ID F7GFC8_CALJA Unreviewed; 475 AA.
AC F7GFC8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
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=PNLIPRP3 {ECO:0000313|Ensembl:ENSCJAP00000036041.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000036041.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000036041.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000036041.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU362046};
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 AlphaFoldDB; F7GFC8; -.
DR ESTHER; calja-f7gfc8; Pancreatic_lipase.
DR Ensembl; ENSCJAT00000038059.4; ENSCJAP00000036041.3; ENSCJAG00000019410.4.
DR eggNOG; ENOG502SHK7; Eukaryota.
DR GeneTree; ENSGT00940000163197; -.
DR HOGENOM; CLU_027171_0_2_1; -.
DR OMA; HARSHQF; -.
DR TreeFam; TF324997; -.
DR Proteomes; UP000008225; Chromosome 12.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00707; Pancreat_lipase_like; 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; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; LIPASE; 1.
DR PANTHER; PTHR11610:SF100; PANCREATIC LIPASE-RELATED PROTEIN 3; 1.
DR Pfam; PF00151; Lipase; 2.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 2.
DR PRINTS; PR00823; PANCLIPASE.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2};
KW Disulfide bond {ECO:0000256|RuleBase:RU362046};
KW 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:UP000008225};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU362046};
KW Signal {ECO:0000256|RuleBase:RU362046}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU362046"
FT CHAIN 18..475
FT /note="Triacylglycerol lipase"
FT /evidence="ECO:0000256|RuleBase:RU362046"
FT /id="PRO_5035337219"
FT DOMAIN 18..224
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
FT DOMAIN 255..380
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 191
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 307
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT BINDING 205
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 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ SEQUENCE 475 AA; 52875 MW; A180327892857E52 CRC64;
MLGIWIVAFL FSGTSRGKEV CYERLGCFKD GLPWISTFST ELGGLPWSPE KINIRFLLYT
IRSPNAYQEI SAVNSLSIQA SYFGTDKITR INIAGWKTDG KWQRDMCNVL LQVEDINCIN
LDWINGSLEY IHAVNNLRVV GAEVAYFIDV LMKKFGYSPS KVHLIGHSLG AHLAGEAGSR
IPGLGRITGL DPAGPLFHNT PKEVRLDPSD AIFVDVIHTN AARIFFELGK FLTESETSLK
HRGDFLEAFT LFLFISGVGT IDTCGHLDFY PNGGKHMPGC EDLLTPLLTL NFNAYKKEVA
SFFDCNHARS HHFYAESILN PDAFIAYPCR SYTSFKAGNC FFCPKEGCPT MGHFADRFHL
KNMKTNGSYY FLNTGSHSPF ARWRHKLSVK LSGSKVTQGT IFLHVSGTIG KTGEFAVASG
ELKPGMTYAK LIDADVDVGN ITSIQFTWKK HLFEHSQNKL GAEMVTDISG KYGYK
//
