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P39877 (PA2G5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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)
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.

Post-translational modification

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

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
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Traceable author statement. Source: ProtInc

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipase A2 activity

Traceable author statement. Source: ProtInc

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

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: 8300559] [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: 16710414] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
+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.
IPIIPI00026664.
PIRA49959.
RefSeqNP_000920.1. NM_000929.2.
UniGeneHs.319438.

3D structure databases

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

Protein-protein interaction databases

STRINGP39877.

Polymorphism databases

DMDM730258.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375108; ENSP00000364249; ENSG00000127472.
GeneID5322.
KEGGhsa:5322.
UCSCuc001bcx.1. human.

Organism-specific databases

CTD5322.
GeneCardsGC01P020354.
H-InvDBHIX0021440.
HGNCHGNC:9038. PLA2G5.
MIM601192. gene.
neXtProtNX_P39877.
PharmGKBPA33366.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG21474.
GeneTreeENSGT00550000074218.
HOGENOMHBG715293.
HOVERGENHBG008137.
InParanoidP39877.
OMAVYCLKRN.
OrthoDBEOG4NKBWW.
PhylomeDBP39877.

Gene expression databases

ArrayExpressP39877.
BgeeP39877.
CleanExHS_PLA2G5.
GenevestigatorP39877.
GermOnlineENSG00000127472. Homo sapiens.

Family and domain databases

InterProIPR016090. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR001211. PLipase_A2_euk.
[Graphical view]
Gene3DG3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
KOK01047.
PANTHERPTHR11716. Phospholipase_A2. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMSSF48619. PhospholipaseA2. 1 hit.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20590.
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: January 25, 2012
This is version 114 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

Human chromosome 1

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families