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Protein

Lipase

Gene
N/A
Organism
Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes ester bonds of triglycerides as well as of their derived partial glycerides with a strong 1,3-positional specificity.1 Publication

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Enzyme regulationi

Lipase activity is maximal at a lipid-water interface (interfacial activation), probably by an induced conformational change that results in an increased accessibility of the active site to the substrate.1 Publication

Kineticsi

  1. KM=4.4 mM for triolein1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei268Nucleophile1 Publication1
    Active sitei327Charge relay system1 Publication1
    Metal bindingi379CalciumBy similarity1
    Active sitei380Charge relay system1 Publication1

    GO - Molecular functioni

    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

    BRENDAi3.1.1.3. 5365.

    Protein family/group databases

    ESTHERirhidl-lipas. Lipase_3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipase (EC:3.1.1.3)
    Alternative name(s):
    RDL
    Triacylglycerol lipase
    Short name:
    ROL
    OrganismiRhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
    Taxonomic identifieri64495 [NCBI]
    Taxonomic lineageiEukaryotaFungiFungi incertae sedisMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi56C → S: Slows folding of the peptide to the mature protein. 1 Publication1
    Mutagenesisi151Y → F: Abolishes lipase activity. 1 Publication1
    Mutagenesisi206T → A or V: Abolishes lipase activity. 1 Publication1
    Mutagenesisi206T → S: Reduces lipase activity by 88%. Reduces lipase activity by 92%; when associated with W-212. 1 Publication1
    Mutagenesisi212A → W: Reduces lipase activity by 44%. Reduces lipase activity by 92%; when associated with S-206. 1 Publication1
    Mutagenesisi215D → N: Reduces lipase activity by 93%. 1 Publication1
    Mutagenesisi267H → F: Abolishes lipase activity. 1 Publication1
    Mutagenesisi267H → S: Reduces lipase activity by 98%. 1 Publication1
    Mutagenesisi327D → A: Abolishes lipase activity. 1 Publication1
    Mutagenesisi388E → D: Abolishes lipase activity. 1 Publication1

    Protein family/group databases

    Allergomei7694. Rhi o Lipase.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 26Sequence analysisAdd BLAST26
    PropeptideiPRO_000001773527 – 951 PublicationAdd BLAST69
    ChainiPRO_000001773696 – 392LipaseAdd BLAST297

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi152 ↔ 391
    Disulfide bondi163 ↔ 166
    Disulfide bondi358 ↔ 367

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond

    Structurei

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1TICX-ray2.60A/B124-392[»]
    ProteinModelPortaliP61872.
    SMRiP61872.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61872.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. Lipase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    OMAiLYQREPR.
    PhylomeDBiP61872.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002921. Fungal_lipase-like.
    [Graphical view]
    PfamiPF01764. Lipase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P61872-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVSFISISQG VSLCLLVSSM MLGSSAVPVS GKSGSSNTAV SASDNAALPP
    60 70 80 90 100
    LISSRCAPPS NKGSKSDLQA EPYNMQKNTE WYESHGGNLT SIGKRDDNLV
    110 120 130 140 150
    GGMTLDLPSD APPISLSSST NSASDGGKVV AATTAQIQEF TKYAGIAATA
    160 170 180 190 200
    YCRSVVPGNK WDCVQCQKWV PDGKIITTFT SLLSDTNGYV LRSDKQKTIY
    210 220 230 240 250
    LVFRGTNSFR SAITDIVFNF SDYKPVKGAK VHAGFLSSYE QVVNDYFPVV
    260 270 280 290 300
    QEQLTAHPTY KVIVTGHSLG GAQALLAGMD LYQREPRLSP KNLSIFTVGG
    310 320 330 340 350
    PRVGNPTFAY YVESTGIPFQ RTVHKRDIVP HVPPQSFGFL HPGVESWIKS
    360 370 380 390
    GTSNVQICTS EIETKDCSNS IVPFTSILDH LSYFDINEGS CL
    Length:392
    Mass (Da):42,139
    Last modified:June 7, 2004 - v1
    Checksum:iD08F651EE77AA5A3
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti37N → T in AAF32408 (PubMed:9765593).Curated1
    Sequence conflicti46A → S in AAF32408 (PubMed:9765593).Curated1
    Sequence conflicti74N → Y in AAF32408 (PubMed:9765593).Curated1
    Sequence conflicti118S → G (PubMed:9765593).Curated1
    Sequence conflicti118S → G (PubMed:15710378).Curated1
    Sequence conflicti257H → N in AAF32408 (PubMed:9765593).Curated1
    Sequence conflicti377I → L in AAF32408 (PubMed:9765593).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M38352 mRNA. Translation: AAA33878.1.
    AF229435 Genomic DNA. Translation: AAF32408.1.
    AY513724 Genomic DNA. Translation: AAS84458.1.
    PIRiJQ1390.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M38352 mRNA. Translation: AAA33878.1.
    AF229435 Genomic DNA. Translation: AAF32408.1.
    AY513724 Genomic DNA. Translation: AAS84458.1.
    PIRiJQ1390.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1TICX-ray2.60A/B124-392[»]
    ProteinModelPortaliP61872.
    SMRiP61872.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    Allergomei7694. Rhi o Lipase.
    ESTHERirhidl-lipas. Lipase_3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    OMAiLYQREPR.
    PhylomeDBiP61872.

    Enzyme and pathway databases

    BRENDAi3.1.1.3. 5365.

    Miscellaneous databases

    EvolutionaryTraceiP61872.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002921. Fungal_lipase-like.
    [Graphical view]
    PfamiPF01764. Lipase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiLIP_RHIOR
    AccessioniPrimary (citable) accession number: P61872
    Secondary accession number(s): P21811
    , Q12237, Q5J329, Q9P312
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: November 2, 2016
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Limited proteolysis produces a smaller peptide starting at residue Ser-124, that has altered substrate specificity and biophysicochemical properties.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.