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Q5R8A5

- PA24A_PONAB

UniProt

Q5R8A5 - PA24A_PONAB

Protein

Cytosolic phospholipase A2

Gene

PLA2G4A

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response By similarity.By similarity

    Catalytic activityi

    Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
    2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

    Enzyme regulationi

    Stimulated by agonists such as ATP, EGF, thrombin and bradykinin as well as by cytosolic Ca2+.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi40 – 401Calcium 1By similarity
    Metal bindingi40 – 401Calcium 2By similarity
    Metal bindingi41 – 411Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi43 – 431Calcium 1By similarity
    Metal bindingi43 – 431Calcium 2By similarity
    Metal bindingi65 – 651Calcium 1By similarity
    Metal bindingi93 – 931Calcium 2By similarity
    Metal bindingi94 – 941Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi95 – 951Calcium 2By similarity
    Active sitei228 – 2281NucleophileBy similarity
    Active sitei549 – 5491Proton acceptorBy similarity

    GO - Molecular functioni

    1. calcium-dependent phospholipid binding Source: UniProtKB
    2. calcium ion binding Source: UniProtKB
    3. lysophospholipase activity Source: UniProtKB-EC
    4. phospholipase A2 activity Source: UniProtKB-EC

    GO - Biological processi

    1. phospholipid catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosolic phospholipase A2
    Short name:
    cPLA2
    Alternative name(s):
    Phospholipase A2 group IVA
    Including the following 2 domains:
    Phospholipase A2 (EC:3.1.1.4)
    Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    Lysophospholipase (EC:3.1.1.5)
    Gene namesi
    Name:PLA2G4A
    Synonyms:CPLA2, PLA2G4
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmic vesicle By similarity
    Note: Translocates to membrane vesicles in a calcium-dependent fashion.By similarity

    GO - Cellular componenti

    1. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 749749Cytosolic phospholipase A2PRO_0000345134Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei268 – 2681PhosphothreonineBy similarity
    Modified residuei437 – 4371PhosphoserineBy similarity
    Modified residuei505 – 5051Phosphoserine; by MAPKBy similarity
    Modified residuei727 – 7271PhosphoserineBy similarity
    Modified residuei729 – 7291PhosphoserineBy similarity

    Post-translational modificationi

    Activated by phosphorylation at both Ser-505 and Ser-727.By similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Interacts with KAT5.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R8A5.
    SMRiQ5R8A5. Positions 13-721.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 106102C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini140 – 740601PLA2cPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 178178Phospholipid bindingBy similarityAdd
    BLAST

    Domaini

    The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca2+ By similarity.By similarity

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 PLA2c domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOGENOMiHOG000115420.
    HOVERGENiHBG053479.
    InParanoidiQ5R8A5.
    KOiK16342.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR016035. Acyl_Trfase/lysoPLipase.
    IPR000008. C2_dom.
    IPR002642. LysoPLipase_cat_dom.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF01735. PLA2_B. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 1 hit.
    SM00022. PLAc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF52151. SSF52151. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS51210. PLA2C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5R8A5-1 [UniParc]FASTAAdd to Basket

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    MSFIDPYQHI IVEHQYSHKF TVVVLCATKV TKGAFGDMLD TPDPYVELFI    50
    STTPDSRKRT RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE 100
    TLGTATFPVS SMKVGEKKEV PFIFNQVTEM ILEMSLEVCS CPDLRFSMAL 150
    CDQEKTFRQQ RKEHIRESMK KLLGPKNSEG LHSARDVPVV AILGSGGGFR 200
    AMVGFSGVMK ALYESGILDC ATYVAGLSGS TWYMSTLYSH PDFPEKGPEE 250
    INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG 300
    ETLIHNRMNT TLSSLKEKVN TAQCPLPLFT CLHVKPDVSE LMFADWVEFS 350
    PYEIGMAKYG TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL 400
    FNRVLGVSGS QSRGSTMEEE LENITTKHIV SNDSSDSDDE SHEPKGTENE 450
    DAGSDYQSDN QASWIHRMIM ALVSDSALFN TREGRAGKVH NFMLGLNLNT 500
    SYPLSPLSDF ATQDSFDDDE LDAAVADPDE FERIYEPLDV KSKKIHVVDS 550
    GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWAKMN 600
    KLPFPKIDPY VFDREGLKEC YVFKPKNPDM EKDCPTIIHF VLANINFRKY 650
    KAPGVPRETE EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMHFN 700
    TLNNIDVIKE AMVESIEYRR QNPSRCSVSL SNVEARRFFN KEFLSKPKA 749
    Length:749
    Mass (Da):85,168
    Last modified:December 21, 2004 - v1
    Checksum:i70C1D0C9E983BBD4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859848 mRNA. Translation: CAH92005.1.
    RefSeqiNP_001126164.1. NM_001132692.1.
    UniGeneiPab.12757.

    Genome annotation databases

    GeneIDi100173125.
    KEGGipon:100173125.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859848 mRNA. Translation: CAH92005.1 .
    RefSeqi NP_001126164.1. NM_001132692.1.
    UniGenei Pab.12757.

    3D structure databases

    ProteinModelPortali Q5R8A5.
    SMRi Q5R8A5. Positions 13-721.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100173125.
    KEGGi pon:100173125.

    Organism-specific databases

    CTDi 5321.

    Phylogenomic databases

    HOGENOMi HOG000115420.
    HOVERGENi HBG053479.
    InParanoidi Q5R8A5.
    KOi K16342.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR016035. Acyl_Trfase/lysoPLipase.
    IPR000008. C2_dom.
    IPR002642. LysoPLipase_cat_dom.
    [Graphical view ]
    Pfami PF00168. C2. 1 hit.
    PF01735. PLA2_B. 1 hit.
    [Graphical view ]
    SMARTi SM00239. C2. 1 hit.
    SM00022. PLAc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF52151. SSF52151. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS51210. PLA2C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiPA24A_PONAB
    AccessioniPrimary (citable) accession number: Q5R8A5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 49 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3