CEL_MOUSE
ID CEL_MOUSE Reviewed; 599 AA.
AC Q64285;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Bile salt-activated lipase;
DE Short=BAL;
DE EC=3.1.1.13 {ECO:0000250|UniProtKB:P19835};
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:P19835};
DE EC=3.1.1.6 {ECO:0000250|UniProtKB:P19835};
DE AltName: Full=Bile salt-stimulated lipase;
DE Short=BSSL;
DE AltName: Full=Carboxyl ester lipase;
DE AltName: Full=Cholesterol esterase;
DE AltName: Full=Pancreatic lysophospholipase;
DE AltName: Full=Sterol esterase;
DE Flags: Precursor;
GN Name=Cel; Synonyms=Lip1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Mammary gland;
RX PubMed=8522186; DOI=10.1016/0378-1119(95)00564-m;
RA Mackay K., Lawn R.M.;
RT "Characterization of the mouse pancreatic/mammary gland cholesterol
RT esterase-encoding cDNA and gene.";
RL Gene 165:255-259(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lactating mammary gland;
RX PubMed=8530060; DOI=10.1006/geno.1995.1221;
RA Lidmer A.S., Kannius M., Lundberg L., Bjursell G., Nilsson J.;
RT "Molecular cloning and characterization of the mouse carboxyl ester lipase
RT gene and evidence for expression in the lactating mammary gland.";
RL Genomics 29:115-122(1995).
RN [3]
RP INTERACTION WITH CLC, AND TISSUE SPECIFICITY.
RX PubMed=11834744; DOI=10.1074/jbc.m200221200;
RA Ackerman S.J., Liu L., Kwatia M.A., Savage M.P., Leonidas D.D.,
RA Swaminathan G.J., Acharya K.R.;
RT "Charcot-Leyden crystal protein (galectin-10) is not a dual function
RT galectin with lysophospholipase activity but binds a lysophospholipase
RT inhibitor in a novel structural fashion.";
RL J. Biol. Chem. 277:14859-14868(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=27509211; DOI=10.1021/acs.biochem.6b00565;
RA Kolar M.J., Kamat S.S., Parsons W.H., Homan E.A., Maher T., Peroni O.D.,
RA Syed I., Fjeld K., Molven A., Kahn B.B., Cravatt B.F., Saghatelian A.;
RT "Branched fatty acid esters of hydroxy fatty acids are preferred substrates
RT of the MODY8 protein carboxyl ester lipase.";
RL Biochemistry 55:4636-4641(2016).
CC -!- FUNCTION: Catalyzes the hydrolysis of a wide range of substrates
CC including cholesteryl esters, phospholipids, lysophospholipids, di- and
CC tri-acylglycerols, and fatty acid esters of hydroxy fatty acids
CC (FAHFAs) (PubMed:27509211). Preferentially hydrolyzes FAHFAs with the
CC ester bond further away from the carboxylate. Unsaturated FAHFAs are
CC hydrolyzed more quickly than saturated FAHFAs (PubMed:27509211). Has an
CC essential role in the complete digestion of dietary lipids and their
CC intestinal absorption, along with the absorption of fat-soluble
CC vitamins (By similarity). {ECO:0000250|UniProtKB:P19835,
CC ECO:0000269|PubMed:27509211}.
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:P19835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:P19835};
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:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:27509211};
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:P19835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sterol ester + H2O = a fatty acid + a sterol + H(+);
CC Xref=Rhea:RHEA:10100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15889, ChEBI:CHEBI:28868, ChEBI:CHEBI:35915; EC=3.1.1.13;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10101;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+);
CC Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; EC=3.1.1.6;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000250|UniProtKB:P07882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000250|UniProtKB:P07882};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-hexadecanoyloxy-octadecanoate + H2O = 9-hydroxy-
CC octadecanoate + H(+) + hexadecanoate; Xref=Rhea:RHEA:52052,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:83670, ChEBI:CHEBI:136286;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52053;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC octadecenoate + 9-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52048,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:136282, ChEBI:CHEBI:136286;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52049;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate +
CC cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:46898; Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000250|UniProtKB:P07882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:P07882};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-hexadecanoyloxy-octadecanoate + H2O = 12-
CC hydroxyoctadecanoate + H(+) + hexadecanoate; Xref=Rhea:RHEA:52056,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:83677, ChEBI:CHEBI:84201;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52057;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC octadecenoate + 12-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:52060,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:84201, ChEBI:CHEBI:136302;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52061;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC octadecenoate + 13-hydroxy-octadecanoate + H(+);
CC Xref=Rhea:RHEA:52064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:136303, ChEBI:CHEBI:136304;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52065;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC hexadecenoate + 9-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52068,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:136286, ChEBI:CHEBI:136309;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52069;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC hexadecenoate + 12-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:52072,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:84201, ChEBI:CHEBI:136312;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52073;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC hexadecenoate + 13-hydroxy-octadecanoate + H(+);
CC Xref=Rhea:RHEA:52076, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32372, ChEBI:CHEBI:136304, ChEBI:CHEBI:136315;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52077;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-octadecanoyloxy-octadecanoate + H2O = 12-
CC hydroxyoctadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52080,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:84201, ChEBI:CHEBI:136330;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52081;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-octadecanoyloxy-octadecanoate + H2O = 13-hydroxy-
CC octadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52084,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:136304, ChEBI:CHEBI:136335;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52085;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC hexadecenoate + 5-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52092,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:136369, ChEBI:CHEBI:136370;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52093;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-octadecanoyloxy-octadecanoate + H2O = 9-hydroxy-
CC octadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52096,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:136286, ChEBI:CHEBI:136373;
CC Evidence={ECO:0000269|PubMed:27509211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52097;
CC Evidence={ECO:0000305|PubMed:27509211};
CC -!- ACTIVITY REGULATION: Activated by bile salts such as sodium
CC taurocholate. {ECO:0000269|PubMed:27509211}.
CC -!- SUBUNIT: Interacts with CLC. {ECO:0000269|PubMed:11834744}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P19835}.
CC -!- TISSUE SPECIFICITY: EXpressed by eosinophils.
CC {ECO:0000269|PubMed:11834744}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; U33169; AAA92088.1; -; mRNA.
DR EMBL; U37386; AAC52279.1; -; mRNA.
DR CCDS; CCDS15841.1; -.
DR PIR; A57701; A57701.
DR RefSeq; NP_034015.1; NM_009885.2.
DR AlphaFoldDB; Q64285; -.
DR SMR; Q64285; -.
DR STRING; 10090.ENSMUSP00000028161; -.
DR SwissLipids; SLP:000001681; -.
DR ESTHER; mouse-pches; Cholesterol_esterase.
DR MEROPS; S09.985; -.
DR GlyGen; Q64285; 2 sites.
DR PhosphoSitePlus; Q64285; -.
DR SWISS-2DPAGE; Q64285; -.
DR MaxQB; Q64285; -.
DR PaxDb; Q64285; -.
DR PRIDE; Q64285; -.
DR ProteomicsDB; 281531; -.
DR Antibodypedia; 1990; 235 antibodies from 27 providers.
DR DNASU; 12613; -.
DR Ensembl; ENSMUST00000028161; ENSMUSP00000028161; ENSMUSG00000026818.
DR GeneID; 12613; -.
DR KEGG; mmu:12613; -.
DR UCSC; uc008iyr.1; mouse.
DR CTD; 1056; -.
DR MGI; MGI:88374; Cel.
DR VEuPathDB; HostDB:ENSMUSG00000026818; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000156231; -.
DR HOGENOM; CLU_006586_13_1_1; -.
DR InParanoid; Q64285; -.
DR OMA; MEYPMLY; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q64285; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.13; 3474.
DR Reactome; R-MMU-192456; Digestion of dietary lipid.
DR BioGRID-ORCS; 12613; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Cel; mouse.
DR PRO; PR:Q64285; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q64285; protein.
DR Bgee; ENSMUSG00000026818; Expressed in pyloric antrum and 36 other tissues.
DR ExpressionAtlas; Q64285; baseline and differential.
DR Genevisible; Q64285; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0042588; C:zymogen granule; ISO:MGI.
DR GO; GO:0008126; F:acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISO:MGI.
DR GO; GO:0043208; F:glycosphingolipid binding; ISO:MGI.
DR GO; GO:0004622; F:lysophospholipase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0050253; F:retinyl-palmitate esterase activity; ISO:MGI.
DR GO; GO:0004771; F:sterol esterase activity; ISO:MGI.
DR GO; GO:0004806; F:triglyceride lipase activity; ISO:MGI.
DR GO; GO:0046514; P:ceramide catabolic process; IMP:MGI.
DR GO; GO:0030299; P:intestinal cholesterol absorption; ISO:MGI.
DR GO; GO:0030157; P:pancreatic juice secretion; ISO:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR033560; BAL.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR PANTHER; PTHR43903:SF1; PTHR43903:SF1; 1.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Repeat; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..599
FT /note="Bile salt-activated lipase"
FT /id="PRO_0000008632"
FT REPEAT 559..569
FT /note="1"
FT REPEAT 570..580
FT /note="2"
FT REPEAT 581..588
FT /note="3"
FT REGION 553..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..588
FT /note="4 X 11 AA tandem repeats, O-glycosylated region"
FT ACT_SITE 214
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 340
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 455
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..100
FT /evidence="ECO:0000250"
FT DISULFID 266..277
FT /evidence="ECO:0000250"
SQ SEQUENCE 599 AA; 65813 MW; 9E4428FDFCA8602E CRC64;
MGRLEVLFLG LTCCLAAACA AKLGAVYTEG GFVEGVNKKL SLLGGDSVDI FKGIPFATAK
TLENPQRHPG WQGTLKATNF KKRCLQATIT QDNTYGQEDC LYLNIWVPQG RKQVSHNLPV
MVWIYGGAFL MGSGQGANFL KNYLYDGEEI ATRGNVIVVT FNYRVGPLGF LSTGDANLPG
NFGLRDQHMA IAWVKRNIAA FGGDPDNITI FGESAGAASV SLQTLSPYNK GLIRRAISQS
GMALSPWAIQ KNPLFWAKTI AKKVGCPTED TGKMAACLKI TDPRALTLAY KLPVKKQEYP
VVHYLAFIPV IDGDFIPDDP INLYNNTADI DYIAGINNMD GHLFATIDVP AVDKTKQTVT
EEDFYRLVSG HTVAKGLKGA QATFDIYTES WAQDPSQENM KKTVVAFETD VLFLIPTEIA
LAQHKAHAKS AKTYSYLFSH PSRMPIYPKW MGADHADDLQ YVFGKPFATP LGYRPQDRAV
SKAMIAYWTN FARSGDPNMG NSPVPTHWYP YTLENGNYLD ITKTITSASM KEHLREKFLK
FWAVTFEVLP TVTGDQDTLT PPEDDSEVAP DPPSDDSQVV PVPPTDDSVE AQMPATIGF
