LIPP_ICTTR
ID LIPP_ICTTR Reviewed; 465 AA.
AC O88354; Q9QWF3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Pancreatic triacylglycerol lipase {ECO:0000305};
DE Short=PL;
DE Short=PTL;
DE Short=Pancreatic lipase;
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:P16233};
DE AltName: Full=Heart pancreatic lipase;
DE AltName: Full=PL-h;
DE Flags: Precursor;
GN Name=PNLIP; Synonyms=PTL;
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND FUNCTION IN HIBERNATION.
RC TISSUE=Heart;
RX PubMed=9653197; DOI=10.1073/pnas.95.14.8392;
RA Andrews M.T., Squire T.L., Bowen C.M., Rollins M.B.;
RT "Low-temperature carbon utilization is regulated by novel gene activity in
RT the heart of a hibernating mammal.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8392-8397(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=14583598; DOI=10.1152/physiolgenomics.00167.2002;
RA Squire T.L., Andrews M.T.;
RT "Pancreatic triacylglycerol lipase in a hibernating mammal. I. Novel
RT genomic organization.";
RL Physiol. Genomics 16:119-130(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=White adipose tissue;
RA Bauer V.W., Andrews M.T.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=14583599; DOI=10.1152/physiolgenomics.00168.2002;
RA Squire T.L., Lowe M.E., Bauer V.W., Andrews M.T.;
RT "Pancreatic triacylglycerol lipase in a hibernating mammal. II. Cold-
RT adapted function and differential expression.";
RL Physiol. Genomics 16:131-140(2003).
CC -!- FUNCTION: Plays an important role in fat metabolism. It preferentially
CC splits the esters of long-chain fatty acids at positions 1 and 3,
CC producing mainly 2-monoacylglycerol and free fatty acids, and shows
CC considerably higher activity against insoluble emulsified substrates
CC than against soluble ones (By similarity). Plays a role in hibernation
CC as a key enzyme that shows high activity at low temperatures. When
CC expressed in the hibernating heart it liberates fatty acids from
CC triglycerides at temperatures as low as 0 degrees Celsius.
CC {ECO:0000250|UniProtKB:P16233, ECO:0000269|PubMed:9653197}.
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:0000250|UniProtKB:P16233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:P16233};
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:0000250|UniProtKB:P16233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000250|UniProtKB:P16233};
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:0000250|UniProtKB:P16233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000250|UniProtKB:P16233};
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:0000250|UniProtKB:P16233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000250|UniProtKB:P16233};
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:0000250|UniProtKB:P16233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38456;
CC Evidence={ECO:0000250|UniProtKB:P16233};
CC -!- ACTIVITY REGULATION: Inhibited by bile salts, is reactivated by
CC (pro)colipase/CLPS. {ECO:0000250|UniProtKB:P16233}.
CC -!- SUBUNIT: Forms a 1:1 stoichiometric complex with (pro)colipase/CLPS.
CC {ECO:0000250|UniProtKB:P16233}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16233}.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues with highest expression
CC in liver. During hibernation there is a significant increases in
CC expression in heart, white adipose tissue (WAT), and testis; but not in
CC pancreas. {ECO:0000269|PubMed:14583599}.
CC -!- INDUCTION: Up-regulated during hibernation.
CC {ECO:0000269|PubMed:9653197}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AF027293; AAC40162.2; -; mRNA.
DR EMBL; AF395870; AAK72259.1; -; mRNA.
DR EMBL; AF177402; AAD51123.2; -; mRNA.
DR EMBL; AF177403; AAD51124.1; -; mRNA.
DR AlphaFoldDB; O88354; -.
DR SMR; O88354; -.
DR STRING; 43179.ENSSTOP00000002036; -.
DR ESTHER; icttr-k7gt76; Pancreatic_lipase.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR InParanoid; O88354; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0042750; P:hibernation; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; -; 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; PTHR11610; 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; SSF49723; SSF49723; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Hibernation; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..465
FT /note="Pancreatic triacylglycerol lipase"
FT /id="PRO_0000250516"
FT DOMAIN 355..465
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 280
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 20..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 107..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 254..278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 302..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 316..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 449..465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT CONFLICT 133
FT /note="Q -> H (in Ref. 3; AAD51123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 51227 MW; A152FB00CD01169B CRC64;
MLLVWSLALL LGAVAGKEVC YDRLGCFSDD SPWSGIVERP LKVLPWSPAD VNTRFLLYTN
ENQDNYQQIT ADSSRIQSSN FKTNRKTRFI IHGFIDKGEE SWLANMCKKM FQVESVNCIC
VDWKGGSRTG YTQASQNIRI VGAEVAYFVD FLRTQLGYSP SNVHVIGHSL GSHAAGEAGR
RTNGAIGRIT GLDPAEPCFE GTPELVRLDP SDAQFVDAIH TDGAPIVPNL GFGMSQTVGH
LDFFPNGGIE MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFAAF
SCASYSVFSA NKCFPCPSGG CPQMGHYADR YSGKTNGVGQ KFYLNTGDKS NFSRWRYKVS
VTLSGQKVTG HILVSLFGNA GNSKQYEIYK GSLHPGYTHS NEFDSDVDVG DLQRVKFIWY
NNVINPSLPR VGASSISVER NDGRVFKFCS AETVREDVLL TLNAC
