O15496 (PA2GX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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
Short name=sPLA2-X
Phosphatidylcholine 2-acylhydrolase 10

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. Ref.6
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 Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	arachidonic acid metabolic process Non-traceable author statement. Source: BHF-UCL axon guidance Inferred from direct assay. Source: MGI cholesterol homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lysophospholipid transport Inferred from direct assay. Source: MGI negative regulation of cholesterol efflux Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: BHF-UCL phospholipid metabolic process Inferred from electronic annotation. Source: InterPro positive regulation of arachidonic acid secretion Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cellular protein metabolic process Inferred from mutant phenotype. Source: BHF-UCL positive regulation of lipid storage Inferred from mutant phenotype. Source: BHF-UCL positive regulation of macrophage derived foam cell differentiation Inferred by curator. Source: BHF-UCL positive regulation of prostaglandin secretion Inferred from mutant phenotype. Source: BHF-UCL regulation of macrophage activation Inferred from mutant phenotype. Source: BHF-UCL
Cellular component	extracellular region Traceable author statement. Source: ProtInc
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro 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 – 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

Ref.6

Active site

133

1

Ref.6

Metal binding

68

1

Calcium; via carbonyl oxygen

Metal binding

70

1

Calcium; via carbonyl oxygen

Metal binding

72

1

Calcium; via carbonyl oxygen

Metal binding

89

1

Calcium

Amino acid modifications

Glycosylation

113

1

N-linked (GlcNAc...) Potential

Disulfide bond

53 ↔ 111

Ref.6

Disulfide bond

67 ↔ 157

Ref.6

Disulfide bond

69 ↔ 85

Ref.6

Disulfide bond

84 ↔ 139

Ref.6

Disulfide bond

90 ↔ 164

Ref.6

Disulfide bond

91 ↔ 132

Ref.6

Disulfide bond

100 ↔ 125

Ref.6

Disulfide bond

118 ↔ 130

Ref.6

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 [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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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].
[6]	"Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes." Pan Y.H., Yu B.Z., Singer A.G., Ghomashchi F., Lambeau G., Gelb M.H., Jain M.K., Bahnson B.J. J. Biol. Chem. 277:29086-29093(2002) [PubMed: 12161451] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 43-165, DISULFIDE BONDS, ACTIVE SITE, COFACTOR, CALCIUM-BINDING SITES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U95301 mRNA. Translation: AAB64410.1.
CR456885 mRNA. Translation: CAG33166.1.
AC009167 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85104.1.
BC069539 mRNA. Translation: AAH69539.1.
BC106731 mRNA. Translation: AAI06732.1.
BC106732 mRNA. Translation: AAI06733.1.
BC111804 mRNA. Translation: AAI11805.1.

IPI

IPI00216471.

RefSeq

NP_003552.1. NM_003561.1.

UniGene

Hs.567366.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O15496.

SMR

O15496. Positions 43-165.

ModBase

Search...

Protein-protein interaction databases

IntAct

O15496. 1 interaction.

MINT

MINT-1411106.

STRING

O15496.

Proteomic databases

PRIDE

O15496.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261659; ENSP00000261659; ENSG00000069764.
ENST00000438167; ENSP00000393847; ENSG00000069764.

GeneID

8399.

KEGG

hsa:8399.

UCSC

uc002dcq.1. human.

Organism-specific databases

CTD

8399.

GeneCards

GC16M014673.

H-InvDB

HIX0026959.
HIX0038631.

HGNC

HGNC:9029. PLA2G10.

HPA

HPA041893.

MIM

603603. gene.

neXtProt

NX_O15496.

PharmGKB

PA33360.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05538.

GeneTree

ENSGT00550000074218.

HOGENOM

HBG715293.

HOVERGEN

HBG008137.

InParanoid

O15496.

OMA

ELLCKCD.

OrthoDB

EOG4GMTZ6.

PhylomeDB

O15496.

Gene expression databases

ArrayExpress

O15496.

Bgee

O15496.

CleanEx

HS_PLA2G10.

Genevestigator

O15496.

GermOnline

ENSG00000069764. 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

31434.

SOURCE

Search...

Entry information

Entry name

PA2GX_HUMAN

Accession

Primary (citable) accession number: O15496
Secondary accession number(s): Q14DU3, Q6NT23

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 16, 2009
Last modified:	November 16, 2011
This is version 116 of the entry and version 3 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.