LIPG_CANLF
ID LIPG_CANLF Reviewed; 398 AA.
AC P80035; O02857;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Gastric triacylglycerol lipase;
DE Short=GL;
DE Short=Gastric lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:11689574, ECO:0000269|PubMed:1568562, ECO:0000269|PubMed:1935982};
DE Flags: Precursor;
GN Name=LIPF;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Stomach;
RX PubMed=10520456; DOI=10.3109/10425179809008461;
RA Vaganay S., Joliff G., Bertaux O., Toselli E., Devignes M.D., Benicourt C.;
RT "The complete cDNA sequence encoding dog gastric lipase.";
RL DNA Seq. 8:257-262(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1568562; DOI=10.1016/0016-5085(92)91711-c;
RA Carriere F., Raphel V., Moreau H., Bernadac A., Devaux M.A., Grimaud R.,
RA Barrowman J.A., Benicourt C., Junien J.L., Laugier R.;
RT "Dog gastric lipase: stimulation of its secretion in vivo and
RT cytolocalization in mucous pit cells.";
RL Gastroenterology 102:1535-1545(1992).
RN [3]
RP PROTEIN SEQUENCE OF 20-59, FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=1935982; DOI=10.1111/j.1432-1033.1991.tb16346.x;
RA Carriere F., Moreau H., Raphel V., Laugier R., Benicourt C., Junien J.-L.,
RA Verger R.;
RT "Purification and biochemical characterization of dog gastric lipase.";
RL Eur. J. Biochem. 202:75-83(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-396, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVE SITES, AND DISULFIDE BOND.
RX PubMed=11689574; DOI=10.1074/jbc.m109484200;
RA Roussel A., Miled N., Berti-Dupuis L., Riviere M., Spinelli S., Berna P.,
RA Gruber V., Verger R., Cambillau C.;
RT "Crystal structure of the open form of dog gastric lipase in complex with a
RT phosphonate inhibitor.";
RL J. Biol. Chem. 277:2266-2274(2002).
CC -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free
CC fatty acids, diacylglycerol, monoacylglycerol, and glycerol
CC (PubMed:1568562, PubMed:1935982, PubMed:11689574). Shows a preferential
CC hydrolysis at the sn-3 position of triacylglycerol (By similarity).
CC {ECO:0000250|UniProtKB:P07098, ECO:0000269|PubMed:11689574,
CC ECO:0000269|PubMed:1568562, ECO:0000269|PubMed:1935982}.
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:11689574, ECO:0000269|PubMed:1568562,
CC ECO:0000269|PubMed:1935982};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:39931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753;
CC Evidence={ECO:0000250|UniProtKB:P07098};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39932;
CC Evidence={ECO:0000250|UniProtKB:P07098};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-trioctanoylglycerol + H2O = 1,2-dioctanoyl-sn-glycerol +
CC H(+) + octanoate; Xref=Rhea:RHEA:40047, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978,
CC ChEBI:CHEBI:76979; Evidence={ECO:0000250|UniProtKB:P07098};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40048;
CC Evidence={ECO:0000250|UniProtKB:P07098};
CC -!- ACTIVITY REGULATION: Inactivated by thiol reagents 5,5'- dithiobis(2-
CC nitrobenzoic acid) and 4,4'-dithiopyridine.
CC {ECO:0000269|PubMed:1935982}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6 for short chain and medium-chain triacylglycerol and
CC 4 for long-chain triacylglycerol (PubMed:1935982). Inactivated when
CC pH is below 1.5 (PubMed:1568562). {ECO:0000269|PubMed:1568562,
CC ECO:0000269|PubMed:1935982};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1568562}.
CC -!- TISSUE SPECIFICITY: Expressed in the mucous pit cells of gastric glands
CC (at protein level) (PubMed:1568562). Expressed in the fundic and
CC pyloric mucosa (PubMed:1935982). {ECO:0000269|PubMed:1568562,
CC ECO:0000269|PubMed:1935982}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; Y13899; CAA74198.1; -; mRNA.
DR PIR; S19539; S19539.
DR RefSeq; NP_001003209.1; NM_001003209.1.
DR PDB; 1K8Q; X-ray; 2.70 A; A/B=21-396.
DR PDBsum; 1K8Q; -.
DR AlphaFoldDB; P80035; -.
DR SMR; P80035; -.
DR STRING; 9615.ENSCAFP00000056433; -.
DR ChEMBL; CHEMBL2169727; -.
DR ESTHER; canfa-1lipg; Acidic_Lipase.
DR MEROPS; S33.A57; -.
DR PaxDb; P80035; -.
DR GeneID; 403867; -.
DR KEGG; cfa:403867; -.
DR CTD; 8513; -.
DR eggNOG; KOG2624; Eukaryota.
DR InParanoid; P80035; -.
DR OrthoDB; 651396at2759; -.
DR EvolutionaryTrace; P80035; -.
DR PRO; PR:P80035; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR039097; Gastric_lipase.
DR InterPro; IPR025483; Lipase_euk.
DR PANTHER; PTHR11005:SF15; PTHR11005:SF15; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1935982"
FT CHAIN 20..398
FT /note="Gastric triacylglycerol lipase"
FT /id="PRO_0000017765"
FT DOMAIN 82..377
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:11689574"
FT ACT_SITE 343
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:11689574"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:11689574"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 246..255
FT /evidence="ECO:0000269|PubMed:11689574"
FT CONFLICT 39
FT /note="I -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:1K8Q"
FT TURN 72..76
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1K8Q"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1K8Q"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:1K8Q"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1K8Q"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 252..263
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 275..279
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 348..355
FT /evidence="ECO:0007829|PDB:1K8Q"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:1K8Q"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:1K8Q"
SQ SEQUENCE 398 AA; 45131 MW; E04D62F7518E386C CRC64;
MWLLLTAASV ISTLGTTHGL FGKLHPTNPE VTMNISQMIT YWGYPAEEYE VVTEDGYILG
IDRIPYGRKN SENIGRRPVA FLQHGLLASA TNWISNLPNN SLAFILADAG YDVWLGNSRG
NTWARRNLYY SPDSVEFWAF SFDEMAKYDL PATIDFILKK TGQDKLHYVG HSQGTTIGFI
AFSTNPKLAK RIKTFYALAP VATVKYTETL LNKLMLVPSF LFKLIFGNKI FYPHHFFDQF
LATEVCSRET VDLLCSNALF IICGFDTMNL NMSRLDVYLS HNPAGTSVQN VLHWSQAVKS
GKFQAFDWGS PVQNMMHYHQ SMPPYYNLTD MHVPIAVWNG GNDLLADPHD VDLLLSKLPN
LIYHRKIPPY NHLDFIWAMD APQAVYNEIV SMMGTDNK
