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P39877 (PA2G5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-dependent phospholipase A2

EC=3.1.1.4
Alternative name(s):
Group V phospholipase A2
PLA2-10
Phosphatidylcholine 2-acylhydrolase 5
Gene names
Name:PLA2G5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length138 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes more efficiently L-alpha-1-palmitoyl-2-oleoyl phosphatidylcholine than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L-alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine, or L-alpha-1-stearoyl-2-arachidonyl phosphatidylinositol. May be involved in the production of lung surfactant, the remodeling or regulation of cardiac muscle.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted.

Tissue specificity

Heart, placenta and less abundantly, in lung. Detected in the outer and inner plexiform layers of the retina (at protein level). Ref.5

Post-translational modification

This enzyme lacks one of the seven disulfide bonds found in similar PA2 proteins.

Involvement in disease

Fleck retina, familial benign (FRFB) [MIM:228980]: An autosomal recessive condition associated with a distinctive retinal appearance and no apparent visual or electrophysiologic deficits. Affected individuals are asymptomatic, but fundus examination reveals a striking pattern of diffuse, yellow-white, fleck-like lesions extending to the far periphery of the retina but sparing the foveal region.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Sequence similarities

Belongs to the phospholipase A2 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.5. Activity remains high up to pH 9.0.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   DiseaseDisease mutation
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid secretion

Inferred from electronic annotation. Source: Ensembl

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

leukotriene biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidic acid biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylcholine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylethanolamine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylglycerol acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylinositol acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylserine acyl-chain remodeling

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

platelet activating factor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipase A2 activity

Traceable author statement Ref.1. Source: ProtInc

heparin binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 138118Calcium-dependent phospholipase A2
PRO_0000022761

Sites

Active site671 By similarity
Active site1111 By similarity
Metal binding471Calcium; via carbonyl oxygen By similarity
Metal binding491Calcium; via carbonyl oxygen By similarity
Metal binding511Calcium; via carbonyl oxygen By similarity
Metal binding681Calcium By similarity

Amino acid modifications

Disulfide bond46 ↔ 137 By similarity
Disulfide bond48 ↔ 64 By similarity
Disulfide bond63 ↔ 117 By similarity
Disulfide bond70 ↔ 110 By similarity
Disulfide bond79 ↔ 103 By similarity
Disulfide bond97 ↔ 108 By similarity

Natural variations

Natural variant451G → C in FRFB. Ref.5
VAR_067343
Natural variant491G → S in FRFB. Ref.5
VAR_067344

Sequences

Sequence LengthMass (Da)Tools
P39877 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 0D17DC76E55F42BC

FASTA13815,674
        10         20         30         40         50         60 
MKGLLPLAWF LACSVPAVQG GLLDLKSMIE KVTGKNALTN YGFYGCYCGW GGRGTPKDGT 

        70         80         90        100        110        120 
DWCCWAHDHC YGRLEEKGCN IRTQSYKYRF AWGVVTCEPG PFCHVNLCAC DRKLVYCLKR 

       130 
NLRSYNPQYQ YFPNILCS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2."
Chen J., Engle S.J., Seilhamer J.J., Tischfield J.A.
J. Biol. Chem. 269:2365-2368(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Stomach.
[2]NIEHS SNPs program
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Biallelic mutations in PLA2G5, encoding group V phospholipase A2, cause benign fleck retina."
Sergouniotis P.I., Davidson A.E., Mackay D.S., Lenassi E., Li Z., Robson A.G., Yang X., Kam J.H., Isaacs T.W., Holder G.E., Jeffery G., Beck J.A., Moore A.T., Plagnol V., Webster A.R.
Am. J. Hum. Genet. 89:782-791(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, VARIANTS FRFB CYS-45 AND SER-49.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03090 mRNA. Translation: AAC28886.1.
AY524778 Genomic DNA. Translation: AAR92480.1.
AL158172 Genomic DNA. Translation: CAC13158.1.
BC036792 mRNA. Translation: AAH36792.2.
CCDSCCDS202.1.
PIRA49959.
RefSeqNP_000920.1. NM_000929.2.
XP_005245950.1. XM_005245893.2.
XP_005245952.1. XM_005245895.2.
XP_005245953.1. XM_005245896.1.
XP_006710755.1. XM_006710692.1.
XP_006710756.1. XM_006710693.1.
XP_006710757.1. XM_006710694.1.
XP_006710758.1. XM_006710695.1.
XP_006710759.1. XM_006710696.1.
UniGeneHs.319438.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GHNmodel-A21-138[»]
ProteinModelPortalP39877.
SMRP39877. Positions 22-138.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000364249.

Chemistry

BindingDBP39877.
ChEMBLCHEMBL4323.

Polymorphism databases

DMDM730258.

Proteomic databases

PaxDbP39877.
PRIDEP39877.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375108; ENSP00000364249; ENSG00000127472.
GeneID5322.
KEGGhsa:5322.
UCSCuc001bcx.3. human.

Organism-specific databases

CTD5322.
GeneCardsGC01P020354.
HGNCHGNC:9038. PLA2G5.
HPAHPA053361.
MIM228980. phenotype.
601192. gene.
neXtProtNX_P39877.
Orphanet363989. Familial benign flecked retina.
PharmGKBPA33366.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG330703.
HOGENOMHOG000231749.
HOVERGENHBG008137.
InParanoidP39877.
KOK01047.
OMACSSALEV.
OrthoDBEOG7N63PF.
PhylomeDBP39877.
TreeFamTF319283.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP39877.
CleanExHS_PLA2G5.
GenevestigatorP39877.

Family and domain databases

Gene3D1.20.90.10. 1 hit.
InterProIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERPTHR11716. PTHR11716. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMSSF48619. SSF48619. 1 hit.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPLA2G5.
GenomeRNAi5322.
NextBio20590.
PROP39877.
SOURCESearch...

Entry information

Entry namePA2G5_HUMAN
AccessionPrimary (citable) accession number: P39877
Secondary accession number(s): Q8N435
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM