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 27-MAR-2024, entry version 215. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; CCDS43896.2; -. [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.ENSP00000501111; -. 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 GlyCosmos; P19835; 11 sites, 43 glycans. DR GlyGen; P19835; 13 sites, 26 N-linked glycans (2 sites), 18 O-linked glycans (2 sites). DR iPTMnet; P19835; -. DR PhosphoSitePlus; P19835; -. DR BioMuta; CEL; -. DR DMDM; 251757481; -. DR jPOST; P19835; -. DR MassIVE; P19835; -. DR MaxQB; P19835; -. DR PaxDb; 9606-ENSP00000361151; -. DR PeptideAtlas; P19835; -. DR ProteomicsDB; 53692; -. [P19835-1] DR ProteomicsDB; 53693; -. [P19835-2] DR Antibodypedia; 1990; 260 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 AGR; HGNC:1848; -. 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 OrthoDB; 4386at2759; -. 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 cell types or 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: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 CDD; cd00312; Esterase_lipase; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR019826; Carboxylesterase_B_AS. DR InterPro; IPR019819; Carboxylesterase_B_CS. DR InterPro; IPR032059; Mucin-like. DR PANTHER; PTHR43903:SF9; BILE SALT-ACTIVATED LIPASE; 1. DR PANTHER; PTHR43903; NEUROLIGIN; 1. DR Pfam; PF00135; COesterase; 1. DR Pfam; PF16058; Mucin-like; 2. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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 //