ID   Q9QUN4_RAT              Unreviewed;       451 AA.
AC   Q9QUN4;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Pancreatic triacylglycerol lipase {ECO:0000256|ARBA:ARBA00040450};
DE            EC=3.1.1.3 {ECO:0000256|ARBA:ARBA00013279};
DE   Flags: Fragment;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:BAA13638.1};
RN   [1] {ECO:0000313|EMBL:BAA13638.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wistar-King {ECO:0000313|EMBL:BAA13638.1};
RC   TISSUE=Pancreas {ECO:0000313|EMBL:BAA13638.1};
RA   Tsujita T., Sumida M., Sumiyoshi M., Kameda K., Okuda H.;
RT   "Direct evidence that alkaline lipase from Rat brain is the same enzyme as
RT   pancreatic lipase from Rat Pancreas.";
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAA13637.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wistar-King {ECO:0000313|EMBL:BAA13637.1};
RA   Sumida M.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:BAA13637.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wistar-King {ECO:0000313|EMBL:BAA13637.1};
RA   Takahiro T.;
RT   "Direct evidence that alkaline lipase from Rat brain is the same enzyme as
RT   pancreatic lipase from Rat Pancreas.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC         octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC         Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC         Evidence={ECO:0000256|ARBA:ARBA00000652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC         Evidence={ECO:0000256|ARBA:ARBA00000652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC         dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC         ChEBI:CHEBI:76478; Evidence={ECO:0000256|ARBA:ARBA00001601};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC         Evidence={ECO:0000256|ARBA:ARBA00001601};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC         (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38455,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:52323, ChEBI:CHEBI:75937;
CC         Evidence={ECO:0000256|ARBA:ARBA00023366};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38456;
CC         Evidence={ECO:0000256|ARBA:ARBA00023366};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00023369};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC         Evidence={ECO:0000256|ARBA:ARBA00023369};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol +
CC         H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC         ChEBI:CHEBI:17616; Evidence={ECO:0000256|ARBA:ARBA00023384};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC         Evidence={ECO:0000256|ARBA:ARBA00023384};
CC   -!- SUBUNIT: Forms a 1:1 stoichiometric complex with (pro)colipase/CLPS.
CC       {ECO:0000256|ARBA:ARBA00038559}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR   EMBL; D88534; BAA13637.1; -; mRNA.
DR   EMBL; D88535; BAA13638.1; -; mRNA.
DR   AlphaFoldDB; Q9QUN4; -.
DR   SMR; Q9QUN4; -.
DR   ESTHER; ratno-1plip; Pancreatic_lipase.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR016272; Lipase_LIPH.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR002331; Lipase_panc.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610; LIPASE; 1.
DR   PANTHER; PTHR11610:SF147; PANCREATIC TRIACYLGLYCEROL LIPASE; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR   PRINTS; PR00823; PANCLIPASE.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SMART; SM00308; LH2; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000865-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..451
FT                   /note="Pancreatic triacylglycerol lipase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013536776"
FT   DOMAIN          355..451
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        193
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        280
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   BINDING         204
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   BINDING         207
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   BINDING         209
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   BINDING         212
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   NON_TER         451
FT                   /evidence="ECO:0000313|EMBL:BAA13638.1"
SQ   SEQUENCE   451 AA;  49939 MW;  65D19706B5D5B732 CRC64;
     MLMLWTFAVL LGAVAGKEVC FDKLGCFSDD APWSGTIDRP LKALPWSPAQ INTRFLLYTN
     ENQDNYQKIT SDASSIRNSN FKTNRKTRII IHGFIDKGEE NWLSDMCKNM FKVESVNCIC
     VDWKGGSRAT YTQATQNVRV VGAEVALLVN VLKSDLGYSP DNVHLIGHSL GSHVAGEAGK
     RTFGAIGRIT GLDAAEPYFQ GTPEEVRLDP TDAQFVDAIH TDAAPIIPNL GFGMSQTVGH
     LDFFPNGGME MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFSGF
     SCSSYNVFSA NKCFPCGSEG CPQMGHYADK YPGKTKELYQ KFYLNTGDKS NFARWRYQVT
     VTLSGQKVTG HILVSLFGNG GNSKQYEVFK GSLHPGDTHV KEFDSDMDVG DLQKVKFIWY
     NNVINPTLPK VGASRISVER NDGRVFNFCS Q
//