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Q9BZM2

- PA2GF_HUMAN

UniProt

Q9BZM2 - PA2GF_HUMAN

Protein

Group IIF secretory phospholipase A2

Gene

PLA2G2F

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 1 calcium ion per subunit.1 Publication

    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 – 671PROSITE-ProRule annotation
    Metal bindingi68 – 681CalciumBy similarity
    Active sitei114 – 1141PROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. phospholipase A2 activity Source: UniProtKB

    GO - Biological processi

    1. glycerophospholipid biosynthetic process Source: Reactome
    2. lipid catabolic process Source: UniProtKB-KW
    3. phosphatidic acid biosynthetic process Source: Reactome
    4. phosphatidylcholine acyl-chain remodeling Source: Reactome
    5. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
    6. phosphatidylglycerol acyl-chain remodeling Source: Reactome
    7. phosphatidylinositol acyl-chain remodeling Source: Reactome
    8. phosphatidylserine acyl-chain remodeling Source: Reactome
    9. phospholipid metabolic process Source: Reactome
    10. 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 IIF secretory phospholipase A2 (EC:3.1.1.4)
    Short name:
    GIIF sPLA2
    Short name:
    sPLA2-IIF
    Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase 2F
    Gene namesi
    Name:PLA2G2F
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:30040. PLA2G2F.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134931043.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 168148Group IIF secretory phospholipase A2PRO_0000022759Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 138By similarity
    Disulfide bondi48 ↔ 64By similarity
    Disulfide bondi63 ↔ 120By similarity
    Disulfide bondi69 ↔ 145By similarity
    Disulfide bondi70 ↔ 113By similarity
    Disulfide bondi79 ↔ 106By similarity
    Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi98 ↔ 111By similarity
    Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9BZM2.
    PRIDEiQ9BZM2.

    Expressioni

    Tissue specificityi

    Expressed at high levels in placenta, testis, thymus and at lower levels in heart, kidney, liver and prostate.1 Publication

    Gene expression databases

    BgeeiQ9BZM2.
    CleanExiHS_PLA2G2F.
    GenevestigatoriQ9BZM2.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000364243.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BZM2.
    SMRiQ9BZM2. Positions 21-151.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phospholipase A2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG296589.
    HOGENOMiHOG000231749.
    HOVERGENiHBG008137.
    InParanoidiQ9BZM2.
    KOiK01047.
    OMAiLPMDEVD.
    OrthoDBiEOG7N63PF.
    PhylomeDBiQ9BZM2.
    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.
    PROSITEiPS00118. PA2_HIS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BZM2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKKFFTVAIL AGSVLSTAHG SLLNLKAMVE AVTGRSAILS FVGYGCYCGL    50
    GGRGQPKDEV DWCCHAHDCC YQELFDQGCH PYVDHYDHTI ENNTEIVCSD 100
    LNKTECDKQT CMCDKNMVLC LMNQTYREEY RGFLNVYCQG PTPNCSIYEP 150
    PPEEVTCSHQ SPAPPAPP 168
    Length:168
    Mass (Da):18,658
    Last modified:June 1, 2001 - v1
    Checksum:i35B159298246A762
    GO
    Isoform 2 (identifier: Q9BZM2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MADGAKANPKGFKKKVLDRCFSGWRGPRFGASCPSRTSRSSLGM

    Show »
    Length:211
    Mass (Da):23,256
    Checksum:i483B5E7850CB4248
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti149 – 1491E → G in BAC04210. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MADGAKANPKGFKKKVLDRC FSGWRGPRFGASCPSRTSRS SLGM in isoform 2. CuratedVSP_037524

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF306566 mRNA. Translation: AAG50242.1.
    AK093645 mRNA. Translation: BAC04210.1.
    AL158172, Z98257 Genomic DNA. Translation: CAI19658.1.
    Z98257, AL158172 Genomic DNA. Translation: CAI20260.1.
    CCDSiCCDS204.2. [Q9BZM2-2]
    RefSeqiNP_073730.3. NM_022819.3. [Q9BZM2-2]
    UniGeneiHs.302034.

    Genome annotation databases

    EnsembliENST00000375102; ENSP00000364243; ENSG00000158786. [Q9BZM2-2]
    GeneIDi64600.
    KEGGihsa:64600.
    UCSCiuc009vpp.1. human. [Q9BZM2-2]

    Polymorphism databases

    DMDMi20139134.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF306566 mRNA. Translation: AAG50242.1 .
    AK093645 mRNA. Translation: BAC04210.1 .
    AL158172 , Z98257 Genomic DNA. Translation: CAI19658.1 .
    Z98257 , AL158172 Genomic DNA. Translation: CAI20260.1 .
    CCDSi CCDS204.2. [Q9BZM2-2 ]
    RefSeqi NP_073730.3. NM_022819.3. [Q9BZM2-2 ]
    UniGenei Hs.302034.

    3D structure databases

    ProteinModelPortali Q9BZM2.
    SMRi Q9BZM2. Positions 21-151.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000364243.

    Chemistry

    BindingDBi Q9BZM2.
    ChEMBLi CHEMBL4278.

    Polymorphism databases

    DMDMi 20139134.

    Proteomic databases

    PaxDbi Q9BZM2.
    PRIDEi Q9BZM2.

    Protocols and materials databases

    DNASUi 64600.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375102 ; ENSP00000364243 ; ENSG00000158786 . [Q9BZM2-2 ]
    GeneIDi 64600.
    KEGGi hsa:64600.
    UCSCi uc009vpp.1. human. [Q9BZM2-2 ]

    Organism-specific databases

    CTDi 64600.
    GeneCardsi GC01P020465.
    H-InvDB HIX0000212.
    HGNCi HGNC:30040. PLA2G2F.
    neXtProti NX_Q9BZM2.
    PharmGKBi PA134931043.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG296589.
    HOGENOMi HOG000231749.
    HOVERGENi HBG008137.
    InParanoidi Q9BZM2.
    KOi K01047.
    OMAi LPMDEVD.
    OrthoDBi EOG7N63PF.
    PhylomeDBi Q9BZM2.
    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

    GenomeRNAii 64600.
    NextBioi 66565.
    PROi Q9BZM2.

    Gene expression databases

    Bgeei Q9BZM2.
    CleanExi HS_PLA2G2F.
    Genevestigatori Q9BZM2.

    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 PS00118. PA2_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and recombinant expression of human group IIF-secreted phospholipase A(2)."
      Valentin E., Singer A.G., Ghomashchi F., Lazdunski M., Gelb M.H., Lambeau G.
      Biochem. Biophys. Res. Commun. 279:223-228(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Fetal lung, Heart and Spleen.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Thymus.
    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].

    Entry informationi

    Entry nameiPA2GF_HUMAN
    AccessioniPrimary (citable) accession number: Q9BZM2
    Secondary accession number(s): Q5R385, Q8N217, Q9H506
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 11, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 115 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3