LIPP_RAT
ID LIPP_RAT Reviewed; 465 AA.
AC P27657;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Pancreatic triacylglycerol lipase {ECO:0000305};
DE Short=PL;
DE Short=Pancreatic lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:10769148};
DE Flags: Precursor;
GN Name=Pnlip {ECO:0000312|RGD:3360};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8203536; DOI=10.1152/ajpgi.1994.266.5.g914;
RA Payne R.M., Sims H.F., Jennens M.L., Lowe M.E.;
RT "Rat pancreatic lipase and two related proteins: enzymatic properties and
RT mRNA expression during development.";
RL Am. J. Physiol. 266:G914-G921(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 17-37.
RC STRAIN=Sprague-Dawley; TISSUE=Pancreas;
RX PubMed=8486693; DOI=10.1016/s0021-9258(18)82203-7;
RA Wishart M.J., Andrews P.C., Nichols R., Blevins G.T. Jr., Logsdon C.D.,
RA Williams J.A.;
RT "Identification and cloning of GP-3 from rat pancreatic acinar zymogen
RT granules as a glycosylated membrane-associated lipase.";
RL J. Biol. Chem. 268:10303-10311(1993).
RN [3]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=10769148; DOI=10.1021/bi9927235;
RA van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H.;
RT "Hydrolysis of retinyl esters by pancreatic triglyceride lipase.";
RL Biochemistry 39:4900-4906(2000).
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. {ECO:0000269|PubMed:10769148,
CC ECO:0000269|PubMed:8203536}.
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:0000269|PubMed:10769148};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:10769148};
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:0000269|PubMed:10769148, ECO:0000269|PubMed:8203536};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:10769148, ECO:0000305|PubMed:8203536};
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=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:0000269|PubMed:8203536}.
CC -!- SUBUNIT: Forms a 1:1 stoichiometric complex with (pro)colipase/CLPS.
CC {ECO:0000250|UniProtKB:P16233}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:8203536}.
CC -!- TISSUE SPECIFICITY: Expressed by the pancreas (PubMed:8203536).
CC Pancreatic secretory (zymogen) granule. {ECO:0000269|PubMed:8203536}.
CC -!- DEVELOPMENTAL STAGE: Expressed a low levels in pancreas at birth,
CC expression increases through the suckling-weanling period to reach
CC adult levels by the time of weaning. {ECO:0000269|PubMed:8203536}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; M58369; AAA79888.1; -; mRNA.
DR RefSeq; NP_037293.1; NM_013161.2.
DR AlphaFoldDB; P27657; -.
DR SMR; P27657; -.
DR STRING; 10116.ENSRNOP00000024065; -.
DR GuidetoPHARMACOLOGY; 2590; -.
DR ESTHER; ratno-1plip; Pancreatic_lipase.
DR PaxDb; P27657; -.
DR PRIDE; P27657; -.
DR GeneID; 25702; -.
DR KEGG; rno:25702; -.
DR CTD; 5406; -.
DR RGD; 3360; Pnlip.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR InParanoid; P27657; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; P27657; -.
DR Reactome; R-RNO-192456; Digestion of dietary lipid.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:P27657; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR GO; GO:0016298; F:lipase activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:RGD.
DR GO; GO:0030299; P:intestinal cholesterol absorption; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IDA:RGD.
DR GO; GO:0061365; P:positive regulation of triglyceride lipase activity; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; IDA:RGD.
DR GO; GO:0033993; P:response to lipid; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
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; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:8486693"
FT CHAIN 17..465
FT /note="Pancreatic triacylglycerol lipase"
FT /id="PRO_0000017788"
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"
SQ SEQUENCE 465 AA; 51440 MW; CF014D58AA09A6A2 CRC64;
MLMLWTFAVL LGAVAGKEVC FDKLGCFSDD APWSGTIDRP LKALPWSPAQ INTRFLLYTN
ENQDNYQKIT SDASSIRNSN FKTNRKTRII IHGFIDKGEE NWLSDMCKNM FKVESVNCIC
VDWKGGSRAT YTQATQNVRV VGAEVALLVN VLKSDLGHPP 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 QDTVREDVLL TLSAC
