P39877 (PA2G5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

PLA2G5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	138 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Traceable author statement. Source: ProtInc
Molecular function	calcium 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 138	118	Calcium-dependent phospholipase A2		PRO_0000022761
Sites
	Active site	67	1	By similarity
	Active site	111	1	By similarity
	Metal binding	47	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	49	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	51	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	68	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	46 ↔ 137		By similarity
	Disulfide bond	48 ↔ 64		By similarity
	Disulfide bond	63 ↔ 117		By similarity
	Disulfide bond	70 ↔ 110		By similarity
	Disulfide bond	79 ↔ 103		By similarity
	Disulfide bond	97 ↔ 108		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P39877 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 0D17DC76E55F42BC	FASTA	138	15,674
	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

References

	« Hide 'large scale' referencesShow '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. , 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

NIEHS-SNPs

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.

IPI

IPI00026664.

PIR

A49959.

RefSeq

NP_000920.1. NM_000929.2.

UniGene

Hs.319438.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GHN	model	-	A	21-138	[»]

ProteinModelPortal

P39877.

SMR

P39877. Positions 22-138.

ModBase

Search...

Protein-protein interaction databases

STRING

P39877.

Polymorphism databases

DMDM

730258.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375108; ENSP00000364249; ENSG00000127472.

GeneID

5322.

KEGG

hsa:5322.

UCSC

uc001bcx.1. human.

Organism-specific databases

CTD

5322.

GeneCards

GC01P020354.

H-InvDB

HIX0021440.

HGNC

HGNC:9038. PLA2G5.

MIM

601192. gene.

neXtProt

NX_P39877.

PharmGKB

PA33366.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG21474.

GeneTree

ENSGT00550000074218.

HOGENOM

HBG715293.

HOVERGEN

HBG008137.

InParanoid

P39877.

OMA

VYCLKRN.

OrthoDB

EOG4NKBWW.

PhylomeDB

P39877.

Gene expression databases

ArrayExpress

P39877.

Bgee

P39877.

CleanEx

HS_PLA2G5.

Genevestigator

P39877.

GermOnline

ENSG00000127472. Homo sapiens.

Family and domain databases

InterPro

IPR016090. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR001211. PLipase_A2_euk.
[Graphical view]

Gene3D

G3DSA:1.20.90.10. Phospholipase_A2. 1 hit.

KO

K01047.

PANTHER

PTHR11716. Phospholipase_A2. 1 hit.

Pfam

PF00068. Phospholip_A2_1. 1 hit.
[Graphical view]

PRINTS

PR00389. PHPHLIPASEA2.

SMART

SM00085. PA2c. 1 hit.
[Graphical view]

SUPFAM

SSF48619. PhospholipaseA2. 1 hit.

PROSITE

PS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

20590.

SOURCE

Search...

Entry information

Entry name

PA2G5_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.