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O88354

- LIPP_SPETR

UniProt

O88354 - LIPP_SPETR

Protein

Pancreatic triacylglycerol lipase

Gene

PNLIP

Organism
Spermophilus tridecemlineatus (Thirteen-lined ground squirrel) (Ictidomys tridecemlineatus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 2 (01 May 2000)
      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 By similarity. Plays a role in hibernation as a key enzyme that shows high activity at low temperatures. When expressed in the hibernating heart it liberates fatty acids from triglycerides at temperatures as low as 0 degrees Celsius.By similarity1 Publication

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.

    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. metal ion binding Source: UniProtKB-KW
    2. triglyceride lipase activity Source: UniProtKB-EC

    GO - Biological processi

    1. hibernation Source: UniProtKB-KW
    2. lipid catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Hibernation, 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:
    PTL
    Short name:
    Pancreatic lipase
    Alternative name(s):
    Heart pancreatic lipase
    PL-h
    Gene namesi
    Name:PNLIP
    Synonyms:PTL
    OrganismiSpermophilus tridecemlineatus (Thirteen-lined ground squirrel) (Ictidomys tridecemlineatus)
    Taxonomic identifieri43179 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiSciuridaeXerinaeMarmotiniIctidomys
    ProteomesiUP000005215: Unplaced

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616By similarityAdd
    BLAST
    Chaini17 – 465449Pancreatic triacylglycerol lipasePRO_0000250516Add
    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

    Expressioni

    Tissue specificityi

    Expressed in many tissues with highest expression in liver. During hibernation there is a significant increases in expression in heart, white adipose tissue (WAT), and testis; but not in pancreas.1 Publication

    Inductioni

    By colipase/CLPS in the presence of bile salts. Up-regulated during hibernation.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliO88354.
    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

    HOGENOMiHOG000038552.
    HOVERGENiHBG003243.

    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.

    O88354-1 [UniParc]FASTAAdd to Basket

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    MLLVWSLALL LGAVAGKEVC YDRLGCFSDD SPWSGIVERP LKVLPWSPAD    50
    VNTRFLLYTN ENQDNYQQIT ADSSRIQSSN FKTNRKTRFI IHGFIDKGEE 100
    SWLANMCKKM FQVESVNCIC VDWKGGSRTG YTQASQNIRI VGAEVAYFVD 150
    FLRTQLGYSP SNVHVIGHSL GSHAAGEAGR RTNGAIGRIT GLDPAEPCFE 200
    GTPELVRLDP SDAQFVDAIH TDGAPIVPNL GFGMSQTVGH LDFFPNGGIE 250
    MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFAAF 300
    SCASYSVFSA NKCFPCPSGG CPQMGHYADR YSGKTNGVGQ KFYLNTGDKS 350
    NFSRWRYKVS VTLSGQKVTG HILVSLFGNA GNSKQYEIYK GSLHPGYTHS 400
    NEFDSDVDVG DLQRVKFIWY NNVINPSLPR VGASSISVER NDGRVFKFCS 450
    AETVREDVLL TLNAC 465
    Length:465
    Mass (Da):51,227
    Last modified:May 1, 2000 - v2
    Checksum:iA152FB00CD01169B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti133 – 1331Q → H in AAD51123. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027293 mRNA. Translation: AAC40162.2.
    AF395870 mRNA. Translation: AAK72259.1.
    AF177402 mRNA. Translation: AAD51123.2.
    AF177403 mRNA. Translation: AAD51124.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027293 mRNA. Translation: AAC40162.2 .
    AF395870 mRNA. Translation: AAK72259.1 .
    AF177402 mRNA. Translation: AAD51123.2 .
    AF177403 mRNA. Translation: AAD51124.1 .

    3D structure databases

    ProteinModelPortali O88354.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOGENOMi HOG000038552.
    HOVERGENi HBG003243.

    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. "Low-temperature carbon utilization is regulated by novel gene activity in the heart of a hibernating mammal."
      Andrews M.T., Squire T.L., Bowen C.M., Rollins M.B.
      Proc. Natl. Acad. Sci. U.S.A. 95:8392-8397(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, FUNCTION IN HIBERNATION.
      Tissue: Heart.
    2. "Pancreatic triacylglycerol lipase in a hibernating mammal. I. Novel genomic organization."
      Squire T.L., Andrews M.T.
      Physiol. Genomics 16:119-130(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pancreas.
    3. Bauer V.W., Andrews M.T.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: White adipose tissue.
    4. "Pancreatic triacylglycerol lipase in a hibernating mammal. II. Cold-adapted function and differential expression."
      Squire T.L., Lowe M.E., Bauer V.W., Andrews M.T.
      Physiol. Genomics 16:131-140(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiLIPP_SPETR
    AccessioniPrimary (citable) accession number: O88354
    Secondary accession number(s): Q9QWF3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 88 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3