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LIPP_PIG
ID   LIPP_PIG                Reviewed;         450 AA.
AC   P00591;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Pancreatic triacylglycerol lipase {ECO:0000305};
DE            Short=PL;
DE            Short=PTL;
DE            Short=Pancreatic lipase;
DE            EC=3.1.1.3 {ECO:0000250|UniProtKB:P16233};
GN   Name=PNLIP;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE OF 308-449.
RX   PubMed=7326260; DOI=10.1016/0005-2795(81)90126-4;
RA   de Caro J.D., Boudouard M., Bonicel J.J., Guidoni A.A., Desnuelle P.,
RA   Rovery M.;
RT   "Porcine pancreatic lipase. Completion of the primary structure.";
RL   Biochim. Biophys. Acta 671:129-138(1981).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-234, AND GLYCOSYLATION AT ASN-167.
RX   PubMed=380992; DOI=10.1111/j.1432-1033.1979.tb13126.x;
RA   Bianchetta J.D., Bidaud J., Guidoni A.A., Bonicel J.J., Rovery M.;
RT   "Porcine pancreatic lipase. Sequence of the first 234 amino acids of the
RT   peptide chain.";
RL   Eur. J. Biochem. 97:395-405(1979).
RN   [3]
RP   PROTEIN SEQUENCE OF 235-307.
RX   PubMed=518929; DOI=10.1016/s0300-9084(79)80278-3;
RA   Guidoni A.A., Bonicel J.J., Bianchetta J.D., Rovery M.;
RT   "Porcine pancreatic lipase. Sequence between the 235th and 307th amino
RT   acids.";
RL   Biochimie 61:841-845(1979).
RN   [4]
RP   DISULFIDE BONDS.
RX   PubMed=7151781;
RA   Benkouka F., Guidoni A.A., de Caro J.D., Bonicel J.J., Desnuelle P.A.,
RA   Rovery M.;
RT   "Porcine pancreatic lipase. The disulfide bridges and the sulfhydryl
RT   groups.";
RL   Eur. J. Biochem. 128:331-341(1982).
RN   [5]
RP   SUBSTRATE-BINDING SITE.
RX   PubMed=6791692; DOI=10.1016/0005-2744(81)90120-0;
RA   Guidoni A.A., Benkouka F., de Caro J.D., Rovery M.;
RT   "Characterization of the serine reacting with diethyl p-nitrophenyl
RT   phosphate in porcine pancreatic lipase.";
RL   Biochim. Biophys. Acta 660:148-150(1981).
RN   [6]
RP   STRUCTURE OF CARBOHYDRATE.
RX   PubMed=3691527; DOI=10.1111/j.1432-1033.1987.tb13709.x;
RA   Fournet B., Leroy Y., Montreuil J., Decaro J., Rovery M., van Kuik J.A.,
RA   Vliegenthart J.F.G.;
RT   "Primary structure of the glycans of porcine pancreatic lipase.";
RL   Eur. J. Biochem. 170:369-371(1987).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SEQUENCE REVISION TO 30-32.
RX   PubMed=8663362; DOI=10.1074/jbc.271.30.18007;
RA   Hermoso J., Pignol D., Kerfelec B., Crenon I., Chapus C.,
RA   Fontecilla-Camps J.-C.;
RT   "Lipase activation by nonionic detergents. The crystal structure of the
RT   porcine lipase-colipase-tetraethylene glycol monooctyl ether complex.";
RL   J. Biol. Chem. 271:18007-18016(1996).
CC   -!- FUNCTION: Plays an important role in fat metabolism. It preferentially
CC       splits the esters of long-chain fatty acids at positions 1 and 3,
CC       producing mainly 2-monoacylglycerol and free fatty acids, and shows
CC       considerably higher activity against insoluble emulsified substrates
CC       than against soluble ones. {ECO:0000250|UniProtKB:P16233}.
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:0000250|UniProtKB:P16233};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC         Evidence={ECO:0000250|UniProtKB:P16233};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC         dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC         ChEBI:CHEBI:76478; Evidence={ECO:0000250|UniProtKB:P16233};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC         Evidence={ECO:0000250|UniProtKB:P16233};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC         octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC         Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC         Evidence={ECO:0000250|UniProtKB:P16233};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC         Evidence={ECO:0000250|UniProtKB:P16233};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol +
CC         H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC         ChEBI:CHEBI:17616; Evidence={ECO:0000250|UniProtKB:P16233};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC         Evidence={ECO:0000250|UniProtKB:P16233};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC         (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38455,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:52323, ChEBI:CHEBI:75937;
CC         Evidence={ECO:0000250|UniProtKB:P16233};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38456;
CC         Evidence={ECO:0000250|UniProtKB:P16233};
CC   -!- ACTIVITY REGULATION: Inhibited by bile salts, is reactivated by
CC       (pro)colipase/CLPS. {ECO:0000250|UniProtKB:P16233}.
CC   -!- SUBUNIT: Forms a 1:1 stoichiometric complex with (pro)colipase/CLPS.
CC       {ECO:0000250|UniProtKB:P16233}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16233}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="https://www.worthington-biochem.com/PL/";
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DR   PIR; A90638; LIPG.
DR   PDB; 1ETH; X-ray; 2.80 A; A/C=1-450.
DR   PDBsum; 1ETH; -.
DR   AlphaFoldDB; P00591; -.
DR   SMR; P00591; -.
DR   STRING; 9823.ENSSSCP00000011355; -.
DR   BindingDB; P00591; -.
DR   ChEMBL; CHEMBL1687677; -.
DR   DrugCentral; P00591; -.
DR   Allergome; 971; Sus s Lipase.
DR   ESTHER; pig-1plip; Pancreatic_lipase.
DR   iPTMnet; P00591; -.
DR   PaxDb; P00591; -.
DR   PRIDE; P00591; -.
DR   eggNOG; ENOG502QUK7; Eukaryota.
DR   InParanoid; P00591; -.
DR   BRENDA; 3.1.1.3; 6170.
DR   EvolutionaryTrace; P00591; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR   GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR016272; Lipase_LIPH.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR002331; Lipase_panc.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610; PTHR11610; 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   SUPFAM; SSF49723; SSF49723; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Metal-binding; Reference proteome; Secreted.
FT   CHAIN           1..450
FT                   /note="Pancreatic triacylglycerol lipase"
FT                   /id="PRO_0000090356"
FT   DOMAIN          339..450
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   ACT_SITE        153
FT                   /note="Nucleophile"
FT   ACT_SITE        177
FT                   /note="Charge relay system"
FT   ACT_SITE        264
FT                   /note="Charge relay system"
FT   BINDING         188
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         191
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         193
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         196
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:380992"
FT   DISULFID        4..10
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:7151781"
FT   DISULFID        91..104
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:7151781"
FT   DISULFID        91..102
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:7151781"
FT   DISULFID        238..262
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:7151781"
FT   DISULFID        286..297
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:7151781"
FT   DISULFID        300..305
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:7151781"
FT   DISULFID        434..450
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:7151781"
FT   TURN            6..8
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          17..20
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          46..53
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           57..61
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           85..97
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          101..106
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           115..138
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          147..152
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           154..165
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   TURN            166..168
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          170..177
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   TURN            181..183
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   TURN            188..190
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           194..196
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          200..203
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           210..213
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          223..227
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           229..231
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           242..246
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           254..274
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   TURN            278..281
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           290..293
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          307..309
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   HELIX           312..314
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          316..322
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          324..327
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          332..334
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          339..349
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          352..364
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          370..377
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          382..391
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          395..405
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          416..425
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          430..434
FT                   /evidence="ECO:0007829|PDB:1ETH"
FT   STRAND          445..448
FT                   /evidence="ECO:0007829|PDB:1ETH"
SQ   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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