Reviewed, UniProtKB/Swiss-Prot O15496 (PA2GX_HUMAN)

Names and origin

Protein names

Recommended name:
    Group 10 secretory phospholipase A2
    EC=3.1.1.4
Alternative name(s):
    Group X secretory phospholipase A2
      Short name=GX sPLA2
    Phosphatidylcholine 2-acylhydrolase GX
    sPLA2-X

Gene names

Name:

PLA2G10

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	165 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. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subcellular location	Secreted.
Tissue specificity	Found in spleen, thymus, peripheral blood leukocytes, pancreas, lung, and colon.
Sequence similarities	Belongs to the phospholipase A2 family.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	arachidonic acid metabolic process Non-traceable author statement. Source: UniProtKB axon guidance Inferred from direct assay. Source: MGI lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lysophospholipid transport Inferred from direct assay. Source: MGI phospholipid metabolic process Inferred from electronic annotation. Source: InterPro positive regulation of cellular protein metabolic process Inferred from mutant phenotype. Source: UniProtKB positive regulation of foam cell differentiation Inferred by curator. Source: UniProtKB positive regulation of lipid storage Inferred from mutant phenotype. Source: UniProtKB positive regulation of prostaglandin secretion Inferred from mutant phenotype. Source: UniProtKB regulation of macrophage activation Inferred from mutant phenotype. Source: UniProtKB
Cellular component	extracellular region Ref.1 Traceable author statement. Source: ProtInc
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase A2 activity Ref.1 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 – 31

31

Potential

Propeptide

32 – 42

11

Potential

PRO_0000022764

Chain

43 – 165

123

Group 10 secretory phospholipase A2

PRO_0000022765

Sites

Active site

88

1

By similarity

Active site

133

1

By similarity

Metal binding

68

1

Calcium; via carbonyl oxygen By similarity

Metal binding

70

1

Calcium; via carbonyl oxygen By similarity

Metal binding

72

1

Calcium; via carbonyl oxygen By similarity

Metal binding

89

1

Calcium By similarity

Amino acid modifications

Glycosylation

113

1

N-linked (GlcNAc...) Potential

Disulfide bond

53 ↔ 111

Potential

Disulfide bond

67 ↔ 157

By similarity

Disulfide bond

69 ↔ 85

By similarity

Disulfide bond

84 ↔ 139

By similarity

Disulfide bond

90 ↔ 164

By similarity

Disulfide bond

91 ↔ 132

By similarity

Disulfide bond

100 ↔ 125

By similarity

Disulfide bond

118 ↔ 130

By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

165

Helix Strand Turn

Details...

Helix

44 – 54

11

Beta strand

55 – 57

3

Helix

59 – 62

4

Beta strand

63 – 65

3

Turn

66 – 68

3

Beta strand

69 – 72

4

Helix

80 – 97

18

Turn

102 – 104

3

Beta strand

109 – 112

4

Beta strand

115 – 118

4

Helix

124 – 141

18

Helix

147 – 149

3

Helix

154 – 156

3

Sequences

	Sequence		Length	Mass (Da)
	O15496-1 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: AD197A164319F102	FASTA	165	18,153
	10 20 30 40 50 60 MGPLPVCLPI MLLLLLPSLL LLLLLPGPGS GEASRILRVH RRGILELAGT VGCVGPRTPI 70 80 90 100 110 120 AYMKYGCFCG LGGHGQPRDA IDWCCHGHDC CYTRAEEAGC SPKTERYSWQ CVNQSVLCGP 130 140 150 160 AENKCQELLC KCDQEIANCL AQTEYNLKYL FYPQFLCEPD SPKCD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2." Cupillard L., Koumanov K., Mattei M.-G., Lazdunski M., Lambeau G. J. Biol. Chem. 272:15745-15752(1997) [PubMed: 9188469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Lung.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed: 15616553] [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].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U95301 mRNA. Translation: AAB64410.1.
CR456885 mRNA. Translation: CAG33166.1.
AC009167 Genomic DNA. No translation available.
BC069539 mRNA. Translation: AAH69539.1.
BC106731 mRNA. Translation: AAI06732.1.
BC106732 mRNA. Translation: AAI06733.1.

IPI

IPI00216471.

RefSeq

NP_003552.1.

UniGene

Hs.567366

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LE6	X-ray	1.97	A/B/C	43-165	[»]
1LE7	X-ray	2.09	A/B	43-165	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O15496. 1 interaction.

Genome annotation databases

Ensembl

ENSG00000069764. Homo sapiens. [Contig view]

GeneID

8399.

KEGG

hsa:8399.

Organism-specific databases

GeneCards

GC16M014673.

H-InvDB

HIX0026959.
HIX0038631.

HGNC

HGNC:9029. PLA2G10.

MIM

603603. gene.

PharmGKB

PA33360.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O15496.

Enzyme and pathway databases

BRENDA

3.1.1.4. 247.

Gene expression databases

ArrayExpress

O15496.

Bgee

O15496.

CleanEx

HS_PLA2G10.

GermOnline

ENSG00000069764. Homo sapiens.

Family and domain databases

InterPro

IPR016090. Phospholipase_A2.
IPR013090. Phospholipase_A2_AS.
IPR001211. Phospholipase_A2_euk.
[Graphical view]

Gene3D

G3DSA:1.20.90.10. Phospholipase_A2. 1 hit.

PANTHER

PTHR11716. Phospholipase_A2. 1 hit.

Pfam

PF00068. Phospholip_A2_1. 1 hit.
[Graphical view]

PRINTS

PR00389. PHPHLIPASEA2.

ProDom

PD000303. PhospholipaseA2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00085. PA2c. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

31434.

SOURCE

Search...

Entry information

Entry name

PA2GX_HUMAN

Accession

Primary (citable) accession number: O15496
Secondary accession number(s): Q6NT23

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 16, 2009
Last modified:	June 16, 2009
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)