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P27657

- LIPP_RAT

UniProt

P27657 - LIPP_RAT

Protein

Pancreatic triacylglycerol lipase

Gene

Pnlip

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones.

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei169 – 1691NucleophileBy similarity
    Active sitei193 – 1931Charge relay systemPROSITE-ProRule annotation
    Metal bindingi204 – 2041Calcium; via carbonyl oxygenBy similarity
    Metal bindingi207 – 2071Calcium; via carbonyl oxygenBy similarity
    Metal bindingi209 – 2091CalciumBy similarity
    Metal bindingi212 – 2121CalciumBy similarity
    Active sitei280 – 2801Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. lipase activity Source: RGD
    2. metal ion binding Source: UniProtKB-KW
    3. triglyceride lipase activity Source: RGD

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW
    2. lipid metabolic process Source: RGD
    3. post-embryonic development Source: RGD
    4. response to lipid Source: RGD
    5. response to peptide hormone Source: RGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pancreatic triacylglycerol lipase (EC:3.1.1.3)
    Short name:
    PL
    Short name:
    Pancreatic lipase
    Gene namesi
    Name:Pnlip
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3360. Pnlip.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: RGD

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 16161 PublicationAdd
    BLAST
    Chaini17 – 465449Pancreatic triacylglycerol lipasePRO_0000017788Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi20 ↔ 26PROSITE-ProRule annotation
    Disulfide bondi107 ↔ 118PROSITE-ProRule annotation
    Disulfide bondi254 ↔ 278PROSITE-ProRule annotation
    Disulfide bondi302 ↔ 313PROSITE-ProRule annotation
    Disulfide bondi316 ↔ 321PROSITE-ProRule annotation
    Disulfide bondi449 ↔ 465PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP27657.
    PRIDEiP27657.

    Expressioni

    Tissue specificityi

    Pancreatic secretory (zymogen) granule.

    Inductioni

    By colipase/CLPS in the presence of bile salts.

    Gene expression databases

    GenevestigatoriP27657.

    Structurei

    3D structure databases

    ProteinModelPortaliP27657.
    SMRiP27657. Positions 18-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini355 – 465111PLATPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. Lipase family.Curated
    Contains 1 PLAT domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40923.
    HOGENOMiHOG000038552.
    HOVERGENiHBG003243.
    InParanoidiP27657.
    KOiK14073.
    PhylomeDBiP27657.

    Family and domain databases

    Gene3Di2.60.60.20. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR008976. Lipase_LipOase.
    IPR013818. Lipase_N.
    IPR002331. Lipase_panc.
    IPR016272. Lipoprotein_lipase_LIPH.
    IPR001024. PLAT/LH2_dom.
    [Graphical view]
    PANTHERiPTHR11610. PTHR11610. 1 hit.
    PfamiPF00151. Lipase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSiPR00823. PANCLIPASE.
    PR00821. TAGLIPASE.
    SMARTiSM00308. LH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49723. SSF49723. 1 hit.
    SSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P27657-1 [UniParc]FASTAAdd to Basket

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    MLMLWTFAVL LGAVAGKEVC FDKLGCFSDD APWSGTIDRP LKALPWSPAQ    50
    INTRFLLYTN ENQDNYQKIT SDASSIRNSN FKTNRKTRII IHGFIDKGEE 100
    NWLSDMCKNM FKVESVNCIC VDWKGGSRAT YTQATQNVRV VGAEVALLVN 150
    VLKSDLGHPP DNVHLIGHSL GSHVAGEAGK RTFGAIGRIT GLDAAEPYFQ 200
    GTPEEVRLDP TDAQFVDAIH TDAAPIIPNL GFGMSQTVGH LDFFPNGGME 250
    MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFSGF 300
    SCSSYNVFSA NKCFPCGSEG CPQMGHYADK YPGKTKELYQ KFYLNTGDKS 350
    NFARWRYQVT VTLSGQKVTG HILVSLFGNG GNSKQYEVFK GSLHPGDTHV 400
    KEFDSDMDVG DLQKVKFIWY NNVINPTLPK VGASRISVER NDGRVFNFCS 450
    QDTVREDVLL TLSAC 465
    Length:465
    Mass (Da):51,440
    Last modified:August 1, 1992 - v1
    Checksum:iCF014D58AA09A6A2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58369 mRNA. Translation: AAA79888.1.
    RefSeqiNP_037293.1. NM_013161.2.
    UniGeneiRn.10130.

    Genome annotation databases

    GeneIDi25702.
    KEGGirno:25702.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58369 mRNA. Translation: AAA79888.1 .
    RefSeqi NP_037293.1. NM_013161.2.
    UniGenei Rn.10130.

    3D structure databases

    ProteinModelPortali P27657.
    SMRi P27657. Positions 18-465.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi P27657.
    PRIDEi P27657.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25702.
    KEGGi rno:25702.

    Organism-specific databases

    CTDi 5406.
    RGDi 3360. Pnlip.

    Phylogenomic databases

    eggNOGi NOG40923.
    HOGENOMi HOG000038552.
    HOVERGENi HBG003243.
    InParanoidi P27657.
    KOi K14073.
    PhylomeDBi P27657.

    Miscellaneous databases

    NextBioi 607735.
    PROi P27657.

    Gene expression databases

    Genevestigatori P27657.

    Family and domain databases

    Gene3Di 2.60.60.20. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR008976. Lipase_LipOase.
    IPR013818. Lipase_N.
    IPR002331. Lipase_panc.
    IPR016272. Lipoprotein_lipase_LIPH.
    IPR001024. PLAT/LH2_dom.
    [Graphical view ]
    PANTHERi PTHR11610. PTHR11610. 1 hit.
    Pfami PF00151. Lipase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSi PR00823. PANCLIPASE.
    PR00821. TAGLIPASE.
    SMARTi SM00308. LH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49723. SSF49723. 1 hit.
    SSF53474. SSF53474. 1 hit.
    PROSITEi PS00120. LIPASE_SER. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rat pancreatic lipase and two related proteins: enzymatic properties and mRNA expression during development."
      Payne R.M., Sims H.F., Jennens M.L., Lowe M.E.
      Am. J. Physiol. 266:G914-G921(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Identification and cloning of GP-3 from rat pancreatic acinar zymogen granules as a glycosylated membrane-associated lipase."
      Wishart M.J., Andrews P.C., Nichols R., Blevins G.T. Jr., Logsdon C.D., Williams J.A.
      J. Biol. Chem. 268:10303-10311(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-37.
      Strain: Sprague-Dawley.
      Tissue: Pancreas.
    3. "Hydrolysis of retinyl esters by pancreatic triglyceride lipase."
      van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H.
      Biochemistry 39:4900-4906(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiLIPP_RAT
    AccessioniPrimary (citable) accession number: P27657
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3