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B0Y665

- PLB1_ASPFC

UniProt

B0Y665 - PLB1_ASPFC

Protein

Lysophospholipase 1

Gene

plb1

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 29 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the release of fatty acids from lysophospholipids.

    Catalytic activityi

    2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

    GO - Molecular functioni

    1. lysophospholipase activity Source: UniProtKB-EC

    GO - Biological processi

    1. phospholipid catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysophospholipase 1 (EC:3.1.1.5)
    Alternative name(s):
    Phospholipase B 1
    Gene namesi
    Name:plb1
    ORF Names:AFUB_065820
    OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
    Taxonomic identifieri451804 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000001699: Unassembled WGS sequence

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Protein family/group databases

    Allergomei8989. Asp f LPL1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 609589Lysophospholipase 1PRO_0000372611Add
    BLAST
    Propeptidei610 – 63324Removed in mature formSequence AnalysisPRO_0000372612Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi246 – 2461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi450 – 4501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi469 – 4691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi497 – 4971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi500 – 5001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi521 – 5211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi549 – 5491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi555 – 5551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi594 – 5941N-linked (GlcNAc...)Sequence Analysis
    Lipidationi609 – 6091GPI-like-anchor amidated serineSequence Analysis

    Post-translational modificationi

    The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.

    Keywords - PTMi

    Glycoprotein, GPI-anchor, Lipoprotein

    Expressioni

    Inductioni

    Induced by lecithin.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliB0Y665.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini47 – 594548PLA2cPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the lysophospholipase family.Curated
    Contains 1 PLA2c domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000189547.
    OrthoDBiEOG7N37NC.
    PhylomeDBiB0Y665.

    Family and domain databases

    InterProiIPR016035. Acyl_Trfase/lysoPLipase.
    IPR002642. LysoPLipase_cat_dom.
    [Graphical view]
    PfamiPF01735. PLA2_B. 1 hit.
    [Graphical view]
    SMARTiSM00022. PLAc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52151. SSF52151. 1 hit.
    PROSITEiPS51210. PLA2C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    B0Y665-1 [UniParc]FASTAAdd to Basket

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    MKTTTVACAV AGLLFSCVSG APDPVHVEIQ QRALPNAPDG YTPSTVGCPA    50
    SRPTIRSAAS LSPNETSWLE TRRGKTTSAM KDFFNHVKIQ DFDAAGYIDR 100
    HSSNSSDLPN IGIAVSGGGY RALMNGAGAI KAFDSRTPNS TSAGQLGGLL 150
    QSATYLSGLS GGSWLVGSIY INNFTTISAL QTHQKGTVWQ FQNSIFEGPD 200
    GGSIQILDSA TYYRDISNAV SGKSDAGYPT SITDYWGRAL SYQMINATNG 250
    GPSYTWSSIA LTDAFQKAEM PMPLVVADGR YPGELLISSN ATVYEFNPWE 300
    FGTFDPTVFG FAPLEYLGTK FNGGSVPSNE SCVRGFDNVG FVMGTSSTLF 350
    NQFLLQINST ALPDWLKSVF TDILKDIGEN DEDIAQYAPN PFYHFSNTTN 400
    PSAAELELDL VDGGEDLQNI PLHPLIQPER HVDVIFAVDS SADTTYSWPN 450
    GTALVATYER SLNSSGIANG TSFPAIPDQN TFVNKGLNTR PTFFGCNSSN 500
    TTGPSPLIVY LPNYPYTAYS NFSTFQPDYT EQERDSTILN GYDVVTMGNS 550
    TRDGNWSTCV GCAILSRSLE RTNTNVPEIC KQCFQRYCWD GSLNSTTPAG 600
    YEPVTILDSA ASGIIPSIST VAMAVVFAAW TIF 633
    Length:633
    Mass (Da):68,144
    Last modified:April 8, 2008 - v1
    Checksum:i277A47E29FD74796
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY376592 mRNA. Translation: AAQ85122.1.
    DS499598 Genomic DNA. Translation: EDP50250.1.

    Genome annotation databases

    EnsemblFungiiCADAFUBT00006532; CADAFUBP00006407; CADAFUBG00006532.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY376592 mRNA. Translation: AAQ85122.1 .
    DS499598 Genomic DNA. Translation: EDP50250.1 .

    3D structure databases

    ProteinModelPortali B0Y665.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 8989. Asp f LPL1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUBT00006532 ; CADAFUBP00006407 ; CADAFUBG00006532 .

    Phylogenomic databases

    HOGENOMi HOG000189547.
    OrthoDBi EOG7N37NC.
    PhylomeDBi B0Y665.

    Family and domain databases

    InterProi IPR016035. Acyl_Trfase/lysoPLipase.
    IPR002642. LysoPLipase_cat_dom.
    [Graphical view ]
    Pfami PF01735. PLA2_B. 1 hit.
    [Graphical view ]
    SMARTi SM00022. PLAc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52151. SSF52151. 1 hit.
    PROSITEi PS51210. PLA2C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterisation and expression of phospholipases B from the opportunistic fungus Aspergillus fumigatus."
      Shen D.-K., Noodeh A.D., Kazemi A., Grillot R., Robson G.D., Brugere J.-F.
      FEMS Microbiol. Lett. 239:87-93(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CEA10 / CBS 144.89 / FGSC A1163.
    3. "Proteome analysis of Aspergillus fumigatus identifies glycosylphosphatidylinositol-anchored proteins associated to the cell wall biosynthesis."
      Bruneau J.-M., Magnin T., Tagat E., Legrand R., Bernard M., Diaquin M., Fudali C., Latge J.-P.
      Electrophoresis 22:2812-2823(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 89-100 AND 122-131, GPI-ANCHOR.
    4. "Structures of the glycosylphosphatidylinositol membrane anchors from Aspergillus fumigatus membrane proteins."
      Fontaine T., Magnin T., Melhert A., Lamont D., Latge J.-P., Ferguson M.A.J.
      Glycobiology 13:169-177(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 90-98, STRUCTURE OF GPI-ANCHOR.

    Entry informationi

    Entry nameiPLB1_ASPFC
    AccessioniPrimary (citable) accession number: B0Y665
    Secondary accession number(s): Q4WPC0, Q6U820, Q9P8P5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 29 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3