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P39457

- PLB1_PENCH

UniProt

P39457 - PLB1_PENCH

Protein

Lysophospholipase

Gene
N/A
Organism
Penicillium chrysogenum (Penicillium notatum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      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 (EC:3.1.1.5)
    Alternative name(s):
    Phospholipase B
    OrganismiPenicillium chrysogenum (Penicillium notatum)
    Taxonomic identifieri5076 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei‹1 – 9›91 Publication
    Chaini10 – 612603LysophospholipasePRO_0000024639Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi25 ↔ ?Sequence Analysis
    Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi446 – 4461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi477 – 4771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi526 – 5261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi532 – 5321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi567 – 5671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi571 – 5711N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliP39457.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 571548PLA2cPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    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: Fragment.

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

    P39457-1 [UniParc]FASTAAdd to Basket

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    DITFAGVQRA LPNAPDGYVP TSVSCPASRP TVRSAAKLST NETSWLEVRR    50
    GKTLSALKDF FGHVKVGDYD VGAYLDKHSG NSSSLPNIGI AVSGGGWRAL 100
    MNGAGAVKAF DSRTDNATAT GHLGGLLQSA TYISGLSGGS WLLGSIYINN 150
    FTTVDKLQTH EAGSVWQFGN SIIEGPDAGG IQLLDSAGYY KDLADAVDGK 200
    KKAGFDTTLT DIWGRALSYQ MFNASNGGLS YTWSSIADTP EFQDGDYPMP 250
    FVVADGRNPG ELVIGSNSTV YEFNPWEFGT FDPTIFGFVP LEYLGSKFEG 300
    GSLPSNESCI RGFDSAGFVI GTSSSLFNQF LLQINTTSLP SFIKDVFNGI 350
    LFDLDKSQND IASYDPNPFY KYNEHSSPYA AQKLLDVVDG GEDGQNVPLH 400
    PLIQPERHVD VIFAVDSSAD TDYFWPNGTS LVATYERSLN SSGIANGTAF 450
    PAVPDQNTFI NLGLSTRPSF FGCDSSNQTG PSPLVVYIPN APYSYHSNIS 500
    TFQLSTDDAE RDNIILNGYE VATMANSTLD DNWTACVACA ILSRSFERTG 550
    TTLPDICSQC FDRYCWNGTV NSTRPESYDP AFYLADNSMA SVSLPTMLST 600
    VVAAGLAMLI LV 612
    Length:612
    Mass (Da):65,751
    Last modified:February 1, 1995 - v1
    Checksum:i7C32F819C3C1ABE5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60348 mRNA. Translation: CAA42906.1.
    PIRiS29318.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60348 mRNA. Translation: CAA42906.1 .
    PIRi S29318.

    3D structure databases

    ProteinModelPortali P39457.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Primary structure of protein moiety of Penicillium notatum phospholipase B deduced from the cDNA."
      Masuda N., Kitamura N., Saito K.
      Eur. J. Biochem. 202:783-787(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-20 AND 185-199.
      Strain: ATCC 34514 / NBRC 4640.

    Entry informationi

    Entry nameiPLB1_PENCH
    AccessioniPrimary (citable) accession number: P39457
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 65 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

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3