CEL_HUMAN
ID CEL_HUMAN Reviewed; 753 AA.
AC P19835; Q16398; Q5T7U7; Q9UCH1; Q9UP41;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Bile salt-activated lipase;
DE Short=BAL;
DE EC=3.1.1.13 {ECO:0000269|PubMed:8471055};
DE EC=3.1.1.3 {ECO:0000269|PubMed:8471055};
DE EC=3.1.1.6 {ECO:0000269|PubMed:10220579};
DE AltName: Full=Bile salt-stimulated lipase;
DE Short=BSSL;
DE AltName: Full=Bucelipase;
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=BAL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Mammary gland;
RX PubMed=1698625; DOI=10.1111/j.1432-1033.1990.tb19259.x;
RA Nilsson J., Blaeckberg L., Carlsson P., Enerbaeck S., Hernell O.,
RA Bjursell G.;
RT "cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for
RT its identity to pancreatic carboxylic ester hydrolase.";
RL Eur. J. Biochem. 192:543-550(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Pancreas;
RX PubMed=2265692; DOI=10.1016/0014-5793(90)80525-n;
RA Hui D.Y., Kissel J.A.;
RT "Sequence identity between human pancreatic cholesterol esterase and bile
RT salt-stimulated milk lipase.";
RL FEBS Lett. 276:131-134(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND PROTEIN SEQUENCE OF 21-81;
RP 122-126; 190-194; 275-279; 302-306; 445-449; 485-490; 500-507; 526-528 AND
RP 531-538.
RC TISSUE=Mammary gland, and Milk;
RX PubMed=1988041; DOI=10.1021/bi00216a028;
RA Baba T., Downs D., Jackson K.W., Tang J., Wang C.-S.;
RT "Structure of human milk bile salt activated lipase.";
RL Biochemistry 30:500-510(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1639390; DOI=10.1016/0888-7543(92)90134-e;
RA Lidberg U., Nilsson J., Stroemberg K., Stenman G., Sahlin P., Enerbaeck S.,
RA Bjursell G.;
RT "Genomic organization, sequence analysis, and chromosomal localization of
RT the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene.";
RL Genomics 13:630-640(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX PubMed=7578248; DOI=10.1016/0167-4781(95)00141-3;
RA Roudani S., Miralles F., Margotat A., Escribano M.J., Lombardo D.;
RT "Bile salt-dependent lipase transcripts in human fetal tissues.";
RL Biochim. Biophys. Acta 1264:141-150(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9530636; DOI=10.1007/s003359900762;
RA Madeyski K., Lidberg U., Bjursell G., Nilsson J.;
RT "Structure and organization of the human carboxyl ester lipase locus.";
RL Mamm. Genome 9:334-338(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 53-76 AND 366-374, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-455.
RC TISSUE=Milk;
RX PubMed=8471055; DOI=10.1042/bj2910065;
RA Hui D.Y., Hayakawa K., Oizumi J.;
RT "Lipoamidase activity in normal and mutagenized pancreatic cholesterol
RT esterase (bile salt-stimulated lipase).";
RL Biochem. J. 291:65-69(1993).
RN [10]
RP PARTIAL PROTEIN SEQUENCE, AND ACTIVE SITE.
RX PubMed=1991511; DOI=10.1016/0014-5793(91)80114-i;
RA Christie D.L., Cleverly D.R., O'Connor C.J.O.;
RT "Human milk bile-salt stimulated lipase. Sequence similarity with rat
RT lysophospholipase and homology with the active site region of
RT cholinesterases.";
RL FEBS Lett. 278:190-194(1991).
RN [11]
RP GLYCOSYLATION AT THR-558; THR-569; THR-579; THR-607; THR-618; THR-629;
RP THR-640; THR-651; THR-662 AND THR-673.
RX PubMed=7654718; DOI=10.1021/bi00033a039;
RA Wang C.S., Dashti A., Jackson K.W., Yeh J.C., Cummings R.D., Tang J.;
RT "Isolation and characterization of human milk bile salt-activated lipase C-
RT tail fragment.";
RL Biochemistry 34:10639-10644(1995).
RN [12]
RP STRUCTURE OF N-LINKED CARBOHYDRATES.
RX PubMed=10024660; DOI=10.1093/glycob/9.3.227;
RA Mechref Y., Chen P., Novotny M.V.;
RT "Structural characterization of the N-linked oligosaccharides in bile salt-
RT stimulated lipase originated from human breast milk.";
RL Glycobiology 9:227-234(1999).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC TISSUE=Milk;
RX PubMed=10220579; DOI=10.1093/oxfordjournals.jbchem.a022364;
RA Tanaka H., Mierau I., Ito F.;
RT "Purification and characterization of bovine pancreatic bile salt-activated
RT lipase.";
RL J. Biochem. 125:883-890(1999).
RN [14]
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 [15]
RP POLYMORPHISM.
RX PubMed=12166660; DOI=10.1007/s100380200027;
RA Higuchi S., Nakamura Y., Saito S.;
RT "Characterization of a VNTR polymorphism in the coding region of the CEL
RT gene.";
RL J. Hum. Genet. 47:213-215(2002).
RN [16]
RP INVOLVEMENT IN MODY8, AND POLYMORPHISM.
RX PubMed=16369531; DOI=10.1038/ng1708;
RA Raeder H., Johansson S., Holm P.I., Haldorsen I.S., Mas E., Sbarra V.,
RA Nermoen I., Eide S.A., Grevle L., Bjoerkhaug L., Sagen J.V., Aksnes L.,
RA Soevik O., Lombardo D., Molven A., Njoelstad P.R.;
RT "Mutations in the CEL VNTR cause a syndrome of diabetes and pancreatic
RT exocrine dysfunction.";
RL Nat. Genet. 38:54-62(2006).
RN [17]
RP POLYMORPHISM.
RX PubMed=19760265; DOI=10.1007/s00439-009-0740-8;
RA Torsvik J., Johansson S., Johansen A., Ek J., Minton J., Raeder H.,
RA Ellard S., Hattersley A., Pedersen O., Hansen T., Molven A.,
RA Njoelstad P.R.;
RT "Mutations in the VNTR of the carboxyl-ester lipase gene (CEL) are a rare
RT cause of monogenic diabetes.";
RL Hum. Genet. 127:55-64(2010).
RN [18]
RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21784842; DOI=10.1074/jbc.m111.222679;
RA Johansson B.B., Torsvik J., Bjoerkhaug L., Vesterhus M., Ragvin A.,
RA Tjora E., Fjeld K., Hoem D., Johansson S., Raeder H., Lindquist S.,
RA Hernell O., Cnop M., Saraste J., Flatmark T., Molven A., Njoelstad P.R.;
RT "Diabetes and pancreatic exocrine dysfunction due to mutations in the
RT carboxyl ester lipase gene-maturity onset diabetes of the young (CEL-MODY):
RT a protein misfolding disease.";
RL J. Biol. Chem. 286:34593-34605(2011).
RN [19]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN [20]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=27650499; DOI=10.1074/jbc.m116.734384;
RA Xiao X., Jones G., Sevilla W.A., Stolz D.B., Magee K.E., Haughney M.,
RA Mukherjee A., Wang Y., Lowe M.E.;
RT "A carboxyl ester lipase (CEL) mutant causes chronic pancreatitis by
RT forming intracellular aggregates that activate apoptosis.";
RL J. Biol. Chem. 291:23224-23236(2016).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-553.
RX PubMed=11045623; DOI=10.1110/ps.9.9.1783;
RA Terzyan S., Wang C.S., Downs D., Hunter B., Zhang X.C.;
RT "Crystal structure of the catalytic domain of human bile salt activated
RT lipase.";
RL Protein Sci. 9:1783-1790(2000).
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:8471055, PubMed:27509211, PubMed:10220579,
CC PubMed:27650499). Preferentially hydrolyzes FAHFAs with the ester bond
CC further away from the carboxylate. Unsaturated FAHFAs are hydrolyzed
CC more quickly than saturated FAHFAs (By similarity). Has an essential
CC role in the complete digestion of dietary lipids and their intestinal
CC absorption, along with the absorption of fat-soluble vitamins
CC (PubMed:8471055, PubMed:27509211, PubMed:10220579, PubMed:27650499).
CC {ECO:0000250|UniProtKB:Q64285, ECO:0000269|PubMed:10220579,
CC ECO:0000269|PubMed:27509211, ECO:0000269|PubMed:27650499,
CC ECO:0000269|PubMed:8471055}.
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:8471055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:8471055};
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:10220579};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:10220579};
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:27650499};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865;
CC Evidence={ECO:0000305|PubMed:27650499};
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:0000269|PubMed:8471055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10101;
CC Evidence={ECO:0000305|PubMed:8471055};
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:0000250|UniProtKB:P07882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876;
CC Evidence={ECO:0000250|UniProtKB:P07882};
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:0000269|PubMed:10220579};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958;
CC Evidence={ECO:0000305|PubMed:10220579};
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=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:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52057;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
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:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52061;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
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:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52065;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
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:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52069;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
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:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52073;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
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:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52077;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
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:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52081;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
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:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52085;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
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:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52093;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
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:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52097;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC -!- ACTIVITY REGULATION: Activated by bile salts such as sodium
CC taurocholate. {ECO:0000269|PubMed:10220579}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 uM for lipoyl-4-aminobenzoate {ECO:0000269|PubMed:8471055};
CC KM=15 uM for triacetin {ECO:0000269|PubMed:8471055};
CC Vmax=45.5 pmol/min/mg enzyme toward lipoyl-4-aminobenzoate
CC {ECO:0000269|PubMed:8471055};
CC Vmax=323 pmol/min/mg enzyme toward triacetin
CC {ECO:0000269|PubMed:8471055};
CC -!- SUBUNIT: Interacts with CLC. {ECO:0000269|PubMed:11834744}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21784842}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P19835-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P19835-2; Sequence=VSP_001463;
CC -!- TISSUE SPECIFICITY: Mammary gland and pancreas. Detected in pancreatic
CC and duodenal juice (at protein level) (PubMed:21784842). Expressed by
CC eosinophils. {ECO:0000269|PubMed:11834744,
CC ECO:0000269|PubMed:21784842}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:21784842}.
CC -!- POLYMORPHISM: The variable number of tandem repeats (VNTR)-region in
CC exon 11 is highly polymorphic, and VNTR number varies between 3 and 23.
CC The most common allele contains 16 repeats (PubMed:12166660,
CC PubMed:16369531, PubMed:19760265). Some alleles contain common single
CC base insertions in the VNTR region that are predicted to lead to
CC protein truncation and may be associated with an increased risk of
CC exocrine pancreatic dysfunction in autoimmune diabetes
CC (PubMed:16369531). {ECO:0000269|PubMed:12166660,
CC ECO:0000269|PubMed:16369531, ECO:0000269|PubMed:19760265}.
CC -!- DISEASE: Maturity-onset diabetes of the young 8 with exocrine
CC dysfunction (MODY8) [MIM:609812]: An autosomal dominant form of
CC diabetes characterized by a primary defect in insulin secretion,
CC exocrine pancreatic dysfunction, altered pancreatic morphology,
CC recurrent abdominal pain, and fecal elastase deficiency. Disease onset
CC is at less than 25 years of age. {ECO:0000269|PubMed:16369531}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry. Single base deletions in the VNTR-region, that result in
CC frame shift and protein truncation, have been identified as disease
CC causing variants in MODY8 families (PubMed:16369531).
CC {ECO:0000269|PubMed:16369531}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA51973.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA52014.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAC26514.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA38325.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAW88033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; X54457; CAA38325.1; ALT_INIT; mRNA.
DR EMBL; M85201; AAA52014.1; ALT_INIT; mRNA.
DR EMBL; M54994; AAA63211.1; -; mRNA.
DR EMBL; M94579; AAA51973.1; ALT_INIT; Genomic_DNA.
DR EMBL; S79774; AAB35488.2; -; mRNA.
DR EMBL; AF072711; AAC26514.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL162417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88033.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS43896.1; -. [P19835-1]
DR PIR; S13586; S13586.
DR PDB; 1F6W; X-ray; 2.30 A; A=21-553.
DR PDB; 1JMY; X-ray; 2.60 A; A=21-538.
DR PDB; 6H0T; X-ray; 1.90 A; A=22-553.
DR PDB; 6H0V; X-ray; 2.20 A; A=22-553.
DR PDB; 6H18; X-ray; 1.85 A; A=22-553.
DR PDB; 6H19; X-ray; 1.89 A; A=22-553.
DR PDB; 6H1A; X-ray; 1.75 A; A=22-553.
DR PDBsum; 1F6W; -.
DR PDBsum; 1JMY; -.
DR PDBsum; 6H0T; -.
DR PDBsum; 6H0V; -.
DR PDBsum; 6H18; -.
DR PDBsum; 6H19; -.
DR PDBsum; 6H1A; -.
DR AlphaFoldDB; P19835; -.
DR SMR; P19835; -.
DR IntAct; P19835; 1.
DR STRING; 9606.ENSP00000361151; -.
DR BindingDB; P19835; -.
DR ChEMBL; CHEMBL3219; -.
DR DrugBank; DB04348; Taurocholic acid.
DR SwissLipids; SLP:000000874; -.
DR ESTHER; human-CEL; Cholesterol_esterase.
DR MEROPS; S09.985; -.
DR GlyConnect; 74; 15 N-Linked glycans (1 site), 9 O-Linked glycans.
DR GlyGen; P19835; 12 sites, 25 N-linked glycans (2 sites), 17 O-linked glycans (1 site).
DR iPTMnet; P19835; -.
DR PhosphoSitePlus; P19835; -.
DR BioMuta; CEL; -.
DR DMDM; 251757481; -.
DR jPOST; P19835; -.
DR MassIVE; P19835; -.
DR MaxQB; P19835; -.
DR PaxDb; P19835; -.
DR PeptideAtlas; P19835; -.
DR PRIDE; P19835; -.
DR ProteomicsDB; 53692; -. [P19835-1]
DR ProteomicsDB; 53693; -. [P19835-2]
DR Antibodypedia; 1990; 235 antibodies from 27 providers.
DR Ensembl; ENST00000372080.8; ENSP00000361151.6; ENSG00000170835.17. [P19835-1]
DR MANE-Select; ENST00000372080.8; ENSP00000361151.6; NM_001807.6; NP_001798.3.
DR GeneCards; CEL; -.
DR GeneReviews; CEL; -.
DR HGNC; HGNC:1848; CEL.
DR HPA; ENSG00000170835; Tissue enriched (pancreas).
DR MalaCards; CEL; -.
DR MIM; 114840; gene.
DR MIM; 609812; phenotype.
DR neXtProt; NX_P19835; -.
DR OpenTargets; ENSG00000170835; -.
DR Orphanet; 552; MODY.
DR PharmGKB; PA26391; -.
DR VEuPathDB; HostDB:ENSG00000170835; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000156231; -.
DR InParanoid; P19835; -.
DR PhylomeDB; P19835; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.13; 2681.
DR PathwayCommons; P19835; -.
DR Reactome; R-HSA-192456; Digestion of dietary lipid.
DR SABIO-RK; P19835; -.
DR SignaLink; P19835; -.
DR ChiTaRS; CEL; human.
DR EvolutionaryTrace; P19835; -.
DR Pharos; P19835; Tchem.
DR PRO; PR:P19835; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P19835; protein.
DR Bgee; ENSG00000170835; Expressed in body of pancreas and 115 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0008126; F:acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0003824; F:catalytic activity; TAS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; NAS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; TAS:UniProtKB.
DR GO; GO:0050253; F:retinyl-palmitate esterase activity; IBA:GO_Central.
DR GO; GO:0004771; F:sterol esterase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IBA:GO_Central.
DR GO; GO:0046514; P:ceramide catabolic process; IBA:GO_Central.
DR GO; GO:0030299; P:intestinal cholesterol absorption; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; NAS:UniProtKB.
DR GO; GO:0030157; P:pancreatic juice secretion; IDA:UniProtKB.
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 InterPro; IPR032059; Mucin-like.
DR PANTHER; PTHR43903:SF1; PTHR43903:SF1; 1.
DR Pfam; PF00135; COesterase; 1.
DR Pfam; PF16058; Mucin-like; 3.
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 3D-structure; Alternative splicing; Diabetes mellitus;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Reference proteome; Repeat; Secreted;
KW Serine esterase; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1988041"
FT CHAIN 21..753
FT /note="Bile salt-activated lipase"
FT /id="PRO_0000008631"
FT REPEAT 559..569
FT /note="1"
FT REPEAT 570..580
FT /note="2"
FT REPEAT 581..591
FT /note="3"
FT REPEAT 592..602
FT /note="4"
FT REPEAT 603..613
FT /note="5"
FT REPEAT 614..624
FT /note="6"
FT REPEAT 625..635
FT /note="7"
FT REPEAT 636..646
FT /note="8"
FT REPEAT 647..657
FT /note="9"
FT REPEAT 658..668
FT /note="10"
FT REPEAT 669..679
FT /note="11"
FT REPEAT 680..690
FT /note="12"
FT REPEAT 691..701
FT /note="13"
FT REPEAT 702..712
FT /note="14"
FT REPEAT 713..723
FT /note="15"
FT REPEAT 724..734
FT /note="16"
FT REPEAT 735..745
FT /note="17"
FT REGION 21..121
FT /note="Heparin-binding"
FT REGION 555..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..745
FT /note="17 X 11 AA tandem repeats, glycodomain, O-linked
FT (mucin type)"
FT COMPBIAS 585..700
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..733
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 214
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039,
FT ECO:0000269|PubMed:1991511"
FT ACT_SITE 340
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:1991511"
FT ACT_SITE 455
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:1991511"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /id="CAR_000141"
FT CARBOHYD 558
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7654718"
FT CARBOHYD 569
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7654718"
FT CARBOHYD 579
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7654718"
FT CARBOHYD 607
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7654718"
FT CARBOHYD 618
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7654718"
FT CARBOHYD 629
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7654718"
FT CARBOHYD 640
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7654718"
FT CARBOHYD 651
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7654718"
FT CARBOHYD 662
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7654718"
FT CARBOHYD 673
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7654718"
FT DISULFID 84..100
FT DISULFID 266..277
FT VAR_SEQ 430..495
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001463"
FT MUTAGEN 455
FT /note="H->Q: Abolishes lipase activity. Decreases Vmax for
FT esterase activity by 2.5-fold."
FT /evidence="ECO:0000269|PubMed:8471055"
FT CONFLICT 73
FT /note="Missing (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="R -> A (in Ref. 5; AAB35488)"
FT /evidence="ECO:0000305"
FT CONFLICT 284..288
FT /note="RALTL -> AAVTV (in Ref. 5; AAB35488)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="G -> E (in Ref. 5; AAB35488)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="T -> I (in Ref. 5; AAB35488)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="S -> F (in Ref. 5; AAB35488)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="A -> P (in Ref. 5; AAB35488)"
FT /evidence="ECO:0000305"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:6H1A"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1JMY"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1JMY"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1JMY"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 203..213
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6H1A"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:6H1A"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1F6W"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:6H1A"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 342..348
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:1JMY"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:6H0V"
FT HELIX 397..412
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 414..427
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:6H1A"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:6H0T"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 475..494
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:6H1A"
FT TURN 513..515
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:6H1A"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:6H1A"
FT HELIX 536..543
FT /evidence="ECO:0007829|PDB:6H1A"
FT TURN 544..548
FT /evidence="ECO:0007829|PDB:6H1A"
SQ SEQUENCE 753 AA; 79322 MW; B3253789D1EABF7F CRC64;
MGRLQLVVLG LTCCWAVASA AKLGAVYTEG GFVEGVNKKL GLLGDSVDIF KGIPFAAPTK
ALENPQPHPG WQGTLKAKNF KKRCLQATIT QDSTYGDEDC LYLNIWVPQG RKQVSRDLPV
MIWIYGGAFL MGSGHGANFL NNYLYDGEEI ATRGNVIVVT FNYRVGPLGF LSTGDANLPG
NYGLRDQHMA IAWVKRNIAA FGGDPNNITL FGESAGGASV SLQTLSPYNK GLIRRAISQS
GVALSPWVIQ KNPLFWAKKV AEKVGCPVGD AARMAQCLKV TDPRALTLAY KVPLAGLEYP
MLHYVGFVPV IDGDFIPADP INLYANAADI DYIAGTNNMD GHIFASIDMP AINKGNKKVT
EEDFYKLVSE FTITKGLRGA KTTFDVYTES WAQDPSQENK KKTVVDFETD VLFLVPTEIA
LAQHRANAKS AKTYAYLFSH PSRMPVYPKW VGADHADDIQ YVFGKPFATP TGYRPQDRTV
SKAMIAYWTN FAKTGDPNMG DSAVPTHWEP YTTENSGYLE ITKKMGSSSM KRSLRTNFLR
YWTLTYLALP TVTDQEATPV PPTGDSEATP VPPTGDSETA PVPPTGDSGA PPVPPTGDSG
APPVPPTGDS GAPPVPPTGD SGAPPVPPTG DSGAPPVPPT GDSGAPPVPP TGDSGAPPVP
PTGDSGAPPV PPTGDAGPPP VPPTGDSGAP PVPPTGDSGA PPVTPTGDSE TAPVPPTGDS
GAPPVPPTGD SEAAPVPPTD DSKEAQMPAV IRF
