ID LIPR2_BOVIN Reviewed; 469 AA.
AC A5PK46;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 86.
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:0000250|UniProtKB:P54317};
DE Flags: Precursor;
GN Name=PNLIPRP2 {ECO:0000250|UniProtKB:P54317};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pancreas;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipase that primarily hydrolyzes triglycerides and
CC galactosylglycerides. 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. Hydrolyzes short-, medium- and long-chain fatty
CC acyls in triglycerides without apparent positional specificity. Can
CC completely deacylate triacylglycerols. When the liver matures and bile
CC salt synthesis increases, likely functions mainly as a galactolipase
CC and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols
CC (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based
CC diet, releasing long-chain polyunsaturated fatty acids. Hydrolyzes
CC medium- and long-chain fatty acyls in galactolipids. May act together
CC with LIPF to hydrolyze partially digested triglycerides. Hydrolyzes
CC long-chain monoglycerides with high efficiency (By similarity). In
CC cytotoxic T cells, contributes to perforin-dependent cell lysis, but is
CC unlikely to mediate direct cytotoxicity (By similarity). Also has low
CC phospholipase activity (By similarity). In neurons, required for the
CC localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to
CC neurite tips through acyl chain remodeling of membrane phospholipids
CC (By similarity). The resulting OPPC-rich lipid membrane domain recruits
CC the 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 -!- 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:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:P54317};
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: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:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000250|UniProtKB:P54317};
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: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:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44665;
CC Evidence={ECO:0000250|UniProtKB:P54317};
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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; BC142351; AAI42352.1; -; mRNA.
DR RefSeq; NP_001098825.1; NM_001105355.2.
DR AlphaFoldDB; A5PK46; -.
DR SMR; A5PK46; -.
DR STRING; 9913.ENSBTAP00000015106; -.
DR ESTHER; bovin-lipr2; Pancreatic_lipase.
DR GlyCosmos; A5PK46; 4 sites, No reported glycans.
DR Ensembl; ENSBTAT00000015106.6; ENSBTAP00000015106.6; ENSBTAG00000000765.6.
DR GeneID; 510772; -.
DR KEGG; bta:510772; -.
DR CTD; 5408; -.
DR VEuPathDB; HostDB:ENSBTAG00000000765; -.
DR GeneTree; ENSGT00940000155139; -.
DR InParanoid; A5PK46; -.
DR OMA; CFSNEKP; -.
DR OrthoDB; 3428256at2759; -.
DR Reactome; R-BTA-192456; Digestion of dietary lipid.
DR UniPathway; UPA00256; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000000765; Expressed in urinary bladder and 21 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0042589; C:zymogen granule membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0047714; F:galactolipase activity; ISS:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; ISS:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0006968; P:cellular defense response; IEA:Ensembl.
DR GO; GO:0019376; P:galactolipid catabolic process; ISS:UniProtKB.
DR GO; GO:0044258; P:intestinal lipid catabolic process; IEA:Ensembl.
DR GO; GO:0009395; P:phospholipid catabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR CDD; cd01759; PLAT_PL; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 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; LIPASE; 1.
DR PANTHER; PTHR11610:SF165; PANCREATIC LIPASE-RELATED PROTEIN 2; 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; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 2: Evidence at transcript 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..469
FT /note="Pancreatic lipase-related protein 2"
FT /id="PRO_0000355143"
FT DOMAIN 357..469
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:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="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"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 109..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 256..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 304..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 318..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 453..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
SQ SEQUENCE 469 AA; 52193 MW; 9B4BD4A17CCCA121 CRC64;
MLPSWTIGLL LLATVRGKEI CYEPFGCFSD EKPWTGILQR PLKLFPWSPE DIDAHFLLYT
NENPNNYQRI NITDLATVRA SNFQLDRKTR FVIHGFIDDG DSGWPTDLCK KMFKVEKVNC
ICVDWEHGAW TKYTQAVHNT RVVGAEIAFF IQGLSTELGY GPENVHLIGH SLGAQLAAEA
GRRLGGQVGR ITGLDPAQPC FEGTPEEVRL DPSDAMFVDV IHTDSASIIP FLSLGIRQKV
GHLDFYPNGG KEMPGCQKNI LSTIIDINGI WQGIQDFVAC SHLRSYKYYS SSILNPDGFL
GYPCASYEEF QEGGCFPCPA GGCPKMGHYA DQFQGKTSAV GQTFFLNTGS SGNFTSWRYR
VSVTLAGTKK VRGSIRIALY GSNGNSKQYQ IFKGSLQPNA SHTHDIDVDL NVGKVQKVKF
LWNNNVINLF WPKLGASRVT VQGGEDRTEY NFCSNDTMRE NALQTLYPC
//
