ID   LIPP_SPETR              Reviewed;         465 AA.
AC   O88354; Q9QWF3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Pancreatic triacylglycerol lipase;
DE            Short=Pancreatic lipase;
DE            Short=PL;
DE            EC=3.1.1.3;
DE   AltName: Full=Heart pancreatic lipase;
DE   AltName: Full=PL-h;
DE   Flags: Precursor;
GN   Name=PNLIP; Synonyms=PTL;
OS   Spermophilus tridecemlineatus (Thirteen-lined ground squirrel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Sciuridae; Xerinae; Marmotini; Spermophilus.
OX   NCBI_TaxID=43179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND FUNCTION IN HIBERNATION.
RC   TISSUE=Heart;
RX   MEDLINE=98318668; PubMed=9653197; DOI=10.1073/pnas.95.14.8392;
RA   Andrews M.T., Squire T.L., Bowen C.M., Rollins M.B.;
RT   "Low-temperature carbon utilization is regulated by novel gene
RT   activity in the heart of a hibernating mammal.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8392-8397(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=14583598; DOI=10.1152/physiolgenomics.00167.2002;
RA   Squire T.L., Andrews M.T.;
RT   "Pancreatic triacylglycerol lipase in a hibernating mammal. I. Novel
RT   genomic organization.";
RL   Physiol. Genomics 16:119-130(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=White adipose tissue;
RA   Bauer V.W., Andrews M.T.;
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=14583599; DOI=10.1152/physiolgenomics.00168.2002;
RA   Squire T.L., Lowe M.E., Bauer V.W., Andrews M.T.;
RT   "Pancreatic triacylglycerol lipase in a hibernating mammal. II. Cold-
RT   adapted function and differential expression.";
RL   Physiol. Genomics 16:131-140(2003).
CC   -!- FUNCTION: Plays an important role in fat metabolism. It
CC       preferentially splits the esters of long-chain fatty acids at
CC       positions 1 and 3, producing mainly 2-monoacylglycerol and free
CC       fatty acids, and shows considerably higher activity against
CC       insoluble emulsified substrates than against soluble ones (By
CC       similarity). Play a role in hibernation as a key enzyme that shows
CC       high activity at low temperatures. When expressed in the
CC       hibernating heart it liberates fatty acids from triglycerides at
CC       temperatures as low as 0 degrees Celsius.
CC   -!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
CC       carboxylate.
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in many tissues with highest
CC       expression in liver. During hibernation there is a significant
CC       increases in expression in heart, white adipose tissue (WAT), and
CC       testis; but not in pancreas.
CC   -!- INDUCTION: Up-regulated during hibernation.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
CC       family.
CC   -!- SIMILARITY: Contains 1 PLAT domain.
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DR   EMBL; AF027293; AAC40162.2; -; mRNA.
DR   EMBL; AF395870; AAK72259.1; -; mRNA.
DR   EMBL; AF177402; AAD51123.2; -; mRNA.
DR   EMBL; AF177403; AAD51124.1; -; mRNA.
DR   HSSP; P16233; 1LPB.
DR   Ensembl; ENSSTOG00000002279; Spermophilus tridecemlineatus.
DR   HOVERGEN; O88354; -.
DR   OMA; O88354; YEIFKGT.
DR   BRENDA; 3.1.1.3; 277892.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004806; F:triacylglycerol lipase activity; IEA:EC.
DR   GO; GO:0042750; P:hibernation; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000734; Lipase.
DR   InterPro; IPR013818; Lipase_N.
DR   InterPro; IPR002331; Lipase_panc.
DR   InterPro; IPR001024; LipOase_LH2.
DR   InterPro; IPR016272; Lipoprotein_lipase_LIPH.
DR   Gene3D; G3DSA:2.60.60.20; Lipase_LipOase; 1.
DR   PANTHER; PTHR11610; Lipase; 1.
DR   PANTHER; PTHR11610:SF8; Lipase_panc; 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   PROSITE; PS00120; LIPASE_SER; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Hibernation; Hydrolase; Lipid degradation; Secreted;
KW   Signal.
FT   SIGNAL        1     16       By similarity.
FT   CHAIN        17    465       Pancreatic triacylglycerol lipase.
FT                                /FTId=PRO_0000250516.
FT   DOMAIN      355    465       PLAT.
FT   ACT_SITE    169    169       Nucleophile (By similarity).
FT   ACT_SITE    193    193       Charge relay system (By similarity).
FT   ACT_SITE    280    280       Charge relay system (By similarity).
FT   DISULFID     20     26       By similarity.
FT   DISULFID    107    118       By similarity.
FT   DISULFID    254    278       By similarity.
FT   DISULFID    302    313       By similarity.
FT   DISULFID    316    321       By similarity.
FT   DISULFID    449    465       By similarity.
FT   CONFLICT    133    133       Q -> H (in Ref. 3; AAD51123).
SQ   SEQUENCE   465 AA;  51227 MW;  A152FB00CD01169B CRC64;
     MLLVWSLALL LGAVAGKEVC YDRLGCFSDD SPWSGIVERP LKVLPWSPAD VNTRFLLYTN
     ENQDNYQQIT ADSSRIQSSN FKTNRKTRFI IHGFIDKGEE SWLANMCKKM FQVESVNCIC
     VDWKGGSRTG YTQASQNIRI VGAEVAYFVD FLRTQLGYSP SNVHVIGHSL GSHAAGEAGR
     RTNGAIGRIT GLDPAEPCFE GTPELVRLDP SDAQFVDAIH TDGAPIVPNL GFGMSQTVGH
     LDFFPNGGIE MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFAAF
     SCASYSVFSA NKCFPCPSGG CPQMGHYADR YSGKTNGVGQ KFYLNTGDKS NFSRWRYKVS
     VTLSGQKVTG HILVSLFGNA GNSKQYEIYK GSLHPGYTHS NEFDSDVDVG DLQRVKFIWY
     NNVINPSLPR VGASSISVER NDGRVFKFCS AETVREDVLL TLNAC
//