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O15496

- PA2GX_HUMAN

UniProt

O15496 - PA2GX_HUMAN

Protein

Group 10 secretory phospholipase A2

Gene

PLA2G10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    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 activityi

    Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

    Cofactori

    Binds 1 calcium ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi68 – 681Calcium; via carbonyl oxygen
    Metal bindingi70 – 701Calcium; via carbonyl oxygen
    Metal bindingi72 – 721Calcium; via carbonyl oxygen
    Active sitei88 – 8811 Publication
    Metal bindingi89 – 891Calcium
    Active sitei133 – 13311 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. phospholipase A2 activity Source: ProtInc
    3. phospholipase activity Source: BHF-UCL

    GO - Biological processi

    1. arachidonic acid metabolic process Source: BHF-UCL
    2. axon guidance Source: MGI
    3. cholesterol homeostasis Source: BHF-UCL
    4. glycerophospholipid biosynthetic process Source: Reactome
    5. lipid catabolic process Source: UniProtKB-KW
    6. lysophospholipid transport Source: MGI
    7. negative regulation of cholesterol efflux Source: BHF-UCL
    8. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    9. phosphatidic acid biosynthetic process Source: Reactome
    10. phosphatidylcholine acyl-chain remodeling Source: Reactome
    11. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
    12. phosphatidylglycerol acyl-chain remodeling Source: Reactome
    13. phosphatidylinositol acyl-chain remodeling Source: Reactome
    14. phosphatidylserine acyl-chain remodeling Source: Reactome
    15. phospholipid metabolic process Source: Reactome
    16. positive regulation of arachidonic acid secretion Source: BHF-UCL
    17. positive regulation of cellular protein metabolic process Source: BHF-UCL
    18. positive regulation of lipid storage Source: BHF-UCL
    19. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
    20. positive regulation of prostaglandin secretion Source: BHF-UCL
    21. regulation of macrophage activation Source: BHF-UCL
    22. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_120722. Acyl chain remodelling of PI.
    REACT_120829. Acyl chain remodelling of PC.
    REACT_120906. Synthesis of PA.
    REACT_121324. Acyl chain remodelling of PG.
    REACT_121369. Acyl chain remodelling of PE.
    REACT_121384. Acyl chain remodelling of PS.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:PLA2G10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:9029. PLA2G10.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33360.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Propeptidei32 – 4211Sequence AnalysisPRO_0000022764Add
    BLAST
    Chaini43 – 165123Group 10 secretory phospholipase A2PRO_0000022765Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi53 ↔ 1111 Publication
    Disulfide bondi67 ↔ 1571 Publication
    Disulfide bondi69 ↔ 851 Publication
    Disulfide bondi84 ↔ 1391 Publication
    Disulfide bondi90 ↔ 1641 Publication
    Disulfide bondi91 ↔ 1321 Publication
    Disulfide bondi100 ↔ 1251 Publication
    Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi118 ↔ 1301 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO15496.
    PRIDEiO15496.

    Expressioni

    Tissue specificityi

    Found in spleen, thymus, peripheral blood leukocytes, pancreas, lung, and colon.

    Gene expression databases

    ArrayExpressiO15496.
    BgeeiO15496.
    CleanExiHS_PLA2G10.
    GenevestigatoriO15496.

    Organism-specific databases

    HPAiHPA041893.

    Interactioni

    Protein-protein interaction databases

    IntActiO15496. 1 interaction.
    MINTiMINT-1411106.
    STRINGi9606.ENSP00000393847.

    Structurei

    Secondary structure

    1
    165
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi44 – 5411
    Beta strandi55 – 573
    Helixi59 – 624
    Beta strandi63 – 653
    Turni66 – 683
    Beta strandi69 – 724
    Helixi80 – 9718
    Turni102 – 1043
    Beta strandi109 – 1124
    Beta strandi115 – 1184
    Helixi124 – 14118
    Helixi147 – 1493
    Helixi154 – 1563

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LE6X-ray1.97A/B/C43-165[»]
    1LE7X-ray2.09A/B43-165[»]
    ProteinModelPortaliO15496.
    SMRiO15496. Positions 43-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15496.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phospholipase A2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG284162.
    HOGENOMiHOG000231749.
    HOVERGENiHBG008137.
    InParanoidiO15496.
    KOiK01047.
    OMAiCQELLCK.
    OrthoDBiEOG7N63PF.
    PhylomeDBiO15496.
    TreeFamiTF319283.

    Family and domain databases

    Gene3Di1.20.90.10. 1 hit.
    InterProiIPR001211. PLipase_A2.
    IPR013090. PLipase_A2_AS.
    IPR016090. PLipase_A2_dom.
    [Graphical view]
    PANTHERiPTHR11716. PTHR11716. 1 hit.
    PfamiPF00068. Phospholip_A2_1. 1 hit.
    [Graphical view]
    PRINTSiPR00389. PHPHLIPASEA2.
    SMARTiSM00085. PA2c. 1 hit.
    [Graphical view]
    SUPFAMiSSF48619. SSF48619. 1 hit.
    PROSITEiPS00119. PA2_ASP. 1 hit.
    PS00118. PA2_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O15496-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPLPVCLPI MLLLLLPSLL LLLLLPGPGS GEASRILRVH RRGILELAGT    50
    VGCVGPRTPI AYMKYGCFCG LGGHGQPRDA IDWCCHGHDC CYTRAEEAGC 100
    SPKTERYSWQ CVNQSVLCGP AENKCQELLC KCDQEIANCL AQTEYNLKYL 150
    FYPQFLCEPD SPKCD 165
    Length:165
    Mass (Da):18,153
    Last modified:June 16, 2009 - v3
    Checksum:iAD197A164319F102
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS10555.1.
    RefSeqiNP_003552.1. NM_003561.1.
    XP_006721021.1. XM_006720958.1.
    XP_006725277.1. XM_006725214.1.
    UniGeneiHs.567366.

    Genome annotation databases

    EnsembliENST00000438167; ENSP00000393847; ENSG00000069764.
    GeneIDi8399.
    KEGGihsa:8399.
    UCSCiuc002dcq.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS10555.1.
    RefSeqi NP_003552.1. NM_003561.1.
    XP_006721021.1. XM_006720958.1.
    XP_006725277.1. XM_006725214.1.
    UniGenei Hs.567366.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali O15496.
    SMRi O15496. Positions 43-165.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O15496. 1 interaction.
    MINTi MINT-1411106.
    STRINGi 9606.ENSP00000393847.

    Chemistry

    BindingDBi O15496.
    ChEMBLi CHEMBL4342.

    Proteomic databases

    PaxDbi O15496.
    PRIDEi O15496.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000438167 ; ENSP00000393847 ; ENSG00000069764 .
    GeneIDi 8399.
    KEGGi hsa:8399.
    UCSCi uc002dcq.3. human.

    Organism-specific databases

    CTDi 8399.
    GeneCardsi GC16M014767.
    H-InvDB HIX0026959.
    HGNCi HGNC:9029. PLA2G10.
    HPAi HPA041893.
    MIMi 603603. gene.
    neXtProti NX_O15496.
    PharmGKBi PA33360.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG284162.
    HOGENOMi HOG000231749.
    HOVERGENi HBG008137.
    InParanoidi O15496.
    KOi K01047.
    OMAi CQELLCK.
    OrthoDBi EOG7N63PF.
    PhylomeDBi O15496.
    TreeFami TF319283.

    Enzyme and pathway databases

    Reactomei REACT_120722. Acyl chain remodelling of PI.
    REACT_120829. Acyl chain remodelling of PC.
    REACT_120906. Synthesis of PA.
    REACT_121324. Acyl chain remodelling of PG.
    REACT_121369. Acyl chain remodelling of PE.
    REACT_121384. Acyl chain remodelling of PS.

    Miscellaneous databases

    EvolutionaryTracei O15496.
    GeneWikii PLA2G10.
    GenomeRNAii 8399.
    NextBioi 31434.
    PROi O15496.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15496.
    Bgeei O15496.
    CleanExi HS_PLA2G10.
    Genevestigatori O15496.

    Family and domain databases

    Gene3Di 1.20.90.10. 1 hit.
    InterProi IPR001211. PLipase_A2.
    IPR013090. PLipase_A2_AS.
    IPR016090. PLipase_A2_dom.
    [Graphical view ]
    PANTHERi PTHR11716. PTHR11716. 1 hit.
    Pfami PF00068. Phospholip_A2_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00389. PHPHLIPASEA2.
    SMARTi SM00085. PA2c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48619. SSF48619. 1 hit.
    PROSITEi PS00119. PA2_ASP. 1 hit.
    PS00118. PA2_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 43-165, DISULFIDE BONDS, ACTIVE SITE, COFACTOR, CALCIUM-BINDING SITES.

    Entry informationi

    Entry nameiPA2GX_HUMAN
    AccessioniPrimary (citable) accession number: O15496
    Secondary accession number(s): Q14DU3, Q6NT23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3