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P39877

- PA2G5_HUMAN

UniProt

P39877 - PA2G5_HUMAN

Protein

Calcium-dependent phospholipase A2

Gene

PLA2G5

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

    PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes more efficiently L-alpha-1-palmitoyl-2-oleoyl phosphatidylcholine than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L-alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine, or L-alpha-1-stearoyl-2-arachidonyl phosphatidylinositol. May be involved in the production of lung surfactant, the remodeling or regulation of cardiac muscle.

    Catalytic activityi

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

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    pH dependencei

    Optimum pH is 6.5. Activity remains high up to pH 9.0.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi47 – 471Calcium; via carbonyl oxygenBy similarity
    Metal bindingi49 – 491Calcium; via carbonyl oxygenBy similarity
    Metal bindingi51 – 511Calcium; via carbonyl oxygenBy similarity
    Active sitei67 – 671By similarity
    Metal bindingi68 – 681CalciumBy similarity
    Active sitei111 – 1111By similarity

    GO - Molecular functioni

    1. calcium-dependent phospholipase A2 activity Source: ProtInc
    2. calcium ion binding Source: InterPro
    3. heparin binding Source: Ensembl

    GO - Biological processi

    1. arachidonic acid secretion Source: Ensembl
    2. glycerophospholipid biosynthetic process Source: Reactome
    3. leukotriene biosynthetic process Source: Ensembl
    4. lipid catabolic process Source: UniProtKB-KW
    5. phosphatidic acid biosynthetic process Source: Reactome
    6. phosphatidylcholine acyl-chain remodeling Source: Reactome
    7. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
    8. phosphatidylglycerol acyl-chain remodeling Source: Reactome
    9. phosphatidylinositol acyl-chain remodeling Source: Reactome
    10. phosphatidylserine acyl-chain remodeling Source: Reactome
    11. phospholipid metabolic process Source: Reactome
    12. platelet activating factor biosynthetic process Source: Ensembl
    13. response to cAMP Source: Ensembl
    14. response to cytokine Source: Ensembl
    15. 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:
    Calcium-dependent phospholipase A2 (EC:3.1.1.4)
    Alternative name(s):
    Group V phospholipase A2
    PLA2-10
    Phosphatidylcholine 2-acylhydrolase 5
    Gene namesi
    Name:PLA2G5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9038. PLA2G5.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. extracellular region Source: Reactome
    3. Golgi apparatus Source: Ensembl
    4. perinuclear region of cytoplasm Source: Ensembl
    5. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Fleck retina, familial benign (FRFB) [MIM:228980]: An autosomal recessive condition associated with a distinctive retinal appearance and no apparent visual or electrophysiologic deficits. Affected individuals are asymptomatic, but fundus examination reveals a striking pattern of diffuse, yellow-white, fleck-like lesions extending to the far periphery of the retina but sparing the foveal region.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451G → C in FRFB. 1 Publication
    VAR_067343
    Natural varianti49 – 491G → S in FRFB. 1 Publication
    VAR_067344

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi228980. phenotype.
    Orphaneti363989. Familial benign flecked retina.
    PharmGKBiPA33366.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 138118Calcium-dependent phospholipase A2PRO_0000022761Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 137By similarity
    Disulfide bondi48 ↔ 64By similarity
    Disulfide bondi63 ↔ 117By similarity
    Disulfide bondi70 ↔ 110By similarity
    Disulfide bondi79 ↔ 103By similarity
    Disulfide bondi97 ↔ 108By similarity

    Post-translational modificationi

    This enzyme lacks one of the seven disulfide bonds found in similar PA2 proteins.

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP39877.
    PRIDEiP39877.

    Expressioni

    Tissue specificityi

    Heart, placenta and less abundantly, in lung. Detected in the outer and inner plexiform layers of the retina (at protein level).1 Publication

    Gene expression databases

    BgeeiP39877.
    CleanExiHS_PLA2G5.
    GenevestigatoriP39877.

    Organism-specific databases

    HPAiHPA053361.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000364249.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GHNmodel-A21-138[»]
    ProteinModelPortaliP39877.
    SMRiP39877. Positions 22-138.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phospholipase A2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG330703.
    HOGENOMiHOG000231749.
    HOVERGENiHBG008137.
    InParanoidiP39877.
    KOiK01047.
    OMAiCSSALEV.
    OrthoDBiEOG7N63PF.
    PhylomeDBiP39877.
    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.

    P39877-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGLLPLAWF LACSVPAVQG GLLDLKSMIE KVTGKNALTN YGFYGCYCGW    50
    GGRGTPKDGT DWCCWAHDHC YGRLEEKGCN IRTQSYKYRF AWGVVTCEPG 100
    PFCHVNLCAC DRKLVYCLKR NLRSYNPQYQ YFPNILCS 138
    Length:138
    Mass (Da):15,674
    Last modified:February 1, 1995 - v1
    Checksum:i0D17DC76E55F42BC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451G → C in FRFB. 1 Publication
    VAR_067343
    Natural varianti49 – 491G → S in FRFB. 1 Publication
    VAR_067344

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03090 mRNA. Translation: AAC28886.1.
    AY524778 Genomic DNA. Translation: AAR92480.1.
    AL158172 Genomic DNA. Translation: CAC13158.1.
    BC036792 mRNA. Translation: AAH36792.2.
    CCDSiCCDS202.1.
    PIRiA49959.
    RefSeqiNP_000920.1. NM_000929.2.
    XP_005245950.1. XM_005245893.2.
    XP_005245952.1. XM_005245895.2.
    XP_005245953.1. XM_005245896.1.
    XP_006710755.1. XM_006710692.1.
    XP_006710756.1. XM_006710693.1.
    XP_006710757.1. XM_006710694.1.
    XP_006710758.1. XM_006710695.1.
    XP_006710759.1. XM_006710696.1.
    UniGeneiHs.319438.

    Genome annotation databases

    EnsembliENST00000375108; ENSP00000364249; ENSG00000127472.
    GeneIDi5322.
    KEGGihsa:5322.
    UCSCiuc001bcx.3. human.

    Polymorphism databases

    DMDMi730258.

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03090 mRNA. Translation: AAC28886.1 .
    AY524778 Genomic DNA. Translation: AAR92480.1 .
    AL158172 Genomic DNA. Translation: CAC13158.1 .
    BC036792 mRNA. Translation: AAH36792.2 .
    CCDSi CCDS202.1.
    PIRi A49959.
    RefSeqi NP_000920.1. NM_000929.2.
    XP_005245950.1. XM_005245893.2.
    XP_005245952.1. XM_005245895.2.
    XP_005245953.1. XM_005245896.1.
    XP_006710755.1. XM_006710692.1.
    XP_006710756.1. XM_006710693.1.
    XP_006710757.1. XM_006710694.1.
    XP_006710758.1. XM_006710695.1.
    XP_006710759.1. XM_006710696.1.
    UniGenei Hs.319438.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GHN model - A 21-138 [» ]
    ProteinModelPortali P39877.
    SMRi P39877. Positions 22-138.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000364249.

    Chemistry

    BindingDBi P39877.
    ChEMBLi CHEMBL4323.

    Polymorphism databases

    DMDMi 730258.

    Proteomic databases

    PaxDbi P39877.
    PRIDEi P39877.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375108 ; ENSP00000364249 ; ENSG00000127472 .
    GeneIDi 5322.
    KEGGi hsa:5322.
    UCSCi uc001bcx.3. human.

    Organism-specific databases

    CTDi 5322.
    GeneCardsi GC01P020354.
    HGNCi HGNC:9038. PLA2G5.
    HPAi HPA053361.
    MIMi 228980. phenotype.
    601192. gene.
    neXtProti NX_P39877.
    Orphaneti 363989. Familial benign flecked retina.
    PharmGKBi PA33366.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG330703.
    HOGENOMi HOG000231749.
    HOVERGENi HBG008137.
    InParanoidi P39877.
    KOi K01047.
    OMAi CSSALEV.
    OrthoDBi EOG7N63PF.
    PhylomeDBi P39877.
    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

    GeneWikii PLA2G5.
    GenomeRNAii 5322.
    NextBioi 20590.
    PROi P39877.
    SOURCEi Search...

    Gene expression databases

    Bgeei P39877.
    CleanExi HS_PLA2G5.
    Genevestigatori P39877.

    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 and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2."
      Chen J., Engle S.J., Seilhamer J.J., Tischfield J.A.
      J. Biol. Chem. 269:2365-2368(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Stomach.
    2. NIEHS SNPs program
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Brain.
    5. Cited for: TISSUE SPECIFICITY, VARIANTS FRFB CYS-45 AND SER-49.

    Entry informationi

    Entry nameiPA2G5_HUMAN
    AccessioniPrimary (citable) accession number: P39877
    Secondary accession number(s): Q8N435
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 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 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

    External Data

    Dasty 3