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Protein

Cytosolic phospholipase A2

Gene

PLA2G4A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

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+.

Kineticsi

    1. Vmax=2.7 µmol/min/mg enzyme for the phospholipase A2 reaction1 Publication
    2. Vmax=4.6 µmol/min/mg enzyme for the lysophosphatase reaction1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi40Calcium 11
    Metal bindingi40Calcium 21
    Metal bindingi41Calcium 1; via carbonyl oxygen1
    Metal bindingi43Calcium 11
    Metal bindingi43Calcium 21
    Metal bindingi65Calcium 11
    Metal bindingi93Calcium 21
    Metal bindingi94Calcium 2; via carbonyl oxygen1
    Metal bindingi95Calcium 21
    Active sitei228Nucleophile1
    Active sitei549Proton acceptor1

    GO - Molecular functioni

    • calcium-dependent phospholipase A2 activity Source: Reactome
    • calcium-dependent phospholipid binding Source: UniProtKB
    • calcium ion binding Source: UniProtKB
    • lysophospholipase activity Source: Reactome
    • phosphatidylcholine 1-acylhydrolase activity Source: Reactome
    • phospholipase A2 activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04039-MONOMER.
    ZFISH:HS04039-MONOMER.
    BRENDAi3.1.1.4. 2681.
    ReactomeiR-HSA-111995. phospho-PLA2 pathway.
    R-HSA-1482788. Acyl chain remodelling of PC.
    R-HSA-1482798. Acyl chain remodeling of CL.
    R-HSA-1482801. Acyl chain remodelling of PS.
    R-HSA-1482839. Acyl chain remodelling of PE.
    R-HSA-1482922. Acyl chain remodelling of PI.
    R-HSA-1482925. Acyl chain remodelling of PG.
    R-HSA-1483115. Hydrolysis of LPC.
    R-HSA-1483166. Synthesis of PA.
    R-HSA-2142753. Arachidonic acid metabolism.
    R-HSA-418592. ADP signalling through P2Y purinoceptor 1.
    R-HSA-432142. Platelet sensitization by LDL.
    R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
    SIGNORiP47712.

    Chemistry databases

    SwissLipidsiSLP:000000565.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9035. PLA2G4A.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle

    Pathology & Biotechi

    Involvement in diseasei

    PLA2G4A mutations resulting in phospholipase A2 deficiency have been found in a patient affected by recurrent episodes of multiple complicated ulcers of the small intestine, not due to cyclooxygenase inhibitors use. Disease features also include platelet dysfunction, and globally decreased eicosanoid synthesis (PubMed:18451993).

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi139C → A: No effect on phospholipase activity; when associated with A-141 and A-151. 1 Publication1
    Mutagenesisi141C → A: No effect on phospholipase activity; when associated with A-139 and A-151. 1 Publication1
    Mutagenesisi151C → A: No effect on phospholipase activity; when associated with A-139 and A-141. 1 Publication1
    Mutagenesisi195S → A: 5-fold reduced phospholipase and lysophosphatase activities. 100-fold reduced phospholipase and lysophosphatase activities; when associated with A-577. 1 Publication1
    Mutagenesisi200R → A or H: Abolishes phospholipase activity. 1 Publication1
    Mutagenesisi200R → K: Reduces phospholipase activity 200-fold. 1 Publication1
    Mutagenesisi215S → A: No effect on phospholipase or lysophosphatase activity. 1 Publication1
    Mutagenesisi220C → A: No effect on phospholipase activity. 1 Publication1
    Mutagenesisi228S → A, C or T: Abolishes both phospholipase and lysophosphatase activities. 3 Publications1
    Mutagenesisi324C → A: No effect on phospholipase activity; when associated with A-331. 1 Publication1
    Mutagenesisi331C → A: No effect on phospholipase activity; when associated with A-324. 1 Publication1
    Mutagenesisi505S → A: Decreases agonist-stimulated release of arachidonic acid. 1 Publication1
    Mutagenesisi549D → A: Abolishes phospholipiase activity. 1 Publication1
    Mutagenesisi549D → E: Reduces phospholipiase activity 2000-fold. 1 Publication1
    Mutagenesisi549D → N: Reduces phospholipiase activity 300-fold. 1 Publication1
    Mutagenesisi577S → A: 7-fold reduced phospholipase and lysophosphatase activities. 100-fold reduced phospholipase and lysophosphatase activities; when associated with A-195. 1 Publication1
    Mutagenesisi620C → A: No effect on phospholipase activity; when associated with A-634. 1 Publication1
    Mutagenesisi634C → A: No effect on phospholipase activity; when associated with A-620. 1 Publication1
    Mutagenesisi726C → A: No effect on phospholipase activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi5321.
    OpenTargetsiENSG00000116711.
    PharmGKBiPA271.

    Chemistry databases

    ChEMBLiCHEMBL3816.
    DrugBankiDB00041. Aldesleukin.
    DB00411. Carbachol.
    DB00578. Carbenicillin.
    DB00445. Epirubicin.
    DB00591. Fluocinolone Acetonide.
    DB00588. Fluticasone Propionate.
    DB04552. Niflumic Acid.
    DB01083. Orlistat.
    DB01103. Quinacrine.
    DB00086. Streptokinase.
    DB04786. Suramin.
    GuidetoPHARMACOLOGYi1424.

    Polymorphism and mutation databases

    BioMutaiPLA2G4A.
    DMDMi317373312.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001872621 – 749Cytosolic phospholipase A2Add BLAST749

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2PhosphoserineCombined sources1
    Modified residuei268PhosphothreonineCombined sources1
    Modified residuei434PhosphoserineBy similarity1
    Modified residuei435PhosphoserineCombined sources1
    Modified residuei437PhosphoserineCombined sources1
    Modified residuei505Phosphoserine; by MAPK2 Publications1
    Modified residuei515PhosphoserineBy similarity1
    Modified residuei727PhosphoserineCombined sources1 Publication1
    Modified residuei729PhosphoserineCombined sources1

    Post-translational modificationi

    Activated by phosphorylation at both Ser-505 and Ser-727.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    EPDiP47712.
    MaxQBiP47712.
    PaxDbiP47712.
    PeptideAtlasiP47712.
    PRIDEiP47712.

    PTM databases

    iPTMnetiP47712.
    PhosphoSitePlusiP47712.

    Miscellaneous databases

    PMAP-CutDBP47712.

    Expressioni

    Tissue specificityi

    Expressed in various tissues such as macrophages, platelets, neutrophils, fibroblasts and lung endothelium.

    Gene expression databases

    BgeeiENSG00000116711.
    CleanExiHS_PLA2G4A.
    GenevisibleiP47712. HS.

    Organism-specific databases

    HPAiCAB010050.
    HPA050062.
    HPA054206.

    Interactioni

    Subunit structurei

    Interacts with KAT5.4 Publications

    Protein-protein interaction databases

    BioGridi111338. 18 interactors.
    DIPiDIP-40991N.
    IntActiP47712. 5 interactors.
    MINTiMINT-118843.
    STRINGi9606.ENSP00000356436.

    Chemistry databases

    BindingDBiP47712.

    Structurei

    Secondary structure

    1749
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi18 – 29Combined sources12
    Helixi34 – 39Combined sources6
    Beta strandi44 – 49Combined sources6
    Beta strandi51 – 54Combined sources4
    Beta strandi57 – 60Combined sources4
    Beta strandi70 – 79Combined sources10
    Beta strandi86 – 93Combined sources8
    Beta strandi96 – 98Combined sources3
    Beta strandi100 – 108Combined sources9
    Helixi109 – 111Combined sources3
    Beta strandi117 – 124Combined sources8
    Turni125 – 127Combined sources3
    Beta strandi128 – 137Combined sources10
    Beta strandi143 – 146Combined sources4
    Helixi152 – 177Combined sources26
    Helixi179 – 181Combined sources3
    Beta strandi190 – 194Combined sources5
    Helixi198 – 214Combined sources17
    Helixi218 – 220Combined sources3
    Beta strandi221 – 226Combined sources6
    Helixi228 – 239Combined sources12
    Turni241 – 245Combined sources5
    Helixi248 – 260Combined sources13
    Helixi263 – 266Combined sources4
    Helixi269 – 284Combined sources16
    Helixi291 – 304Combined sources14
    Helixi305 – 307Combined sources3
    Helixi313 – 318Combined sources6
    Turni319 – 321Combined sources3
    Beta strandi326 – 333Combined sources8
    Helixi341 – 343Combined sources3
    Beta strandi344 – 349Combined sources6
    Beta strandi354 – 356Combined sources3
    Turni357 – 360Combined sources4
    Beta strandi361 – 363Combined sources3
    Helixi365 – 367Combined sources3
    Beta strandi370 – 373Combined sources4
    Beta strandi376 – 379Combined sources4
    Helixi386 – 393Combined sources8
    Helixi396 – 399Combined sources4
    Helixi401 – 404Combined sources4
    Helixi417 – 423Combined sources7
    Helixi426 – 429Combined sources4
    Helixi463 – 476Combined sources14
    Beta strandi488 – 490Combined sources3
    Turni492 – 495Combined sources4
    Beta strandi543 – 548Combined sources6
    Helixi550 – 552Combined sources3
    Helixi558 – 561Combined sources4
    Helixi564 – 566Combined sources3
    Beta strandi570 – 575Combined sources6
    Helixi588 – 599Combined sources12
    Helixi611 – 615Combined sources5
    Beta strandi619 – 623Combined sources5
    Beta strandi636 – 641Combined sources6
    Helixi646 – 648Combined sources3
    Beta strandi650 – 652Combined sources3
    Helixi660 – 666Combined sources7
    Beta strandi670 – 672Combined sources3
    Helixi687 – 702Combined sources16
    Helixi705 – 718Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1BCINMR-A1-138[»]
    1CJYX-ray2.50A/B1-749[»]
    1RLWX-ray2.40A17-141[»]
    ProteinModelPortaliP47712.
    SMRiP47712.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP47712.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini5 – 106C2PROSITE-ProRule annotationAdd BLAST102
    Domaini140 – 740PLA2cPROSITE-ProRule annotationAdd BLAST601

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 178Phospholipid bindingCuratedAdd BLAST178

    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+.2 Publications

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiKOG1012. Eukaryota.
    KOG1325. Eukaryota.
    ENOG410XR72. LUCA.
    GeneTreeiENSGT00550000074489.
    HOGENOMiHOG000115420.
    HOVERGENiHBG053479.
    InParanoidiP47712.
    KOiK16342.
    OMAiRFSMALC.
    OrthoDBiEOG091G0276.
    PhylomeDBiP47712.
    TreeFamiTF325228.

    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.

    P47712-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI
    60 70 80 90 100
    STTPDSRKRT RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE
    110 120 130 140 150
    TLGTATFTVS SMKVGEKKEV PFIFNQVTEM VLEMSLEVCS CPDLRFSMAL
    160 170 180 190 200
    CDQEKTFRQQ RKEHIRESMK KLLGPKNSEG LHSARDVPVV AILGSGGGFR
    210 220 230 240 250
    AMVGFSGVMK ALYESGILDC ATYVAGLSGS TWYMSTLYSH PDFPEKGPEE
    260 270 280 290 300
    INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG
    310 320 330 340 350
    ETLIHNRMNT TLSSLKEKVN TAQCPLPLFT CLHVKPDVSE LMFADWVEFS
    360 370 380 390 400
    PYEIGMAKYG TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL
    410 420 430 440 450
    FNRVLGVSGS QSRGSTMEEE LENITTKHIV SNDSSDSDDE SHEPKGTENE
    460 470 480 490 500
    DAGSDYQSDN QASWIHRMIM ALVSDSALFN TREGRAGKVH NFMLGLNLNT
    510 520 530 540 550
    SYPLSPLSDF ATQDSFDDDE LDAAVADPDE FERIYEPLDV KSKKIHVVDS
    560 570 580 590 600
    GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWAKMN
    610 620 630 640 650
    KLPFPKIDPY VFDREGLKEC YVFKPKNPDM EKDCPTIIHF VLANINFRKY
    660 670 680 690 700
    RAPGVPRETE EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMHFN
    710 720 730 740
    TLNNIDVIKE AMVESIEYRR QNPSRCSVSL SNVEARRFFN KEFLSKPKA
    Length:749
    Mass (Da):85,239
    Last modified:January 11, 2011 - v2
    Checksum:iEE71CA0EBE617856
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_029276103G → R.Corresponds to variant rs28395828dbSNPEnsembl.1
    Natural variantiVAR_070778111S → P Probable disease-associated mutation found in a compound heterozygote affected by phospholipase A2 deficiency also carrying H-485. 1 PublicationCorresponds to variant rs121434634dbSNPEnsembl.1
    Natural variantiVAR_018760224V → I.1 PublicationCorresponds to variant rs12720588dbSNPEnsembl.1
    Natural variantiVAR_035826442H → Q in a breast cancer sample; somatic mutation. 1 Publication1
    Natural variantiVAR_070779485R → H Probable disease-associated mutation found in a compound heterozygote affected by phospholipase A2 deficiency also carrying P-111. 1 PublicationCorresponds to variant rs121434635dbSNPEnsembl.1
    Natural variantiVAR_062128637I → V.Corresponds to variant rs28395831dbSNPEnsembl.1
    Natural variantiVAR_018424651R → K.5 PublicationsCorresponds to variant rs2307198dbSNPEnsembl.1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M72393 mRNA. Translation: AAB00789.1.
    M68874 mRNA. Translation: AAA60105.1.
    AY552098 Genomic DNA. Translation: AAS45712.1.
    AL022147 Genomic DNA. Translation: CAB42689.2.
    AL049797, AL022147 Genomic DNA. Translation: CAI22252.1.
    BC114340 mRNA. Translation: AAI14341.1.
    CCDSiCCDS1372.1.
    PIRiA39329.
    RefSeqiNP_001298122.1. NM_001311193.1.
    NP_077734.1. NM_024420.2.
    XP_011507944.1. XM_011509642.2.
    UniGeneiHs.497200.

    Genome annotation databases

    EnsembliENST00000367466; ENSP00000356436; ENSG00000116711.
    GeneIDi5321.
    KEGGihsa:5321.
    UCSCiuc001gsc.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M72393 mRNA. Translation: AAB00789.1.
    M68874 mRNA. Translation: AAA60105.1.
    AY552098 Genomic DNA. Translation: AAS45712.1.
    AL022147 Genomic DNA. Translation: CAB42689.2.
    AL049797, AL022147 Genomic DNA. Translation: CAI22252.1.
    BC114340 mRNA. Translation: AAI14341.1.
    CCDSiCCDS1372.1.
    PIRiA39329.
    RefSeqiNP_001298122.1. NM_001311193.1.
    NP_077734.1. NM_024420.2.
    XP_011507944.1. XM_011509642.2.
    UniGeneiHs.497200.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1BCINMR-A1-138[»]
    1CJYX-ray2.50A/B1-749[»]
    1RLWX-ray2.40A17-141[»]
    ProteinModelPortaliP47712.
    SMRiP47712.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111338. 18 interactors.
    DIPiDIP-40991N.
    IntActiP47712. 5 interactors.
    MINTiMINT-118843.
    STRINGi9606.ENSP00000356436.

    Chemistry databases

    BindingDBiP47712.
    ChEMBLiCHEMBL3816.
    DrugBankiDB00041. Aldesleukin.
    DB00411. Carbachol.
    DB00578. Carbenicillin.
    DB00445. Epirubicin.
    DB00591. Fluocinolone Acetonide.
    DB00588. Fluticasone Propionate.
    DB04552. Niflumic Acid.
    DB01083. Orlistat.
    DB01103. Quinacrine.
    DB00086. Streptokinase.
    DB04786. Suramin.
    GuidetoPHARMACOLOGYi1424.
    SwissLipidsiSLP:000000565.

    PTM databases

    iPTMnetiP47712.
    PhosphoSitePlusiP47712.

    Polymorphism and mutation databases

    BioMutaiPLA2G4A.
    DMDMi317373312.

    Proteomic databases

    EPDiP47712.
    MaxQBiP47712.
    PaxDbiP47712.
    PeptideAtlasiP47712.
    PRIDEiP47712.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000367466; ENSP00000356436; ENSG00000116711.
    GeneIDi5321.
    KEGGihsa:5321.
    UCSCiuc001gsc.4. human.

    Organism-specific databases

    CTDi5321.
    DisGeNETi5321.
    GeneCardsiPLA2G4A.
    HGNCiHGNC:9035. PLA2G4A.
    HPAiCAB010050.
    HPA050062.
    HPA054206.
    MIMi600522. gene.
    neXtProtiNX_P47712.
    OpenTargetsiENSG00000116711.
    PharmGKBiPA271.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1012. Eukaryota.
    KOG1325. Eukaryota.
    ENOG410XR72. LUCA.
    GeneTreeiENSGT00550000074489.
    HOGENOMiHOG000115420.
    HOVERGENiHBG053479.
    InParanoidiP47712.
    KOiK16342.
    OMAiRFSMALC.
    OrthoDBiEOG091G0276.
    PhylomeDBiP47712.
    TreeFamiTF325228.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04039-MONOMER.
    ZFISH:HS04039-MONOMER.
    BRENDAi3.1.1.4. 2681.
    ReactomeiR-HSA-111995. phospho-PLA2 pathway.
    R-HSA-1482788. Acyl chain remodelling of PC.
    R-HSA-1482798. Acyl chain remodeling of CL.
    R-HSA-1482801. Acyl chain remodelling of PS.
    R-HSA-1482839. Acyl chain remodelling of PE.
    R-HSA-1482922. Acyl chain remodelling of PI.
    R-HSA-1482925. Acyl chain remodelling of PG.
    R-HSA-1483115. Hydrolysis of LPC.
    R-HSA-1483166. Synthesis of PA.
    R-HSA-2142753. Arachidonic acid metabolism.
    R-HSA-418592. ADP signalling through P2Y purinoceptor 1.
    R-HSA-432142. Platelet sensitization by LDL.
    R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
    SIGNORiP47712.

    Miscellaneous databases

    EvolutionaryTraceiP47712.
    GeneWikiiPLA2G4A.
    GenomeRNAii5321.
    PMAP-CutDBP47712.
    PROiP47712.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000116711.
    CleanExiHS_PLA2G4A.
    GenevisibleiP47712. HS.

    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]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPA24A_HUMAN
    AccessioniPrimary (citable) accession number: P47712
    Secondary accession number(s): B1AKG4, Q29R80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 11, 2011
    Last modified: November 2, 2016
    This is version 178 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.