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Q9TT38

- PA24A_RABIT

UniProt

Q9TT38 - PA24A_RABIT

Protein

Cytosolic phospholipase A2

Gene

PLA2G4A

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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 sitei548 – 5481Proton 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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: 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 – 748748Cytosolic phospholipase A2PRO_0000345135Add
    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 residuei726 – 7261PhosphoserineBy similarity
    Modified residuei728 – 7281PhosphoserineBy similarity

    Post-translational modificationi

    Activated by phosphorylation at both Ser-505 and Ser-726.By similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Interacts with KAT5.By similarity

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000012590.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9TT38.
    SMRiQ9TT38. Positions 13-720.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 106102C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini138 – 739602PLA2cPROSITE-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

    eggNOGiNOG257248.
    HOGENOMiHOG000115420.
    HOVERGENiHBG053479.

    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.

    Q9TT38-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI    50
    ATTPDSRKRT RHFNNDINPV WNEAFEFILD PNQGNVLEIT LMDANYVMDE 100
    TLGTATFPVS SMKVGEKKEV PFIFNQVTEM ILEMSLEVCS SPDLRFSMAL 150
    CDQEKAFRQQ RKENIKENMR KLLGPKKSEG LYSTRDVPVV AILGSGGGFR 200
    AMVGFSGVMK ALYESGILDC ATYIAGLSGS TWYMSTLYSH PDFPEKGPQE 250
    INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG 300
    ETLIHNRMHT TLSSLKEKVS SAQCPLPLFT CLHVKPDVSE LMFADWVEFS 350
    PYEIGMAKYG TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL 400
    FNRVLGVSGS HNKGSTMEEE LENITAKHIV SNDSSDSDDE SQEPKGTEGE 450
    DAEREYQNDH QASWVHRMLM ALVSDSALFN TREGRAGKVH NFMLGLNLNT 500
    SYPLSPLRDF TQESFDDDEL DAAVADPDEF ERIYEPLDVK SKKIHVVDSG 550
    LTFNLPYPLI LRPQRGVDLI ISFDFSARPS DTSPPFKELL LAEKWAKMNK 600
    LPFPKIDPYV FDREGLKECY VFKPKNPDVE KDCPIIIHFV LANINFRKYK 650
    SPGVPRETKE EKEIADFDIF DDPESPFSTF NFQYPNQAFK RLHDLMYFNT 700
    LNNIDVIKDA MVESIEYRRQ NPSRCSVSLS NVEARRFFNK EFLSKPTA 748
    Length:748
    Mass (Da):85,235
    Last modified:May 1, 2000 - v1
    Checksum:i7661A3EFC41FF668
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF204923 mRNA. Translation: AAF15299.1.
    RefSeqiNP_001075541.1. NM_001082072.1.
    UniGeneiOcu.2401.

    Genome annotation databases

    GeneIDi100008748.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF204923 mRNA. Translation: AAF15299.1 .
    RefSeqi NP_001075541.1. NM_001082072.1.
    UniGenei Ocu.2401.

    3D structure databases

    ProteinModelPortali Q9TT38.
    SMRi Q9TT38. Positions 13-720.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000012590.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100008748.

    Organism-specific databases

    CTDi 5321.

    Phylogenomic databases

    eggNOGi NOG257248.
    HOGENOMi HOG000115420.
    HOVERGENi HBG053479.

    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. "Molecular cloning of cDNA coding for phospholipase A2."
      Al-Khalili O.K., Eaton D.C.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: New Zealand white.
      Tissue: Heart.

    Entry informationi

    Entry nameiPA24A_RABIT
    AccessioniPrimary (citable) accession number: Q9TT38
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 66 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