ID H2NBQ2_PONAB Unreviewed; 465 AA.
AC H2NBQ2; A0A2J8W6U7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 68.
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:ENSPPYP00000003131.2};
GN ORFNames=CR201_G0012793 {ECO:0000313|EMBL:PNJ65505.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000003131.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000003131.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ65505.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ65505.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000003131.2}
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; NDHI03003398; PNJ65505.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000003131; -.
DR ESTHER; ponab-a0a2j8w6u7; Pancreatic_lipase.
DR Ensembl; ENSPPYT00000003237.2; ENSPPYP00000003131.2; ENSPPYG00000002681.2.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR GeneTree; ENSGT00940000160632; -.
DR HOGENOM; CLU_027171_0_2_1; -.
DR OMA; RNIDLTP; -.
DR OrthoDB; 3428256at2759; -.
DR TreeFam; TF324997; -.
DR Proteomes; UP000001595; Chromosome 10.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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:UP000001595};
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_5041474101"
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; 51043 MW; 4BBCBAF2F0527C61 CRC64;
MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGIVERP LHILPWSPKD VNTRFLLYTN
ENPNNFQEVV ADSSSISGSN FKTNRKTRFI IHGFIDKGEE NWLADLCKNL FKVESVNCIC
VDWKGGSRTG YTQASQNIRI VGAEVAYFVE VLQSAFSYSP SNVHVIGHSL GAHAAGEAGR
RTSGTIGRIT GLDPAEPCFQ GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH
LDFFPNGGVE MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF
PCSSYSVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS NFARWRYKVS
VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS NEFDSDVDVG DLQKVKFIWY
NNVINPTLPT VGASKIIVET NVGTQFNFCS PETVREDVLL TLTPC
//
