LIPR2_MYOCO
ID LIPR2_MYOCO Reviewed; 470 AA.
AC Q64424;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
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:8130186};
DE Flags: Precursor;
GN Name=PNLIPRP2 {ECO:0000250|UniProtKB:P54317};
OS Myocastor coypus (Coypu) (Nutria).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha;
OC Myocastoridae; Myocastor.
OX NCBI_TaxID=10157;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-23, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=7851384; DOI=10.1111/j.1432-1033.1995.tb20375.x;
RA Thirstrup K., Carriere F., Hjorth S.A., Rasmussen P.B., Nielsen P.F.,
RA Ladefoged C., Thim L., Boel E.;
RT "Cloning and expression in insect cells of two pancreatic lipases and a
RT procolipase from Myocastor coypus.";
RL Eur. J. Biochem. 227:186-193(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=8130186; DOI=10.1021/bi00176a002;
RA Thirstrup K., Verger R., Carriere F.;
RT "Evidence for a pancreatic lipase subfamily with new kinetic properties.";
RL Biochemistry 33:2748-2756(1994).
CC -!- FUNCTION: Lipase that primarily hydrolyzes triglycerides and
CC galactosylglycerides (PubMed:8130186). 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 (By similarity). Hydrolyzes
CC short-, medium- and long-chain fatty acyls in triglycerides without
CC apparent positional specificity (By similarity). 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. 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:8130186). In neurons, required for the localization of
CC the 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:8130186}.
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:8130186};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:8130186};
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:0000269|PubMed:8130186};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000305|PubMed:8130186};
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:0000269|PubMed:8130186};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44665;
CC Evidence={ECO:0000305|PubMed:8130186};
CC -!- ACTIVITY REGULATION: Triacylglycerol lipase activity is inhibited by
CC increasing bile salts concentrations and not reactivated by CLPS.
CC {ECO:0000269|PubMed:8130186}.
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:7851384}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; X83000; CAA58121.1; -; mRNA.
DR PIR; A54232; A54232.
DR AlphaFoldDB; Q64424; -.
DR SMR; Q64424; -.
DR ESTHER; myoco-2plrp; Pancreatic_lipase.
DR UniPathway; UPA00256; -.
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; 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:0019376; P:galactolipid catabolic process; ISS:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS: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; ISS: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; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:7851384"
FT CHAIN 19..470
FT /note="Pancreatic lipase-related protein 2"
FT /id="PRO_0000017795"
FT DOMAIN 358..470
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 94..106
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT REGION 258..280
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..28
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 110..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 257..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 305..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 319..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 454..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
SQ SEQUENCE 470 AA; 52060 MW; 5F06DBCBF8648869 CRC64;
MMLFVWTTGL LLLATARGNE VCYSHLGCFS DEKPWAGTLQ RPVKSLPASP ESINTRFLLY
TNENPNNYQL ITATDPATIK ASNFNLHRKT RFVIHGFIDN GEKDWLTDIC KRMFQVEKVN
CICVDWQGGS LAIYSQAVQN IRVVGAEVAY LVQVLSDQLG YKPGNVHMIG HSLGAHTAAE
AGRRLKGLVG RITGLDPAEP CFQDTPEEVR LDPSDAMFVD VIHTDIAPII PSFGFGMSQK
VGHMDFFPNG GKEMPGCEKN IISTIVDVNG FLEGITSLAA CNHMRSYQYY SSSILNPDGF
LGYPCASYEE FQKDGCFPCP AEGCPKMGHY ADQFQGKANG VEKTYFLNTG DSDNFPRWRY
KVSVTLSGEK ELSGDIKIAL FGRNGNSKQY EIFKGSLKPD ARYTHDIDVD LNVGEIQKVK
FLWHNNGINL LQPKLGASQI TVQSGEYGTK YNFCSSNTVQ EDVLQSLSPC
