ID   LIPF_CANLF              Reviewed;         398 AA.
AC   P80035; O02857;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   27-MAR-2024, entry version 142.
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   GlyCosmos; P80035; 4 sites, No reported glycans.
DR   PaxDb; 9612-ENSCAFP00000023039; -.
DR   GeneID; 403867; -.
DR   KEGG; cfa:403867; -.
DR   CTD; 8513; -.
DR   eggNOG; KOG2624; Eukaryota.
DR   InParanoid; P80035; -.
DR   OrthoDB; 5474043at2759; -.
DR   EvolutionaryTrace; P80035; -.
DR   PRO; PR:P80035; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; 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; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR025483; Lipase_euk.
DR   PANTHER; PTHR11005:SF15; GASTRIC TRIACYLGLYCEROL LIPASE; 1.
DR   PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//