ID PA2GX_HUMAN Reviewed; 165 AA. AC O15496; Q14DU3; Q6NT23; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 3. DT 13-FEB-2019, entry version 177. DE RecName: Full=Group 10 secretory phospholipase A2; DE EC=3.1.1.4; DE AltName: Full=Group X secretory phospholipase A2; DE Short=GX sPLA2; DE Short=sPLA2-X; DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 10; DE Flags: Precursor; GN Name=PLA2G10; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Lung; RX PubMed=9188469; DOI=10.1074/jbc.272.25.15745; RA Cupillard L., Koumanov K., Mattei M.-G., Lazdunski M., Lambeau G.; RT "Cloning, chromosomal mapping, and expression of a novel human RT secretory phospholipase A2."; RL J. Biol. Chem. 272:15745-15752(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 43-165, DISULFIDE BONDS, RP ACTIVE SITE, COFACTOR, CALCIUM-BINDING SITES, AND FUNCTION. RX PubMed=12161451; DOI=10.1074/jbc.M202531200; RA Pan Y.H., Yu B.Z., Singer A.G., Ghomashchi F., Lambeau G., Gelb M.H., RA Jain M.K., Bahnson B.J.; RT "Crystal structure of human group X secreted phospholipase A2. RT Electrostatically neutral interfacial surface targets zwitterionic RT membranes."; RL J. Biol. Chem. 277:29086-29093(2002). CC -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2- CC acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for CC releasing arachidonic acid from cell membrane phospholipids. CC Prefers phosphatidylethanolamine and phosphatidylcholine liposomes CC to those of phosphatidylserine. {ECO:0000269|PubMed:12161451, CC ECO:0000269|PubMed:9188469}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1- CC acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); CC Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; CC EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, CC ECO:0000255|PROSITE-ProRule:PRU10036}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:12161451}; CC Note=Binds 1 Ca(2+) ion per subunit. CC {ECO:0000269|PubMed:12161451}; CC -!- INTERACTION: CC Q0VD86:INCA1; NbExp=4; IntAct=EBI-726466, EBI-6509505; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9188469}. CC -!- TISSUE SPECIFICITY: Found in spleen, thymus, peripheral blood CC leukocytes, pancreas, lung, and colon. CC {ECO:0000269|PubMed:9188469}. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; U95301; AAB64410.1; -; mRNA. DR EMBL; CR456885; CAG33166.1; -; mRNA. DR EMBL; AC009167; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471112; EAW85104.1; -; Genomic_DNA. DR EMBL; BC069539; AAH69539.1; -; mRNA. DR EMBL; BC106731; AAI06732.1; -; mRNA. DR EMBL; BC106732; AAI06733.1; -; mRNA. DR EMBL; BC111804; AAI11805.1; -; mRNA. DR CCDS; CCDS10555.1; -. DR RefSeq; NP_003552.1; NM_003561.2. DR UniGene; Hs.567366; -. DR PDB; 1LE6; X-ray; 1.97 A; A/B/C=43-165. DR PDB; 1LE7; X-ray; 2.09 A; A/B=43-165. DR PDB; 4UY1; X-ray; 2.20 A; A/B=43-165. DR PDB; 5G3M; X-ray; 1.85 A; A/B=43-165. DR PDB; 5OW8; X-ray; 1.90 A; A/B=43-165. DR PDB; 5OWC; X-ray; 1.75 A; A/B=43-164. DR PDB; 6G5J; X-ray; 1.85 A; A/B=1-165. DR PDBsum; 1LE6; -. DR PDBsum; 1LE7; -. DR PDBsum; 4UY1; -. DR PDBsum; 5G3M; -. DR PDBsum; 5OW8; -. DR PDBsum; 5OWC; -. DR PDBsum; 6G5J; -. DR ProteinModelPortal; O15496; -. DR SMR; O15496; -. DR BioGrid; 113987; 57. DR IntAct; O15496; 48. DR STRING; 9606.ENSP00000393847; -. DR BindingDB; O15496; -. DR ChEMBL; CHEMBL4342; -. DR GuidetoPHARMACOLOGY; 1422; -. DR SwissLipids; SLP:000001084; -. DR iPTMnet; O15496; -. DR BioMuta; PLA2G10; -. DR jPOST; O15496; -. DR PaxDb; O15496; -. DR PeptideAtlas; O15496; -. DR PRIDE; O15496; -. DR ProteomicsDB; 48696; -. DR Ensembl; ENST00000438167; ENSP00000393847; ENSG00000069764. DR Ensembl; ENST00000621727; ENSP00000479397; ENSG00000276870. DR GeneID; 8399; -. DR KEGG; hsa:8399; -. DR UCSC; uc002dcq.4; human. DR CTD; 8399; -. DR DisGeNET; 8399; -. DR EuPathDB; HostDB:ENSG00000069764.9; -. DR GeneCards; PLA2G10; -. DR H-InvDB; HIX0026959; -. DR HGNC; HGNC:9029; PLA2G10. DR HPA; HPA041893; -. DR MIM; 603603; gene. DR neXtProt; NX_O15496; -. DR OpenTargets; ENSG00000069764; -. DR PharmGKB; PA33360; -. DR eggNOG; KOG4087; Eukaryota. DR eggNOG; ENOG411283D; LUCA. DR GeneTree; ENSGT00940000157803; -. DR HOGENOM; HOG000231749; -. DR HOVERGEN; HBG008137; -. DR InParanoid; O15496; -. DR KO; K01047; -. DR OMA; EIAYCLA; -. DR OrthoDB; 1422829at2759; -. DR PhylomeDB; O15496; -. DR TreeFam; TF319283; -. DR BRENDA; 3.1.1.4; 2681. DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC. DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS. DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE. DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI. DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG. DR Reactome; R-HSA-1483166; Synthesis of PA. DR EvolutionaryTrace; O15496; -. DR GeneWiki; PLA2G10; -. DR GenomeRNAi; 8399; -. DR PRO; PR:O15496; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000069764; Expressed in 101 organ(s), highest expression level in sigmoid colon. DR ExpressionAtlas; O15496; baseline and differential. DR Genevisible; O15496; HS. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central. DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central. DR GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC. DR GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC. DR GO; GO:0004620; F:phospholipase activity; ISS:BHF-UCL. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0019369; P:arachidonic acid metabolic process; NAS:BHF-UCL. DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro. DR GO; GO:0007411; P:axon guidance; IDA:MGI. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IBA:GO_Central. DR GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0051977; P:lysophospholipid transport; IDA:MGI. DR GO; GO:0090370; P:negative regulation of cholesterol efflux; ISS:BHF-UCL. DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL. DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome. DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome. DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome. DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome. DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; TAS:Reactome. DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome. DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central. DR GO; GO:0090238; P:positive regulation of arachidonic acid secretion; ISS:BHF-UCL. DR GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IMP:BHF-UCL. DR GO; GO:0010884; P:positive regulation of lipid storage; IMP:BHF-UCL. DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IC:BHF-UCL. DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; IMP:BHF-UCL. DR GO; GO:0043030; P:regulation of macrophage activation; IMP:BHF-UCL. DR CDD; cd00125; PLA2c; 1. DR Gene3D; 1.20.90.10; -; 1. DR InterPro; IPR001211; PLipase_A2. DR InterPro; IPR033112; PLipase_A2_Asp_AS. DR InterPro; IPR016090; PLipase_A2_dom. DR InterPro; IPR036444; PLipase_A2_dom_sf. DR InterPro; IPR033113; PLipase_A2_His_AS. DR PANTHER; PTHR11716; PTHR11716; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SMART; SM00085; PA2c; 1. DR SUPFAM; SSF48619; SSF48619; 1. DR PROSITE; PS00119; PA2_ASP; 1. DR PROSITE; PS00118; PA2_HIS; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cleavage on pair of basic residues; KW Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; KW Lipid degradation; Lipid metabolism; Metal-binding; KW Reference proteome; Secreted; Signal. FT SIGNAL 1 31 {ECO:0000255}. FT PROPEP 32 42 {ECO:0000255}. FT /FTId=PRO_0000022764. FT CHAIN 43 165 Group 10 secretory phospholipase A2. FT /FTId=PRO_0000022765. FT ACT_SITE 88 88 {ECO:0000269|PubMed:12161451}. FT ACT_SITE 133 133 {ECO:0000269|PubMed:12161451}. FT METAL 68 68 Calcium; via carbonyl oxygen. FT METAL 70 70 Calcium; via carbonyl oxygen. FT METAL 72 72 Calcium; via carbonyl oxygen. FT METAL 89 89 Calcium. FT CARBOHYD 113 113 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 53 111 {ECO:0000269|PubMed:12161451}. FT DISULFID 67 157 {ECO:0000269|PubMed:12161451}. FT DISULFID 69 85 {ECO:0000269|PubMed:12161451}. FT DISULFID 84 139 {ECO:0000269|PubMed:12161451}. FT DISULFID 90 164 {ECO:0000269|PubMed:12161451}. FT DISULFID 91 132 {ECO:0000269|PubMed:12161451}. FT DISULFID 100 125 {ECO:0000269|PubMed:12161451}. FT DISULFID 118 130 {ECO:0000269|PubMed:12161451}. FT HELIX 44 54 {ECO:0000244|PDB:5OWC}. FT STRAND 55 57 {ECO:0000244|PDB:5OWC}. FT HELIX 59 62 {ECO:0000244|PDB:5OWC}. FT STRAND 63 65 {ECO:0000244|PDB:5OWC}. FT TURN 66 68 {ECO:0000244|PDB:5OWC}. FT STRAND 69 72 {ECO:0000244|PDB:5OWC}. FT HELIX 80 97 {ECO:0000244|PDB:5OWC}. FT TURN 102 104 {ECO:0000244|PDB:5OWC}. FT STRAND 109 112 {ECO:0000244|PDB:5OWC}. FT STRAND 115 118 {ECO:0000244|PDB:5OWC}. FT HELIX 124 141 {ECO:0000244|PDB:5OWC}. FT HELIX 147 149 {ECO:0000244|PDB:5OWC}. FT HELIX 154 156 {ECO:0000244|PDB:5OWC}. SQ SEQUENCE 165 AA; 18153 MW; AD197A164319F102 CRC64; MGPLPVCLPI MLLLLLPSLL LLLLLPGPGS GEASRILRVH RRGILELAGT VGCVGPRTPI AYMKYGCFCG LGGHGQPRDA IDWCCHGHDC CYTRAEEAGC SPKTERYSWQ CVNQSVLCGP AENKCQELLC KCDQEIANCL AQTEYNLKYL FYPQFLCEPD SPKCD //