Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot O15496 (PA2GX_HUMAN)

Last modified June 16, 2009. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length165 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. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Propeptide32 – 4211 Potential
PRO_0000022764
Chain43 – 165123Group 10 secretory phospholipase A2
PRO_0000022765

Sites

Active site881 By similarity
Active site1331 By similarity
Metal binding681Calcium; via carbonyl oxygen By similarity
Metal binding701Calcium; via carbonyl oxygen By similarity
Metal binding721Calcium; via carbonyl oxygen By similarity
Metal binding891Calcium By similarity

Amino acid modifications

Glycosylation1131N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 111 Potential
Disulfide bond67 ↔ 157 By similarity
Disulfide bond69 ↔ 85 By similarity
Disulfide bond84 ↔ 139 By similarity
Disulfide bond90 ↔ 164 By similarity
Disulfide bond91 ↔ 132 By similarity
Disulfide bond100 ↔ 125 By similarity
Disulfide bond118 ↔ 130 By similarity

Secondary structure

....................... 165
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15496-1 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: AD197A164319F102

FASTA16518,153
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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

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.
IPIIPI00216471.
RefSeqNP_003552.1.
UniGeneHs.567366

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1LE6X-ray1.97A/B/C43-165[»]
1LE7X-ray2.09A/B43-165[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO15496. 1 interaction.

Genome annotation databases

EnsemblENSG00000069764. Homo sapiens. [Contig view]
GeneID8399.
KEGGhsa:8399.

Organism-specific databases

GeneCardsGC16M014673.
H-InvDBHIX0026959.
HIX0038631.
HGNCHGNC:9029. PLA2G10.
MIM603603. gene.
PharmGKBPA33360.
GenAtlasSearch...

Phylogenomic databases

HOVERGENO15496.

Enzyme and pathway databases

BRENDA3.1.1.4. 247.

Gene expression databases

ArrayExpressO15496.
BgeeO15496.
CleanExHS_PLA2G10.
GermOnlineENSG00000069764. Homo sapiens.

Family and domain databases

InterProIPR016090. Phospholipase_A2.
IPR013090. Phospholipase_A2_AS.
IPR001211. Phospholipase_A2_euk.
[Graphical view]
Gene3DG3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
PANTHERPTHR11716. Phospholipase_A2. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
ProDomPD000303. PhospholipaseA2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio31434.
SOURCESearch...

Entry information

Entry namePA2GX_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 16

Human chromosome 16: 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents