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P29183

- LIPP_HORSE

UniProt

P29183 - LIPP_HORSE

Protein

Pancreatic triacylglycerol lipase

Gene

PNLIP

Organism
Equus caballus (Horse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei165 – 1651Nucleophile
    Active sitei189 – 1891Charge relay system
    Metal bindingi200 – 2001Calcium; via carbonyl oxygen
    Metal bindingi203 – 2031Calcium; via carbonyl oxygen
    Metal bindingi205 – 2051Calcium
    Metal bindingi208 – 2081Calcium
    Active sitei276 – 2761Charge relay system

    GO - Molecular functioni

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

    GO - Biological processi

    1. intestinal cholesterol absorption Source: Ensembl
    2. lipid catabolic process Source: UniProtKB-KW

    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:
    PTL
    Short name:
    Pancreatic lipase
    Gene namesi
    Name:PNLIP
    OrganismiEquus caballus (Horse)
    Taxonomic identifieri9796 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
    ProteomesiUP000002281: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi165 – 1651S → X: 80% loss of P-nitrophenyl acetate hydrolysis activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei‹1 – 12›12Add
    BLAST
    Chaini13 – 461449Pancreatic triacylglycerol lipasePRO_0000017784Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi16 ↔ 22
    Disulfide bondi103 ↔ 114
    Disulfide bondi250 ↔ 274
    Disulfide bondi298 ↔ 309
    Disulfide bondi312 ↔ 317
    Disulfide bondi445 ↔ 461

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Inductioni

    By colipase/CLPS in the presence of bile salts.

    Interactioni

    Protein-protein interaction databases

    STRINGi9796.ENSECAP00000007877.

    Structurei

    Secondary structure

    1
    461
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 174
    Turni18 – 203
    Beta strandi21 – 244
    Beta strandi29 – 324
    Helixi44 – 474
    Beta strandi50 – 556
    Beta strandi58 – 658
    Helixi69 – 746
    Beta strandi81 – 877
    Helixi98 – 10912
    Beta strandi112 – 1187
    Helixi120 – 1234
    Helixi127 – 15226
    Helixi156 – 1583
    Beta strandi159 – 1646
    Helixi167 – 17711
    Turni178 – 1803
    Beta strandi182 – 1898
    Turni193 – 1975
    Turni200 – 2023
    Helixi206 – 2083
    Beta strandi209 – 2157
    Helixi222 – 2254
    Beta strandi235 – 2417
    Helixi261 – 2655
    Helixi274 – 28815
    Helixi301 – 3055
    Beta strandi319 – 3213
    Helixi324 – 3263
    Turni328 – 3314
    Beta strandi332 – 3409
    Beta strandi344 – 3474
    Beta strandi351 – 36111
    Beta strandi364 – 37411
    Beta strandi382 – 3898
    Beta strandi394 – 40310
    Beta strandi407 – 41711
    Beta strandi427 – 4359
    Beta strandi441 – 4455
    Beta strandi456 – 4616

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HPLX-ray2.30A/B13-461[»]
    ProteinModelPortaliP29183.
    SMRiP29183. Positions 13-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29183.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini351 – 461111PLATPROSITE-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.
    InParanoidiP29183.
    KOiK14073.

    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: Fragment.

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

    P29183-1 [UniParc]FASTAAdd to Basket

    « Hide

    WTLSLLLGAV VGNEVCYERL GCFSDDSPWA GIVERPLKIL PWSPEKVNTR    50
    FLLYTNENPD NFQEIVADPS TIQSSNFNTG RKTRFIIHGF IDKGEESWLS 100
    TMCQNMFKVE SVNCICVDWK SGSRTAYSQA SQNVRIVGAE VAYLVGVLQS 150
    SFDYSPSNVH IIGHSLGSHA AGEAGRRTNG AVGRITGLDP AEPCFQGTPE 200
    LVRLDPSDAQ FVDVIHTDIA PFIPNLGFGM SQTAGHLDFF PNGGKEMPGC 250
    QKNVLSQIVD IDGIWQGTRD FAACNHLRSY KYYTDSILNP DGFAGFSCAS 300
    YSDFTANKCF PCSSEGCPQM GHYADRFPGR TKGVGQLFYL NTGDASNFAR 350
    WRYRVDVTLS GKKVTGHVLV SLFGNKGNSR QYEIFQGTLK PDNTYSNEFD 400
    SDVEVGDLEK VKFIWYNNVI NLTLPKVGAS KITVERNDGS VFNFCSEETV 450
    REDVLLTLTA C 461
    Length:461
    Mass (Da):50,921
    Last modified:April 1, 1993 - v2
    Checksum:i382F33F3CE446738
    GO

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66218 mRNA. Translation: CAA46961.1.
    PIRiS21223.
    RefSeqiNP_001157421.1. NM_001163949.1.
    UniGeneiEca.12462.

    Genome annotation databases

    GeneIDi100034202.
    KEGGiecb:100034202.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66218 mRNA. Translation: CAA46961.1 .
    PIRi S21223.
    RefSeqi NP_001157421.1. NM_001163949.1.
    UniGenei Eca.12462.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HPL X-ray 2.30 A/B 13-461 [» ]
    ProteinModelPortali P29183.
    SMRi P29183. Positions 13-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9796.ENSECAP00000007877.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100034202.
    KEGGi ecb:100034202.

    Organism-specific databases

    CTDi 5406.

    Phylogenomic databases

    eggNOGi NOG40923.
    HOGENOMi HOG000038552.
    HOVERGENi HBG003243.
    InParanoidi P29183.
    KOi K14073.

    Miscellaneous databases

    EvolutionaryTracei P29183.

    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. "Sequence of horse pancreatic lipase as determined by protein and cDNA sequencing. Implications for p-nitrophenyl acetate hydrolysis by pancreatic lipases."
      Kerfelec B., Foglizzo E., Bonicel J., Bougis P.E., Chapus C.
      Eur. J. Biochem. 206:279-287(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Horse pancreatic lipase. The crystal structure refined at 2.3-A resolution."
      Bourne Y., Martinez C., Kerfelec B., Lombardo D., Chapus C., Cambillau C.
      J. Mol. Biol. 238:709-732(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiLIPP_HORSE
    AccessioniPrimary (citable) accession number: P29183
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 110 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3