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Protein

Calcium-dependent phospholipase A2

Gene

PLA2G5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

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

pH dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Calcium; via carbonyl oxygenBy similarity
Metal bindingi49 – 491Calcium; via carbonyl oxygenBy similarity
Metal bindingi51 – 511Calcium; via carbonyl oxygenBy similarity
Active sitei67 – 671By similarity
Metal bindingi68 – 681CalciumBy similarity
Active sitei111 – 1111By similarity

GO - Molecular functioni

  1. calcium-dependent phospholipase A2 activity Source: ProtInc
  2. calcium ion binding Source: InterPro
  3. heparin binding Source: Ensembl

GO - Biological processi

  1. arachidonic acid secretion Source: Ensembl
  2. glycerophospholipid biosynthetic process Source: Reactome
  3. leukotriene biosynthetic process Source: Ensembl
  4. lipid catabolic process Source: UniProtKB-KW
  5. phosphatidic acid biosynthetic process Source: Reactome
  6. phosphatidylcholine acyl-chain remodeling Source: Reactome
  7. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
  8. phosphatidylglycerol acyl-chain remodeling Source: Reactome
  9. phosphatidylinositol acyl-chain remodeling Source: Reactome
  10. phosphatidylserine acyl-chain remodeling Source: Reactome
  11. phospholipid metabolic process Source: Reactome
  12. platelet activating factor biosynthetic process Source: Ensembl
  13. response to cAMP Source: Ensembl
  14. response to cytokine Source: Ensembl
  15. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_120722. Acyl chain remodelling of PI.
REACT_120829. Acyl chain remodelling of PC.
REACT_120906. Synthesis of PA.
REACT_121324. Acyl chain remodelling of PG.
REACT_121369. Acyl chain remodelling of PE.
REACT_121384. Acyl chain remodelling of PS.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-dependent phospholipase A2 (EC:3.1.1.4)
Alternative name(s):
Group V phospholipase A2
PLA2-10
Phosphatidylcholine 2-acylhydrolase 5
Gene namesi
Name:PLA2G5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9038. PLA2G5.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. extracellular region Source: Reactome
  3. Golgi apparatus Source: Ensembl
  4. perinuclear region of cytoplasm Source: Ensembl
  5. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Fleck retina, familial benign (FRFB)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:228980
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451G → C in FRFB. 1 Publication
VAR_067343
Natural varianti49 – 491G → S in FRFB. 1 Publication
VAR_067344

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi228980. phenotype.
Orphaneti363989. Familial benign flecked retina.
PharmGKBiPA33366.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 138118Calcium-dependent phospholipase A2PRO_0000022761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 137By similarity
Disulfide bondi48 ↔ 64By similarity
Disulfide bondi63 ↔ 117By similarity
Disulfide bondi70 ↔ 110By similarity
Disulfide bondi79 ↔ 103By similarity
Disulfide bondi97 ↔ 108By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP39877.
PRIDEiP39877.

Expressioni

Tissue specificityi

Heart, placenta and less abundantly, in lung. Detected in the outer and inner plexiform layers of the retina (at protein level).1 Publication

Gene expression databases

BgeeiP39877.
CleanExiHS_PLA2G5.
GenevestigatoriP39877.

Organism-specific databases

HPAiHPA053361.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000364249.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GHNmodel-A21-138[»]
ProteinModelPortaliP39877.
SMRiP39877. Positions 22-138.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG330703.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP39877.
KOiK01047.
OMAiGTDWCCW.
OrthoDBiEOG7N63PF.
PhylomeDBiP39877.
TreeFamiTF319283.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39877-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGLLPLAWF LACSVPAVQG GLLDLKSMIE KVTGKNALTN YGFYGCYCGW
60 70 80 90 100
GGRGTPKDGT DWCCWAHDHC YGRLEEKGCN IRTQSYKYRF AWGVVTCEPG
110 120 130
PFCHVNLCAC DRKLVYCLKR NLRSYNPQYQ YFPNILCS
Length:138
Mass (Da):15,674
Last modified:February 1, 1995 - v1
Checksum:i0D17DC76E55F42BC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451G → C in FRFB. 1 Publication
VAR_067343
Natural varianti49 – 491G → S in FRFB. 1 Publication
VAR_067344

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03090 mRNA. Translation: AAC28886.1.
AY524778 Genomic DNA. Translation: AAR92480.1.
AL158172 Genomic DNA. Translation: CAC13158.1.
BC036792 mRNA. Translation: AAH36792.2.
CCDSiCCDS202.1.
PIRiA49959.
RefSeqiNP_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.
UniGeneiHs.319438.

Genome annotation databases

EnsembliENST00000375108; ENSP00000364249; ENSG00000127472.
GeneIDi5322.
KEGGihsa:5322.
UCSCiuc001bcx.3. human.

Polymorphism databases

DMDMi730258.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03090 mRNA. Translation: AAC28886.1.
AY524778 Genomic DNA. Translation: AAR92480.1.
AL158172 Genomic DNA. Translation: CAC13158.1.
BC036792 mRNA. Translation: AAH36792.2.
CCDSiCCDS202.1.
PIRiA49959.
RefSeqiNP_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.
UniGeneiHs.319438.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GHNmodel-A21-138[»]
ProteinModelPortaliP39877.
SMRiP39877. Positions 22-138.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000364249.

Chemistry

BindingDBiP39877.
ChEMBLiCHEMBL4323.

Polymorphism databases

DMDMi730258.

Proteomic databases

PaxDbiP39877.
PRIDEiP39877.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375108; ENSP00000364249; ENSG00000127472.
GeneIDi5322.
KEGGihsa:5322.
UCSCiuc001bcx.3. human.

Organism-specific databases

CTDi5322.
GeneCardsiGC01P020354.
HGNCiHGNC:9038. PLA2G5.
HPAiHPA053361.
MIMi228980. phenotype.
601192. gene.
neXtProtiNX_P39877.
Orphaneti363989. Familial benign flecked retina.
PharmGKBiPA33366.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG330703.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP39877.
KOiK01047.
OMAiGTDWCCW.
OrthoDBiEOG7N63PF.
PhylomeDBiP39877.
TreeFamiTF319283.

Enzyme and pathway databases

ReactomeiREACT_120722. Acyl chain remodelling of PI.
REACT_120829. Acyl chain remodelling of PC.
REACT_120906. Synthesis of PA.
REACT_121324. Acyl chain remodelling of PG.
REACT_121369. Acyl chain remodelling of PE.
REACT_121384. Acyl chain remodelling of PS.

Miscellaneous databases

GeneWikiiPLA2G5.
GenomeRNAii5322.
NextBioi20590.
PROiP39877.
SOURCEiSearch...

Gene expression databases

BgeeiP39877.
CleanExiHS_PLA2G5.
GenevestigatoriP39877.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Stomach.
  2. NIEHS SNPs program
    Submitted (DEC-2003) 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.
    , 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(2005) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. Cited for: TISSUE SPECIFICITY, VARIANTS FRFB CYS-45 AND SER-49.

Entry informationi

Entry nameiPA2G5_HUMAN
AccessioniPrimary (citable) accession number: P39877
Secondary accession number(s): Q8N435
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.