LIPP_PIG
ID LIPP_PIG Reviewed; 450 AA.
AC P00591;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
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};
GN Name=PNLIP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE OF 308-449.
RX PubMed=7326260; DOI=10.1016/0005-2795(81)90126-4;
RA de Caro J.D., Boudouard M., Bonicel J.J., Guidoni A.A., Desnuelle P.,
RA Rovery M.;
RT "Porcine pancreatic lipase. Completion of the primary structure.";
RL Biochim. Biophys. Acta 671:129-138(1981).
RN [2]
RP PROTEIN SEQUENCE OF 1-234, AND GLYCOSYLATION AT ASN-167.
RX PubMed=380992; DOI=10.1111/j.1432-1033.1979.tb13126.x;
RA Bianchetta J.D., Bidaud J., Guidoni A.A., Bonicel J.J., Rovery M.;
RT "Porcine pancreatic lipase. Sequence of the first 234 amino acids of the
RT peptide chain.";
RL Eur. J. Biochem. 97:395-405(1979).
RN [3]
RP PROTEIN SEQUENCE OF 235-307.
RX PubMed=518929; DOI=10.1016/s0300-9084(79)80278-3;
RA Guidoni A.A., Bonicel J.J., Bianchetta J.D., Rovery M.;
RT "Porcine pancreatic lipase. Sequence between the 235th and 307th amino
RT acids.";
RL Biochimie 61:841-845(1979).
RN [4]
RP DISULFIDE BONDS.
RX PubMed=7151781;
RA Benkouka F., Guidoni A.A., de Caro J.D., Bonicel J.J., Desnuelle P.A.,
RA Rovery M.;
RT "Porcine pancreatic lipase. The disulfide bridges and the sulfhydryl
RT groups.";
RL Eur. J. Biochem. 128:331-341(1982).
RN [5]
RP SUBSTRATE-BINDING SITE.
RX PubMed=6791692; DOI=10.1016/0005-2744(81)90120-0;
RA Guidoni A.A., Benkouka F., de Caro J.D., Rovery M.;
RT "Characterization of the serine reacting with diethyl p-nitrophenyl
RT phosphate in porcine pancreatic lipase.";
RL Biochim. Biophys. Acta 660:148-150(1981).
RN [6]
RP STRUCTURE OF CARBOHYDRATE.
RX PubMed=3691527; DOI=10.1111/j.1432-1033.1987.tb13709.x;
RA Fournet B., Leroy Y., Montreuil J., Decaro J., Rovery M., van Kuik J.A.,
RA Vliegenthart J.F.G.;
RT "Primary structure of the glycans of porcine pancreatic lipase.";
RL Eur. J. Biochem. 170:369-371(1987).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SEQUENCE REVISION TO 30-32.
RX PubMed=8663362; DOI=10.1074/jbc.271.30.18007;
RA Hermoso J., Pignol D., Kerfelec B., Crenon I., Chapus C.,
RA Fontecilla-Camps J.-C.;
RT "Lipase activation by nonionic detergents. The crystal structure of the
RT porcine lipase-colipase-tetraethylene glycol monooctyl ether complex.";
RL J. Biol. Chem. 271:18007-18016(1996).
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:0000250|UniProtKB:P16233}.
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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/PL/";
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DR PIR; A90638; LIPG.
DR PDB; 1ETH; X-ray; 2.80 A; A/C=1-450.
DR PDBsum; 1ETH; -.
DR AlphaFoldDB; P00591; -.
DR SMR; P00591; -.
DR STRING; 9823.ENSSSCP00000011355; -.
DR BindingDB; P00591; -.
DR ChEMBL; CHEMBL1687677; -.
DR DrugCentral; P00591; -.
DR Allergome; 971; Sus s Lipase.
DR ESTHER; pig-1plip; Pancreatic_lipase.
DR iPTMnet; P00591; -.
DR PaxDb; P00591; -.
DR PRIDE; P00591; -.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR InParanoid; P00591; -.
DR BRENDA; 3.1.1.3; 6170.
DR EvolutionaryTrace; P00591; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Reference proteome; Secreted.
FT CHAIN 1..450
FT /note="Pancreatic triacylglycerol lipase"
FT /id="PRO_0000090356"
FT DOMAIN 339..450
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT ACT_SITE 153
FT /note="Nucleophile"
FT ACT_SITE 177
FT /note="Charge relay system"
FT ACT_SITE 264
FT /note="Charge relay system"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:380992"
FT DISULFID 4..10
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:7151781"
FT DISULFID 91..104
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:7151781"
FT DISULFID 91..102
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:7151781"
FT DISULFID 238..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:7151781"
FT DISULFID 286..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:7151781"
FT DISULFID 300..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:7151781"
FT DISULFID 434..450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:7151781"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 115..138
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:1ETH"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1ETH"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1ETH"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 254..274
FT /evidence="ECO:0007829|PDB:1ETH"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1ETH"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 339..349
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 352..364
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 382..391
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 395..405
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 416..425
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:1ETH"
SQ SEQUENCE 450 AA; 50084 MW; 76E13BBDB4541E0E CRC64;
SEVCFPRLGC FSDDAPWAGI VQRPLKILPW SPKDVDTRFL LYTNQNQNNY QELVADPSTI
TNSNFRMDRK TRFIIHGFID KGEEDWLSNI CKNLFKVESV NCICVDWKGG SRTGYTQASQ
NIRIVGAEVA YFVEVLKSSL GYSPSNVHVI GHSLGSHAAG EAGRRTNGTI ERITGLDPAE
PCFQGTPELV RLDPSDAKFV DVIHTDAAPI IPNLGFGMSQ TVGHLDFFPN GGKQMPGCQK
NILSQIVDID GIWEGTRDFV ACNHLRSYKY YADSILNPDG FAGFPCDSYN VFTANKCFPC
PSEGCPQMGH YADRFPGKTN GVSQVFYLNT GDASNFARWR YKVSVTLSGK KVTGHILVSL
FGNEGNSRQY EIYKGTLQPD NTHSDEFDSD VEVGDLQKVK FIWYNNNVIN PTLPRVGASK
ITVERNDGKV YDFCSQETVR EEVLLTLNPC
