ID G1S348_NOMLE Unreviewed; 465 AA.
AC G1S348;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Triacylglycerol lipase {ECO:0000256|RuleBase:RU362046};
DE EC=3.1.1.3 {ECO:0000256|RuleBase:RU362046};
DE AltName: Full=Pancreatic lipase {ECO:0000256|RuleBase:RU362046};
GN Name=PNLIP {ECO:0000313|Ensembl:ENSNLEP00000019936.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000019936.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000019936.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000019936.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 ECO:0000256|RuleBase:RU362046}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
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DR EMBL; ADFV01164275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01164276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003255037.1; XM_003254989.2.
DR AlphaFoldDB; G1S348; -.
DR STRING; 61853.ENSNLEP00000019936; -.
DR ESTHER; nomle-g1s348; Pancreatic_lipase.
DR Ensembl; ENSNLET00000020935.2; ENSNLEP00000019936.1; ENSNLEG00000016413.2.
DR GeneID; 100581408; -.
DR KEGG; nle:100581408; -.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR GeneTree; ENSGT00940000160632; -.
DR HOGENOM; CLU_027171_0_2_1; -.
DR InParanoid; G1S348; -.
DR OMA; RNIDLTP; -.
DR OrthoDB; 3428256at2759; -.
DR TreeFam; TF324997; -.
DR Proteomes; UP000001073; Chromosome 3.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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; IEA:UniProtKB-EC.
DR GO; GO:0030299; P:intestinal cholesterol absorption; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR CDD; cd01759; PLAT_PL; 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 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000865-3, ECO:0000256|PROSITE-
KW ProRule:PRU00152}; Lipid degradation {ECO:0000256|RuleBase:RU362046};
KW Lipid metabolism {ECO:0000256|RuleBase:RU362046};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU362046};
KW Signal {ECO:0000256|RuleBase:RU362046}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU362046"
FT CHAIN 17..465
FT /note="Triacylglycerol lipase"
FT /evidence="ECO:0000256|RuleBase:RU362046"
FT /id="PRO_5005131180"
FT DOMAIN 355..465
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 DISULFID 20..26
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3"
FT DISULFID 107..118
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3"
FT DISULFID 254..278
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3"
FT DISULFID 302..313
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3"
FT DISULFID 316..321
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3"
FT DISULFID 449..465
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3,
FT ECO:0000256|PROSITE-ProRule:PRU00152"
SQ SEQUENCE 465 AA; 51266 MW; D597E2D0F1BB7132 CRC64;
MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGIVERP LHILPWDPKD VNTRFLLYTN
ENPNNFQELV ANSSTISGSN FKTNRKTRFI IHGFIDKGEE DWLVNICKNL FQVESVNCIC
VDWKGGSRTG YTQASQNIRI VGAEVAYFVE VLQSAFDYSP SNVHVIGHSL GAHAAGEAGR
RTNGTIGRIT GLDPAEPCFQ GTPELVRLDP SDAQFVDVIH TDGAPIVPNL GFGMSQVVGH
LDFFPNGGVE MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF
PCASYNVFTA NKCFPCPSEG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS NFARWRYKVS
VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS NEFDSDVEVG DLEKVKFVWY
NNVINPTLPR VGASKIIVET SAGKQFNFCS PETVREDVLL TLTAC
//
