ID G1Q7B4_MYOLU Unreviewed; 471 AA.
AC G1Q7B4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Triacylglycerol lipase {ECO:0000256|RuleBase:RU362046};
DE EC=3.1.1.3 {ECO:0000256|RuleBase:RU362046};
DE AltName: Full=Pancreatic lipase {ECO:0000256|RuleBase:RU362046};
GN Name=LOC102435411 {ECO:0000313|Ensembl:ENSMLUP00000019597.1};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000019597.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000019597.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000019597.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39956;
CC Evidence={ECO:0000256|ARBA:ARBA00036227};
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:0000256|ARBA:ARBA00000652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000256|ARBA:ARBA00000652};
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:0000256|ARBA:ARBA00001601};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000256|ARBA:ARBA00001601};
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:0000256|ARBA:ARBA00036981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865;
CC Evidence={ECO:0000256|ARBA:ARBA00036981};
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:0000256|ARBA:ARBA00036387};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48025;
CC Evidence={ECO:0000256|ARBA:ARBA00036387};
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:0000256|ARBA:ARBA00036325};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48373;
CC Evidence={ECO:0000256|ARBA:ARBA00036325};
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:0000256|ARBA:ARBA00036578};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48597;
CC Evidence={ECO:0000256|ARBA:ARBA00036578};
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:0000256|ARBA:ARBA00036129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48517;
CC Evidence={ECO:0000256|ARBA:ARBA00036129};
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:0000256|ARBA:ARBA00036023};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48541;
CC Evidence={ECO:0000256|ARBA:ARBA00036023};
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:0000256|ARBA:ARBA00036257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48693;
CC Evidence={ECO:0000256|ARBA:ARBA00036257};
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:0000256|ARBA:ARBA00036373};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48697;
CC Evidence={ECO:0000256|ARBA:ARBA00036373};
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:0000256|ARBA:ARBA00023407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000256|ARBA:ARBA00023407};
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:0000256|ARBA:ARBA00036575};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48537;
CC Evidence={ECO:0000256|ARBA:ARBA00036575};
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:0000256|ARBA:ARBA00035982};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48709;
CC Evidence={ECO:0000256|ARBA:ARBA00035982};
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:0000256|ARBA:ARBA00035858};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48701;
CC Evidence={ECO:0000256|ARBA:ARBA00035858};
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:0000256|ARBA:ARBA00036503};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190;
CC Evidence={ECO:0000256|ARBA:ARBA00036503};
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:0000256|ARBA:ARBA00036063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44665;
CC Evidence={ECO:0000256|ARBA:ARBA00036063};
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:0000256|ARBA:ARBA00023369};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000256|ARBA:ARBA00023369};
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:0000256|ARBA:ARBA00036921};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47869;
CC Evidence={ECO:0000256|ARBA:ARBA00036921};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC {ECO:0000256|ARBA:ARBA00004879}.
CC -!- PATHWAY: Glycolipid metabolism. {ECO:0000256|ARBA:ARBA00023590}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SUBCELLULAR LOCATION: Cell projection, neuron projection
CC {ECO:0000256|ARBA:ARBA00004487}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU362046}. Zymogen
CC granule membrane {ECO:0000256|ARBA:ARBA00024321}; Peripheral membrane
CC protein {ECO:0000256|ARBA:ARBA00024321}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
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DR EMBL; AAPE02016473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1Q7B4; -.
DR STRING; 59463.ENSMLUP00000019597; -.
DR ESTHER; myolu-g1pat6; Pancreatic_lipase.
DR Ensembl; ENSMLUT00000023094.1; ENSMLUP00000019597.1; ENSMLUG00000008126.2.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR GeneTree; ENSGT00940000155139; -.
DR InParanoid; G1Q7B4; -.
DR OMA; WIHDINE; -.
DR TreeFam; TF324997; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0042589; C:zymogen granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047714; F:galactolipase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00707; Pancreat_lipase_like; 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.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000865-3,
KW ECO:0000256|RuleBase:RU362046};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU362046};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU362046};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU362046};
KW Signal {ECO:0000256|RuleBase:RU362046}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU362046"
FT CHAIN 18..471
FT /note="Triacylglycerol lipase"
FT /evidence="ECO:0000256|RuleBase:RU362046"
FT /id="PRO_5005131103"
FT DOMAIN 359..471
FT /note="PLAT"
FT /evidence="ECO:0000259|SMART:SM00308"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 284
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT DISULFID 21..27
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3"
FT DISULFID 109..120
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3"
FT DISULFID 256..282
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3"
FT DISULFID 306..317
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3"
FT DISULFID 320..325
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3"
FT DISULFID 455..471
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3"
SQ SEQUENCE 471 AA; 53054 MW; FF07EBC521B07E8A CRC64;
MLPSWIVGLL LLATVRGKEV CYEPFGCFPD DKPWTGILQR PLKLFPWPPK LIKTRFLLYT
NENPNSYQPI SSMNLATVNI SNFQLDRKTR FIIHGFIDKG EERWLMDMCQ KMFKVERVNC
ICVDWKRGAR TGYNQAVHNI RVVGAEIAFL IQELSTKMGY SLKKVHIIGH SLGAHAAGEA
GRRLGGSVGR ITGLDPAEPG FQGTPEEVRL DPSDAMFVDV IHTDTSPTVP YLGFGMSQKV
GHLDFYPNGG KQMPGCKKNI PSPIVDFNFS AFTSELSSFK TCNHLRSYKY YASSILNPDG
FLGYPCASYE KFQKNGCFPC PVTGCPKMGH YADQFLGKTR AVGQTFFLNT GASGNFARWR
YRVAVTLAGK KTRSGSFSIA LYGRNRNSGQ YEIFSGSLKP HTKYVRDIDV DFNVGKIQKV
TFLWRKHGIN LIWYKLGALR VTVQSGEYGT EYKFCSCETV RQKRLQTLYP C
//
