LIPR2_PIG
ID LIPR2_PIG Reviewed; 471 AA.
AC D7EZN2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Galactolipase;
DE EC=3.1.1.26 {ECO:0000250|UniProtKB:P54317};
DE AltName: Full=Triacylglycerol lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:23770034};
DE Flags: Precursor;
GN Name=PNLIPRP2;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Intestine;
RX PubMed=14681463; DOI=10.1093/nar/gkh037;
RA Uenishi H., Eguchi T., Suzuki K., Sawazaki T., Toki D., Shinkai H.,
RA Okumura N., Hamasima N., Awata T.;
RT "PEDE (Pig EST Data Explorer): construction of a database for ESTs derived
RT from porcine full-length cDNA libraries.";
RL Nucleic Acids Res. 32:D484-D488(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheng L., Xiong Y.;
RT "Cloning, Expression, Regulation and Association Analysis with Production
RT Traits of the Porcine PNLIPRP2 Gene.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND PATHWAY.
RX PubMed=23770034; DOI=10.1016/j.bbalip.2013.06.002;
RA Xiao X., Ross L.E., Sevilla W.A., Wang Y., Lowe M.E.;
RT "Porcine pancreatic lipase related protein 2 has high triglyceride lipase
RT activity in the absence of colipase.";
RL Biochim. Biophys. Acta 1831:1435-1441(2013).
CC -!- FUNCTION: Lipase that primarily hydrolyzes triglycerides and
CC galactosylglycerides (PubMed:23770034). In neonates, may play a major
CC role in pancreatic digestion of dietary fats such as milk fat globules
CC enriched in long-chain triglycerides (PubMed:23770034). Hydrolyzes
CC short-, medium- and long-chain fatty acyls in triglycerides without
CC apparent positional specificity (PubMed:23770034). Can completely
CC deacylate triacylglycerols (By similarity). When the liver matures and
CC bile salt synthesis increases, likely functions mainly as a
CC galactolipase and monoacylglycerol lipase (By similarity). Hydrolyzes
CC monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG)
CC present in a plant-based diet, releasing long-chain polyunsaturated
CC fatty acids (By similarity). Hydrolyzes medium- and long-chain fatty
CC acyls in galactolipids. May act together with LIPF to hydrolyze
CC partially digested triglycerides (By similarity). Hydrolyzes long-chain
CC monoglycerides with high efficiency (By similarity). In cytotoxic T
CC cells, contributes to perforin-dependent cell lysis, but is unlikely to
CC mediate direct cytotoxicity (By similarity). Also has low phospholipase
CC activity (PubMed:23770034). In neurons, required for the localization
CC of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips
CC through acyl chain remodeling of membrane phospholipids (By
CC similarity). The resulting OPPC-rich lipid membrane domain recruits the
CC t-SNARE protein STX4 by selectively interacting with the STX4
CC transmembrane domain and this promotes surface expression of the
CC dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion
CC of SLC6A3-containing transport vesicles with the plasma membrane (By
CC similarity). {ECO:0000250|UniProtKB:P17892,
CC ECO:0000250|UniProtKB:P54317, ECO:0000250|UniProtKB:P54318,
CC ECO:0000269|PubMed:23770034}.
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:23770034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:23770034};
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:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190;
CC Evidence={ECO:0000250|UniProtKB:P54317};
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:0000269|PubMed:23770034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:23770034};
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:23770034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000305|PubMed:23770034};
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:0000269|PubMed:23770034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865;
CC Evidence={ECO:0000305|PubMed:23770034};
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:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48701;
CC Evidence={ECO:0000250|UniProtKB:P54317};
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:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48697;
CC Evidence={ECO:0000250|UniProtKB:P54317};
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:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48709;
CC Evidence={ECO:0000250|UniProtKB:P54317};
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:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48693;
CC Evidence={ECO:0000250|UniProtKB:P54317};
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:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48517;
CC Evidence={ECO:0000250|UniProtKB:P54317};
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:23770034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44665;
CC Evidence={ECO:0000305|PubMed:23770034};
CC -!- ACTIVITY REGULATION: Up-regulated by CLPS in the presence of increasing
CC concentrations of bile salts. {ECO:0000269|PubMed:23770034}.
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC {ECO:0000269|PubMed:23770034}.
CC -!- PATHWAY: Glycolipid metabolism. {ECO:0000269|PubMed:23770034}.
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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AK231359; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; EU715062; ACI00230.1; -; mRNA.
DR EMBL; EU715063; ACI00231.1; -; Genomic_DNA.
DR RefSeq; NP_001177220.1; NM_001190291.1.
DR AlphaFoldDB; D7EZN2; -.
DR SMR; D7EZN2; -.
DR SwissLipids; SLP:000001433; -.
DR ESTHER; pig-a0a287b364; Pancreatic_lipase.
DR GeneID; 100462755; -.
DR KEGG; ssc:100462755; -.
DR CTD; 5408; -.
DR UniPathway; UPA00256; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0047714; F:galactolipase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; IDA:UniProtKB.
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; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell projection; Cytoplasmic vesicle; Disulfide bond;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..471
FT /note="Pancreatic lipase-related protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5009996558"
FT DOMAIN 359..471
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 93..105
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT REGION 257..279
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 21..27
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 109..120
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 256..280
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 304..317
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 320..325
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 455..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
SQ SEQUENCE 471 AA; 53199 MW; F20CC860496E9992 CRC64;
MLPSWTIGLL LLATVRGKEI CYQPFGCFSD ETPWARTCHW PFKLFPWAPK DIDTHFLLYT
NENPNNFQLI NITNLDTIEA SNFQLDRKTR FIIHGFIDKG EDSWPSEMCK KMFKVEKVNC
ICVDWRRGAL TRYTQAVHNT RVVGAEIAFL IQGLSTKFDY NPENVHLIGH SLGAHTAAEA
GRRLGGHVGR LTGLDPAQPC FQNTPEEVRL DPSDAMFVDV IHTDSAPFIP FLGFGMSQKV
GHLDFYPNGG KEMPGCQKNT LSTIVDVDGI WEGIEDFAAC NHLRSYKYYS SSIFSPDGFL
GYPCASYDEF QEEENKCFPC PAEGCPKMGH YADQFQGKTS AVGQTFFLNT GDSGNFTRWR
YRVSVTLAGK RNVHGYIRIA LYGSNANSKQ YNIFKGSLQP NARYTHDIDV DLNVGKVQKV
KFLWYNHIID LFHPELGASQ VMVQSGEDKT EHKFCGSDTV RENILQTLNP C
