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Pancreatic triacylglycerol lipase (PL) (PTL) (Pancreatic lipase) (EC 3.1.1.3) (Fragment)

 LIPP_HORSE              Reviewed;         461 AA.
P29183;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 2.
25-OCT-2017, entry version 125.
RecName: Full=Pancreatic triacylglycerol lipase;
Short=PL;
Short=PTL;
Short=Pancreatic lipase;
EC=3.1.1.3;
Flags: Precursor; Fragment;
Name=PNLIP;
Equus caballus (Horse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9796;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1587279; DOI=10.1111/j.1432-1033.1992.tb16926.x;
Kerfelec B., Foglizzo E., Bonicel J., Bougis P.E., Chapus C.;
"Sequence of horse pancreatic lipase as determined by protein and cDNA
sequencing. Implications for p-nitrophenyl acetate hydrolysis by
pancreatic lipases.";
Eur. J. Biochem. 206:279-287(1992).
[2]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=8182745; DOI=10.1006/jmbi.1994.1331;
Bourne Y., Martinez C., Kerfelec B., Lombardo D., Chapus C.,
Cambillau C.;
"Horse pancreatic lipase. The crystal structure refined at 2.3-A
resolution.";
J. Mol. Biol. 238:709-732(1994).
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate.
-!- SUBCELLULAR LOCATION: Secreted.
-!- INDUCTION: By colipase/CLPS in the presence of bile salts.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000320}.
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EMBL; X66218; CAA46961.1; -; mRNA.
PIR; S21223; S21223.
RefSeq; NP_001157421.1; NM_001163949.1.
UniGene; Eca.12462; -.
PDB; 1HPL; X-ray; 2.30 A; A/B=13-461.
PDBsum; 1HPL; -.
ProteinModelPortal; P29183; -.
SMR; P29183; -.
STRING; 9796.ENSECAP00000007877; -.
ESTHER; horse-1plip; Pancreatic_lipase.
PaxDb; P29183; -.
PRIDE; P29183; -.
GeneID; 100034202; -.
KEGG; ecb:100034202; -.
CTD; 5406; -.
eggNOG; ENOG410IHRX; Eukaryota.
eggNOG; ENOG410Y92X; LUCA.
HOGENOM; HOG000038552; -.
HOVERGEN; HBG003243; -.
InParanoid; P29183; -.
KO; K14073; -.
EvolutionaryTrace; P29183; -.
Proteomes; UP000002281; Unplaced.
GO; GO:0005576; C:extracellular region; RCA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; RCA:UniProtKB-KW.
GO; GO:0004806; F:triglyceride lipase activity; HMP:UniProtKB.
GO; GO:0016042; P:lipid catabolic process; RCA:UniProtKB-KW.
CDD; cd00707; Pancreat_lipase_like; 1.
Gene3D; 2.60.60.20; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR013818; Lipase/vitellogenin.
InterPro; IPR016272; Lipase_LIPH.
InterPro; IPR033906; Lipase_N.
InterPro; IPR002331; Lipase_panc.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
InterPro; IPR000734; TAG_lipase.
PANTHER; PTHR11610; PTHR11610; 1.
Pfam; PF00151; Lipase; 1.
Pfam; PF01477; PLAT; 1.
PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
PRINTS; PR00823; PANCLIPASE.
PRINTS; PR00821; TAGLIPASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF49723; SSF49723; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00120; LIPASE_SER; 1.
PROSITE; PS50095; PLAT; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Direct protein sequencing;
Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
Metal-binding; Reference proteome; Secreted; Signal.
SIGNAL <1 12
CHAIN 13 461 Pancreatic triacylglycerol lipase.
/FTId=PRO_0000017784.
DOMAIN 351 461 PLAT. {ECO:0000270|PROSITE-
ProRule:PRU00152}.
ACT_SITE 165 165 Nucleophile.
ACT_SITE 189 189 Charge relay system.
ACT_SITE 276 276 Charge relay system.
METAL 200 200 Calcium; via carbonyl oxygen.
METAL 203 203 Calcium; via carbonyl oxygen.
METAL 205 205 Calcium.
METAL 208 208 Calcium.
DISULFID 16 22
DISULFID 103 114
DISULFID 250 274
DISULFID 298 309
DISULFID 312 317
DISULFID 445 461
MUTAGEN 165 165 S->X: 80% loss of P-nitrophenyl acetate
hydrolysis activity.
NON_TER 1 1
STRAND 14 17 {ECO:0000307|PDB:1HPL}.
TURN 18 20 {ECO:0000307|PDB:1HPL}.
STRAND 21 24 {ECO:0000307|PDB:1HPL}.
STRAND 29 32 {ECO:0000307|PDB:1HPL}.
HELIX 44 47 {ECO:0000307|PDB:1HPL}.
STRAND 50 55 {ECO:0000307|PDB:1HPL}.
STRAND 58 65 {ECO:0000307|PDB:1HPL}.
HELIX 69 74 {ECO:0000307|PDB:1HPL}.
STRAND 81 87 {ECO:0000307|PDB:1HPL}.
HELIX 98 109 {ECO:0000307|PDB:1HPL}.
STRAND 112 118 {ECO:0000307|PDB:1HPL}.
HELIX 120 123 {ECO:0000307|PDB:1HPL}.
HELIX 127 152 {ECO:0000307|PDB:1HPL}.
HELIX 156 158 {ECO:0000307|PDB:1HPL}.
STRAND 159 164 {ECO:0000307|PDB:1HPL}.
HELIX 167 177 {ECO:0000307|PDB:1HPL}.
TURN 178 180 {ECO:0000307|PDB:1HPL}.
STRAND 182 189 {ECO:0000307|PDB:1HPL}.
TURN 193 197 {ECO:0000307|PDB:1HPL}.
TURN 200 202 {ECO:0000307|PDB:1HPL}.
HELIX 206 208 {ECO:0000307|PDB:1HPL}.
STRAND 209 215 {ECO:0000307|PDB:1HPL}.
HELIX 222 225 {ECO:0000307|PDB:1HPL}.
STRAND 235 241 {ECO:0000307|PDB:1HPL}.
HELIX 261 265 {ECO:0000307|PDB:1HPL}.
HELIX 274 288 {ECO:0000307|PDB:1HPL}.
HELIX 301 305 {ECO:0000307|PDB:1HPL}.
STRAND 319 321 {ECO:0000307|PDB:1HPL}.
HELIX 324 326 {ECO:0000307|PDB:1HPL}.
TURN 328 331 {ECO:0000307|PDB:1HPL}.
STRAND 332 340 {ECO:0000307|PDB:1HPL}.
STRAND 344 347 {ECO:0000307|PDB:1HPL}.
STRAND 351 361 {ECO:0000307|PDB:1HPL}.
STRAND 364 374 {ECO:0000307|PDB:1HPL}.
STRAND 382 389 {ECO:0000307|PDB:1HPL}.
STRAND 394 403 {ECO:0000307|PDB:1HPL}.
STRAND 407 417 {ECO:0000307|PDB:1HPL}.
STRAND 427 435 {ECO:0000307|PDB:1HPL}.
STRAND 441 445 {ECO:0000307|PDB:1HPL}.
STRAND 456 461 {ECO:0000307|PDB:1HPL}.
SEQUENCE 461 AA; 50921 MW; 382F33F3CE446738 CRC64;
WTLSLLLGAV VGNEVCYERL GCFSDDSPWA GIVERPLKIL PWSPEKVNTR FLLYTNENPD
NFQEIVADPS TIQSSNFNTG RKTRFIIHGF IDKGEESWLS TMCQNMFKVE SVNCICVDWK
SGSRTAYSQA SQNVRIVGAE VAYLVGVLQS SFDYSPSNVH IIGHSLGSHA AGEAGRRTNG
AVGRITGLDP AEPCFQGTPE LVRLDPSDAQ FVDVIHTDIA PFIPNLGFGM SQTAGHLDFF
PNGGKEMPGC QKNVLSQIVD IDGIWQGTRD FAACNHLRSY KYYTDSILNP DGFAGFSCAS
YSDFTANKCF PCSSEGCPQM GHYADRFPGR TKGVGQLFYL NTGDASNFAR WRYRVDVTLS
GKKVTGHVLV SLFGNKGNSR QYEIFQGTLK PDNTYSNEFD SDVEVGDLEK VKFIWYNNVI
NLTLPKVGAS KITVERNDGS VFNFCSEETV REDVLLTLTA C


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