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

 LIPP_PIG                Reviewed;         450 AA.
P00591;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
25-OCT-2017, entry version 124.
RecName: Full=Pancreatic triacylglycerol lipase;
Short=PL;
Short=PTL;
Short=Pancreatic lipase;
EC=3.1.1.3;
Name=PNLIP;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
PROTEIN SEQUENCE OF 308-449.
PubMed=7326260; DOI=10.1016/0005-2795(81)90126-4;
de Caro J.D., Boudouard M., Bonicel J.J., Guidoni A.A., Desnuelle P.,
Rovery M.;
"Porcine pancreatic lipase. Completion of the primary structure.";
Biochim. Biophys. Acta 671:129-138(1981).
[2]
PROTEIN SEQUENCE OF 1-234, AND GLYCOSYLATION AT ASN-167.
PubMed=380992; DOI=10.1111/j.1432-1033.1979.tb13126.x;
Bianchetta J.D., Bidaud J., Guidoni A.A., Bonicel J.J., Rovery M.;
"Porcine pancreatic lipase. Sequence of the first 234 amino acids of
the peptide chain.";
Eur. J. Biochem. 97:395-405(1979).
[3]
PROTEIN SEQUENCE OF 235-307.
PubMed=518929; DOI=10.1016/S0300-9084(79)80278-3;
Guidoni A.A., Bonicel J.J., Bianchetta J.D., Rovery M.;
"Porcine pancreatic lipase. Sequence between the 235th and 307th amino
acids.";
Biochimie 61:841-845(1979).
[4]
DISULFIDE BONDS.
PubMed=7151781;
Benkouka F., Guidoni A.A., de Caro J.D., Bonicel J.J., Desnuelle P.A.,
Rovery M.;
"Porcine pancreatic lipase. The disulfide bridges and the sulfhydryl
groups.";
Eur. J. Biochem. 128:331-341(1982).
[5]
SUBSTRATE-BINDING SITE.
PubMed=6791692; DOI=10.1016/0005-2744(81)90120-0;
Guidoni A.A., Benkouka F., de Caro J.D., Rovery M.;
"Characterization of the serine reacting with diethyl p-nitrophenyl
phosphate in porcine pancreatic lipase.";
Biochim. Biophys. Acta 660:148-150(1981).
[6]
STRUCTURE OF CARBOHYDRATE.
PubMed=3691527; DOI=10.1111/j.1432-1033.1987.tb13709.x;
Fournet B., Leroy Y., Montreuil J., Decaro J., Rovery M.,
van Kuik J.A., Vliegenthart J.F.G.;
"Primary structure of the glycans of porcine pancreatic lipase.";
Eur. J. Biochem. 170:369-371(1987).
[7]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SEQUENCE REVISION TO 30-32.
PubMed=8663362; DOI=10.1074/jbc.271.30.18007;
Hermoso J., Pignol D., Kerfelec B., Crenon I., Chapus C.,
Fontecilla-Camps J.-C.;
"Lipase activation by nonionic detergents. The crystal structure of
the porcine lipase-colipase-tetraethylene glycol monooctyl ether
complex.";
J. Biol. Chem. 271:18007-18016(1996).
-!- 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:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/PL/";
-----------------------------------------------------------------------
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PIR; A90638; LIPG.
UniGene; Ssc.61171; -.
PDB; 1ETH; X-ray; 2.80 A; A/C=1-450.
PDBsum; 1ETH; -.
ProteinModelPortal; P00591; -.
SMR; P00591; -.
STRING; 9823.ENSSSCP00000011355; -.
BindingDB; P00591; -.
ChEMBL; CHEMBL1687677; -.
Allergome; 971; Sus s Lipase.
ESTHER; sussc-1plip; Pancreatic_lipase.
iPTMnet; P00591; -.
PaxDb; P00591; -.
PRIDE; P00591; -.
eggNOG; ENOG410IHRX; Eukaryota.
eggNOG; ENOG410Y92X; LUCA.
HOGENOM; HOG000038552; -.
HOVERGEN; HBG003243; -.
InParanoid; P00591; -.
BRENDA; 3.1.1.3; 6170.
EvolutionaryTrace; P00591; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
GO; GO:0016042; P:lipid catabolic process; IEA: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; Glycoprotein; Hydrolase; Lipid degradation;
Lipid metabolism; Metal-binding; Reference proteome; Secreted.
CHAIN 1 450 Pancreatic triacylglycerol lipase.
/FTId=PRO_0000090356.
DOMAIN 339 450 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
ACT_SITE 153 153 Nucleophile.
ACT_SITE 177 177 Charge relay system.
ACT_SITE 264 264 Charge relay system.
METAL 188 188 Calcium; via carbonyl oxygen.
METAL 191 191 Calcium; via carbonyl oxygen.
METAL 193 193 Calcium.
METAL 196 196 Calcium.
CARBOHYD 167 167 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:380992}.
DISULFID 4 10 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:7151781}.
DISULFID 91 104 Alternate. {ECO:0000255|PROSITE-
ProRule:PRU00152,
ECO:0000269|PubMed:7151781}.
DISULFID 91 102 Alternate. {ECO:0000255|PROSITE-
ProRule:PRU00152,
ECO:0000269|PubMed:7151781}.
DISULFID 238 262 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:7151781}.
DISULFID 286 297 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:7151781}.
DISULFID 300 305 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:7151781}.
DISULFID 434 450 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:7151781}.
TURN 6 8 {ECO:0000244|PDB:1ETH}.
STRAND 17 20 {ECO:0000244|PDB:1ETH}.
STRAND 38 43 {ECO:0000244|PDB:1ETH}.
STRAND 46 53 {ECO:0000244|PDB:1ETH}.
HELIX 57 61 {ECO:0000244|PDB:1ETH}.
STRAND 62 64 {ECO:0000244|PDB:1ETH}.
STRAND 71 75 {ECO:0000244|PDB:1ETH}.
HELIX 85 97 {ECO:0000244|PDB:1ETH}.
STRAND 101 106 {ECO:0000244|PDB:1ETH}.
HELIX 110 112 {ECO:0000244|PDB:1ETH}.
HELIX 115 138 {ECO:0000244|PDB:1ETH}.
HELIX 144 146 {ECO:0000244|PDB:1ETH}.
STRAND 147 152 {ECO:0000244|PDB:1ETH}.
HELIX 154 165 {ECO:0000244|PDB:1ETH}.
TURN 166 168 {ECO:0000244|PDB:1ETH}.
STRAND 170 177 {ECO:0000244|PDB:1ETH}.
TURN 181 183 {ECO:0000244|PDB:1ETH}.
STRAND 184 186 {ECO:0000244|PDB:1ETH}.
TURN 188 190 {ECO:0000244|PDB:1ETH}.
HELIX 194 196 {ECO:0000244|PDB:1ETH}.
STRAND 200 203 {ECO:0000244|PDB:1ETH}.
HELIX 210 213 {ECO:0000244|PDB:1ETH}.
STRAND 223 227 {ECO:0000244|PDB:1ETH}.
HELIX 229 231 {ECO:0000244|PDB:1ETH}.
HELIX 242 246 {ECO:0000244|PDB:1ETH}.
HELIX 254 274 {ECO:0000244|PDB:1ETH}.
TURN 278 281 {ECO:0000244|PDB:1ETH}.
HELIX 290 293 {ECO:0000244|PDB:1ETH}.
STRAND 307 309 {ECO:0000244|PDB:1ETH}.
HELIX 312 314 {ECO:0000244|PDB:1ETH}.
STRAND 316 322 {ECO:0000244|PDB:1ETH}.
STRAND 324 327 {ECO:0000244|PDB:1ETH}.
STRAND 332 334 {ECO:0000244|PDB:1ETH}.
STRAND 339 349 {ECO:0000244|PDB:1ETH}.
STRAND 352 364 {ECO:0000244|PDB:1ETH}.
STRAND 370 377 {ECO:0000244|PDB:1ETH}.
STRAND 382 391 {ECO:0000244|PDB:1ETH}.
STRAND 395 405 {ECO:0000244|PDB:1ETH}.
STRAND 416 425 {ECO:0000244|PDB:1ETH}.
STRAND 430 434 {ECO:0000244|PDB:1ETH}.
STRAND 445 448 {ECO:0000244|PDB:1ETH}.
SEQUENCE 450 AA; 50084 MW; 76E13BBDB4541E0E CRC64;
SEVCFPRLGC FSDDAPWAGI VQRPLKILPW SPKDVDTRFL LYTNQNQNNY QELVADPSTI
TNSNFRMDRK TRFIIHGFID KGEEDWLSNI CKNLFKVESV NCICVDWKGG SRTGYTQASQ
NIRIVGAEVA YFVEVLKSSL GYSPSNVHVI GHSLGSHAAG EAGRRTNGTI ERITGLDPAE
PCFQGTPELV RLDPSDAKFV DVIHTDAAPI IPNLGFGMSQ TVGHLDFFPN GGKQMPGCQK
NILSQIVDID GIWEGTRDFV ACNHLRSYKY YADSILNPDG FAGFPCDSYN VFTANKCFPC
PSEGCPQMGH YADRFPGKTN GVSQVFYLNT GDASNFARWR YKVSVTLSGK KVTGHILVSL
FGNEGNSRQY EIYKGTLQPD NTHSDEFDSD VEVGDLQKVK FIWYNNNVIN PTLPRVGASK
ITVERNDGKV YDFCSQETVR EEVLLTLNPC


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