LIPR2_CAVPO
ID LIPR2_CAVPO Reviewed; 434 AA.
AC P81139;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Pancreatic lipase-related protein 2 {ECO:0000250|UniProtKB:P54317};
DE Short=PL-RP2 {ECO:0000250|UniProtKB:P54317};
DE AltName: Full=Cytotoxic T lymphocyte lipase {ECO:0000250|UniProtKB:P17892};
DE AltName: Full=GPL {ECO:0000303|PubMed:8490016};
DE AltName: Full=Galactolipase;
DE EC=3.1.1.26 {ECO:0000269|PubMed:20083229, ECO:0000269|PubMed:8939760};
DE AltName: Full=Triacylglycerol lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:8490016, ECO:0000269|PubMed:8939760};
GN Name=PNLIPRP2 {ECO:0000250|UniProtKB:P54317};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-23 AND 415-432, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas {ECO:0000269|PubMed:8490016};
RX PubMed=8490016; DOI=10.1021/bi00069a003;
RA Hjorth A., Carriere F., Cudrey C., Woldike H., Boel E., Lawson D.M.,
RA Ferrato F., Cambillau C., Dodson G.G., Thim L., Verger R.;
RT "A structural domain (the lid) found in pancreatic lipases is absent in the
RT guinea pig (phospho)lipase.";
RL Biochemistry 32:4702-4707(1993).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17401110; DOI=10.1194/jlr.m600486-jlr200;
RA Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R.,
RA Carriere F., De Caro A.;
RT "Further biochemical characterization of human pancreatic lipase-related
RT protein 2 expressed in yeast cells.";
RL J. Lipid Res. 48:1539-1549(2007).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20083229; DOI=10.1016/j.bbalip.2010.01.003;
RA Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P.,
RA De Caro A., Carriere F.;
RT "Lipolysis of natural long chain and synthetic medium chain galactolipids
RT by pancreatic lipase-related protein 2.";
RL Biochim. Biophys. Acta 1801:508-516(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 1-326 IN COMPLEX WITH CALCIUM,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8939760; DOI=10.1016/s0969-2126(96)00143-8;
RA Withers-Martinez C., Carriere F., Verger R., Bourgeois D., Cambillau C.;
RT "A pancreatic lipase with a phospholipase A1 activity: crystal structure of
RT a chimeric pancreatic lipase-related protein 2 from guinea pig.";
RL Structure 4:1363-1374(1996).
CC -!- FUNCTION: Lipase that primarily hydrolyzes triglycerides and
CC galactosylglycerides (PubMed:8490016, PubMed:17401110, PubMed:20083229,
CC PubMed:8939760). In neonates, may play a major role in pancreatic
CC digestion of dietary fats such as milk fat globules enriched in long-
CC chain triglycerides (By similarity). Hydrolyzes short-, medium- and
CC long-chain fatty acyls in triglycerides without apparent positional
CC specificity (PubMed:8490016, PubMed:8939760). Can completely deacylate
CC triacylglycerols (By similarity). When the liver matures and bile salt
CC synthesis increases, likely functions mainly as a galactolipase and
CC monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG)
CC and digalactosyldiacylglycerols (DGDG) present in a plant-based diet,
CC releasing long-chain polyunsaturated fatty acids (PubMed:20083229,
CC PubMed:8939760). Hydrolyzes medium- and long-chain fatty acyls in
CC galactolipids. May act together with LIPF to hydrolyze partially
CC digested triglycerides (By similarity). Hydrolyzes long-chain
CC monoglycerides with high efficiency. In cytotoxic T cells, contributes
CC to perforin-dependent cell lysis, but is unlikely to mediate direct
CC cytotoxicity (By similarity). Also has low phospholipase activity (By
CC similarity). In neurons, required for the localization of the
CC phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through
CC acyl chain remodeling of membrane phospholipids (By similarity). The
CC resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein
CC STX4 by selectively interacting with the STX4 transmembrane domain and
CC this promotes surface expression of the dopamine transporter SLC6A3/DAT
CC at neurite tips by facilitating fusion of SLC6A3-containing transport
CC vesicles with the plasma membrane (By similarity).
CC {ECO:0000250|UniProtKB:P17892, ECO:0000250|UniProtKB:P54317,
CC ECO:0000250|UniProtKB:P54318, ECO:0000269|PubMed:17401110,
CC ECO:0000269|PubMed:20083229, ECO:0000269|PubMed:8490016,
CC ECO:0000269|PubMed:8939760}.
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:0000269|PubMed:8490016, ECO:0000269|PubMed:8939760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:8490016, ECO:0000305|PubMed:8939760};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-
CC beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+);
CC Xref=Rhea:RHEA:13189, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15754, ChEBI:CHEBI:17615, ChEBI:CHEBI:28868; EC=3.1.1.26;
CC Evidence={ECO:0000269|PubMed:20083229, ECO:0000269|PubMed:8939760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190;
CC Evidence={ECO:0000305|PubMed:20083229, ECO:0000305|PubMed:8939760};
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:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-(9Z)-octadecenoylglycerol + H2O = (9Z)-octadecenoate + (9Z-
CC octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:47868,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75937, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47869;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:39955, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75937; Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39956;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tripropanoylglycerol + H2O = dipropanoylglycerol + H(+)
CC + propanoate; Xref=Rhea:RHEA:48024, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:88153,
CC ChEBI:CHEBI:88155; Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48025;
CC Evidence={ECO:0000250|UniProtKB:P54317};
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:0000269|PubMed:8939760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000305|PubMed:8939760};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978,
CC ChEBI:CHEBI:88066; Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoylglycerol + H2O = decanoate + decanoylglycerol +
CC H(+); Xref=Rhea:RHEA:48596, ChEBI:CHEBI:11152, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:90605;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48597;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + long chain 1,2-diacyl-3-O-beta-D-galactosyl-sn-glycerol
CC = a fatty acid + H(+) + long chain acyl-3-O-beta-D-galactosyl-sn-
CC glycerol; Xref=Rhea:RHEA:48700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:90477, ChEBI:CHEBI:90770;
CC Evidence={ECO:0000269|PubMed:20083229, ECO:0000269|PubMed:8939760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48701;
CC Evidence={ECO:0000305|PubMed:20083229, ECO:0000305|PubMed:8939760};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-3-O-beta-D-galactosyl-sn-glycerol + H2O = H(+)
CC + octanoate + octanoyl-3-(beta-D-galactosyl)-sn-glycerol;
CC Xref=Rhea:RHEA:48696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:90453, ChEBI:CHEBI:90769;
CC Evidence={ECO:0000269|PubMed:20083229};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48697;
CC Evidence={ECO:0000305|PubMed:20083229};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didodecanoyl-3-beta-D-galactosyl-sn-glycerol + H2O =
CC dodecanoate + dodecanoyl-3-beta-D-galactosyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:48540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:90340, ChEBI:CHEBI:90515;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48541;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-beta-D-galactosyl-2,3-didodecanoyl-sn-glycerol + H2O = 1-
CC beta-D-galactosyl-dodecanoyl-sn-glycerol + dodecanoate + H(+);
CC Xref=Rhea:RHEA:48536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:90342, ChEBI:CHEBI:90514;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48537;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-
CC sn-glycerol + H2O = a fatty acid + acyl-3-O-[alpha-D-galactosyl-
CC (1->6)-beta-D-galactosyl]-sn-glycerol + H(+); Xref=Rhea:RHEA:48372,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28396,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:90310;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48373;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + long chain 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-
CC beta-D-galactosyl]-sn-glycerol = a fatty acid + H(+) + long chain
CC acyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol;
CC Xref=Rhea:RHEA:48708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:90463, ChEBI:CHEBI:90774;
CC Evidence={ECO:0000269|PubMed:20083229};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48709;
CC Evidence={ECO:0000305|PubMed:20083229};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-
CC galactosyl]-sn-glycerol + H2O = H(+) + octanoate + octanoyl-3-O-
CC [alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol;
CC Xref=Rhea:RHEA:48692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:90457, ChEBI:CHEBI:90768;
CC Evidence={ECO:0000269|PubMed:20083229};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48693;
CC Evidence={ECO:0000305|PubMed:20083229};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didodecanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-
CC galactosyl]-sn-glycerol + H2O = dodecanoate + dodecanoyl-3-O-[alpha-
CC D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:48516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:90337, ChEBI:CHEBI:90359;
CC Evidence={ECO:0000269|PubMed:17401110};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48517;
CC Evidence={ECO:0000305|PubMed:17401110};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a fatty acid
CC + a monoacyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:44664, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:84465;
CC Evidence={ECO:0000269|PubMed:8939760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44665;
CC Evidence={ECO:0000305|PubMed:8939760};
CC -!- ACTIVITY REGULATION: CLPS stimulates triacylglycerol lipase activity.
CC Not inhibited by bile salts. {ECO:0000269|PubMed:8490016}.
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC {ECO:0000250|UniProtKB:P54317}.
CC -!- PATHWAY: Glycolipid metabolism. {ECO:0000250|UniProtKB:P54317}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P54317}. Zymogen
CC granule membrane {ECO:0000250|UniProtKB:P54318}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P54318}. Cell projection, neuron
CC projection {ECO:0000250|UniProtKB:P54318}. Note=Localizes to neurite
CC tips in neuronal cells. {ECO:0000250|UniProtKB:P54318}.
CC -!- TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:8490016}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000255}.
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DR PIR; A49488; A49488.
DR PDB; 1GPL; X-ray; 2.01 A; A=1-434.
DR PDBsum; 1GPL; -.
DR AlphaFoldDB; P81139; -.
DR SMR; P81139; -.
DR STRING; 10141.ENSCPOP00000020465; -.
DR ChEMBL; CHEMBL2169729; -.
DR SwissLipids; SLP:000001439; -.
DR ESTHER; cavpo-2plrp; Pancreatic_lipase.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR InParanoid; P81139; -.
DR BRENDA; 3.1.1.26; 1225.
DR SABIO-RK; P81139; -.
DR UniPathway; UPA00256; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0102549; F:1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0047714; F:galactolipase activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0019376; P:galactolipid catabolic process; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IDA:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; IEA:UniProtKB-UniPathway.
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; Cell projection; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
KW Reference proteome; Secreted.
FT CHAIN 1..434
FT /note="Pancreatic lipase-related protein 2"
FT /id="PRO_0000090357"
FT DOMAIN 322..434
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 76..88
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT REGION 240..244
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54318,
FT ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 247
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54318,
FT ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8939760,
FT ECO:0007744|PDB:1GPL"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8939760,
FT ECO:0007744|PDB:1GPL"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8939760,
FT ECO:0007744|PDB:1GPL"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8939760,
FT ECO:0007744|PDB:1GPL"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT DISULFID 4..10
FT /evidence="ECO:0000250|UniProtKB:P54318,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 92..103
FT /evidence="ECO:0000250|UniProtKB:P54318,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 239..245
FT /evidence="ECO:0000250|UniProtKB:P54318,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 269..280
FT /evidence="ECO:0000250|UniProtKB:P54318,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 283..288
FT /evidence="ECO:0000250|UniProtKB:P54318,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 418..434
FT /evidence="ECO:0000250|UniProtKB:P54318,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 116..141
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:1GPL"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:1GPL"
FT TURN 182..186
FT /evidence="ECO:0007829|PDB:1GPL"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 245..259
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1GPL"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1GPL"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 303..311
FT /evidence="ECO:0007829|PDB:1GPL"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:1GPL"
SQ SEQUENCE 434 AA; 47678 MW; E15EED77F3DD59D2 CRC64;
AEVCYSHLGC FSDEKPWAGT SQRPIKSLPS DPKKINTRFL LYTNENQNSY QLITATDIAT
IKASNFNLNR KTRFIIHGFT DSGENSWLSD MCKNMFQVEK VNCICVDWKG GSKAQYSQAS
QNIRVVGAEV AYLVQVLSTS LNYAPENVHI IGHSLGAHTA GEAGKRLNGL VGRITGLDPA
EPYFQDTPEE VRLDPSDAKF VDVIHTDISP ILPSLGFGMS QKVGHMDFFP NGGKDMPGCK
TGISCNHHRS IEYYHSSILN PEGFLGYPCA SYDEFQESGC FPCPAKGCPK MGHFADQYPG
KTNAVEQTFF LNTGASDNFT RWRYKVTVTL SGEKDPSGNI NVALLGKNGN SAQYQVFKGT
LKPDASYTNS IDVELNVGTI QKVTFLWKRS GISVSKPKMG ASRITVQSGK DGTKYNFCSS
DIVQENVEQT LSPC
