ID   LIPG_CANFA              Reviewed;         398 AA.
AC   P80035; O02857;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   04-NOV-2008, entry version 69.
DE   RecName: Full=Gastric triacylglycerol lipase;
DE            Short=Gastric lipase;
DE            Short=GL;
DE            EC=3.1.1.3;
DE   Flags: Precursor;
GN   Name=LIPF;
OS   Canis familiaris (Dog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Stomach;
RX   MEDLINE=99450174; PubMed=10520456;
RA   Vaganay S., Joliff G., Bertaux O., Toselli E., Devignes M.D.,
RA   Benicourt C.;
RT   "The complete cDNA sequence encoding dog gastric lipase.";
RL   DNA Seq. 8:257-262(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-59.
RX   MEDLINE=92037652; PubMed=1935982;
RA   Carriere F., Moreau H., Raphel V., Laugier R., Benicourt C.,
RA   Junien J.-L., Verger R.;
RT   "Purification and biochemical characterization of dog gastric
RT   lipase.";
RL   Eur. J. Biochem. 202:75-83(1991).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-396.
RX   MEDLINE=21648681; PubMed=11689574; DOI=10.1074/jbc.M109484200;
RA   Roussel A., Miled N., Berti-Dupuis L., Riviere M., Spinelli S.,
RA   Berna P., Gruber V., Verger R., Cambillau C.;
RT   "Crystal structure of the open form of dog gastric lipase in complex
RT   with a phosphonate inhibitor.";
RL   J. Biol. Chem. 277:2266-2274(2002).
CC   -!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
CC       carboxylate.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Y13899; CAA74198.1; -; mRNA.
DR   PIR; S19539; S19539.
DR   RefSeq; NP_001003209.1; -.
DR   UniGene; Cfa.3733; -.
DR   PDB; 1K8Q; X-ray; 2.70 A; A/B=21-396.
DR   PDBsum; 1K8Q; -.
DR   Ensembl; ENSCAFG00000015682; Canis familiaris.
DR   GeneID; 403867; -.
DR   KEGG; cfa:403867; -.
DR   HOVERGEN; P80035; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004806; F:triacylglycerol lipase activity; IEA:EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006693; AB_hydro_lipase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR008262; Lipase_AS.
DR   Pfam; PF04083; Abhydro_lipase; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Lipid degradation; Secreted; Signal.
FT   SIGNAL        1     19
FT   CHAIN        20    398       Gastric triacylglycerol lipase.
FT                                /FTId=PRO_0000017765.
FT   ACT_SITE    172    172       Charge relay system.
FT   ACT_SITE    343    343       Charge relay system.
FT   ACT_SITE    372    372       Charge relay system.
FT   CARBOHYD     34     34       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     99     99       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    271    271       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    327    327       N-linked (GlcNAc...) (Potential).
FT   DISULFID    246    255
FT   CONFLICT     39     39       I -> T (in Ref. 2; AA sequence).
FT   STRAND       23     25
FT   HELIX        29     32
FT   HELIX        35     41
FT   STRAND       47     52
FT   STRAND       56     64
FT   TURN         72     76
FT   STRAND       79     83
FT   HELIX        90     93
FT   STRAND       94     96
FT   TURN         98    100
FT   HELIX       102    108
FT   STRAND      112    115
FT   STRAND      126    130
FT   TURN        135    138
FT   HELIX       142    147
FT   HELIX       149    161
FT   STRAND      166    171
FT   HELIX       173    184
FT   HELIX       186    189
FT   STRAND      192    199
FT   HELIX       210    215
FT   HELIX       219    225
FT   STRAND      228    232
FT   HELIX       236    244
FT   TURN        245    247
FT   TURN        249    251
FT   HELIX       252    263
FT   HELIX       267    269
FT   HELIX       272    274
FT   HELIX       275    279
FT   HELIX       288    300
FT   HELIX       311    318
FT   STRAND      319    322
FT   HELIX       328    330
FT   STRAND      335    340
FT   STRAND      344    346
FT   HELIX       348    355
FT   STRAND      361    367
FT   HELIX       374    377
FT   HELIX       381    384
FT   HELIX       386    394
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
//