtiNX_Q9NZ20
OpenTargetsiENSG00000100078
PharmGKBiPA38267
VEuPathDBiHostDB:ENSG00000100078.3

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG502QTYI, Eukaryota
GeneTreeiENSGT00940000161662
HOGENOMiCLU_535922_0_0_1
InParanoidiQ9NZ20
OMAiCPQNISP
OrthoDBi893757at2759
PhylomeDBiQ9NZ20
TreeFamiTF324679

Enzyme and pathway databases

PathwayCommonsiQ9NZ20
ReactomeiR-HSA-1482788, Acyl chain remodelling of PC
R-HSA-1482839, Acyl chain remodelling of PE
R-HSA-1482925, Acyl chain remodelling of PG

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		50487, 3 hits in 987 CRISPR screens

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		50487
PharosiQ9NZ20, Tbio

Protein Ontology

More...PROi		PR:Q9NZ20
RNActiQ9NZ20, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000100078, Expressed in ectocervix and 97 other tissues
GenevisibleiQ9NZ20, HS

Family and domain databases

Gene3Di1.20.90.10, 2 hits
InterProiView protein in InterPro
IPR016090, PLipase_A2_dom
IPR036444, PLipase_A2_dom_sf
IPR033113, PLipase_A2_His_AS
PfamiView protein in Pfam
PF05826, Phospholip_A2_2, 1 hit
SUPFAMiSSF48619, SSF48619, 2 hits
PROSITEiView protein in PROSITE
PS00118, PA2_HIS, 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 nameiPA2G3_HUMAN
<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: Q9NZ20
Secondary accession number(s): O95768
<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: February 11, 2002
Last sequence update: January 11, 2011
Last modified: April 7, 2021
This is version 165 of the entry and version 2 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families
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