ID CEL_BOVIN Reviewed; 597 AA. AC P30122; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 138. 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:0000269|PubMed:10220579}; 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; Fragment; GN Name=CEL; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2590203; DOI=10.1016/0006-291x(89)91811-1; RA Kyger E.M., Wiegand R.C., Lange L.G.; RT "Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase."; RL Biochem. Biophys. Res. Commun. 164:1302-1309(1989). RN [2] RP PROTEIN SEQUENCE OF 19-40, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY RP REGULATION. RC TISSUE=Pancreas; 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 [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 19-565, AND SEQUENCE REVISION TO RP 45. RX PubMed=9331420; DOI=10.1016/s0969-2126(97)00271-2; RA Wang X., Wang C.S., Tang J., Dyda F., Zhang X.C.; RT "The crystal structure of bovine bile salt activated lipase: insights into RT the bile salt activation mechanism."; RL Structure 5:1209-1218(1997). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 19-597. RX PubMed=9548741; DOI=10.1021/bi972989g; RA Chen J.C.-H., Miercke L.J.W., Krucinski J., Starr J.R., Saenz G., Wang X., RA Spilburg C.A., Lange L.G., Ellsworth J.L., Stroud R.M.; RT "Structure of bovine pancreatic cholesterol esterase at 1.6 A: novel RT structural features involved in lipase activation."; RL Biochemistry 37:5107-5117(1998). 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 (FAHFA) CC (PubMed:10220579). 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 (By CC similarity). {ECO:0000250|UniProtKB:P19835, CC ECO:0000250|UniProtKB:Q64285, ECO:0000269|PubMed:10220579}. 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: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: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=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:0000250|UniProtKB:P19835}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52053; CC Evidence={ECO:0000250|UniProtKB:P19835}; 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:0000250|UniProtKB:P19835}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52049; CC Evidence={ECO:0000250|UniProtKB:P19835}; 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 -!- SUBUNIT: Interacts with CLC. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P19835}. CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family. CC {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; M28402; AAA56788.1; -; mRNA. DR PIR; A33668; A33668. DR PDB; 1AKN; X-ray; 2.80 A; A=19-597. DR PDB; 1AQL; X-ray; 2.80 A; A/B=19-550. DR PDB; 2BCE; X-ray; 1.60 A; A=19-597. DR PDBsum; 1AKN; -. DR PDBsum; 1AQL; -. DR PDBsum; 2BCE; -. DR AlphaFoldDB; P30122; -. DR SMR; P30122; -. DR STRING; 9913.ENSBTAP00000032584; -. DR BindingDB; P30122; -. DR ChEMBL; CHEMBL2988; -. DR SwissLipids; SLP:000000735; -. DR ESTHER; bovin-balip; Cholesterol_esterase. DR MEROPS; S09.985; -. DR GlyCosmos; P30122; 2 sites, No reported glycans. DR PaxDb; 9913-ENSBTAP00000032584; -. DR eggNOG; KOG1516; Eukaryota. DR InParanoid; P30122; -. DR EvolutionaryTrace; P30122; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008126; F:acetylesterase activity; IEA:UniProtKB-EC. 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:0030157; P:pancreatic juice secretion; IBA:GO_Central. 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 PANTHER; PTHR43903:SF9; BILE SALT-ACTIVATED LIPASE; 1. DR PANTHER; PTHR43903; NEUROLIGIN; 1. DR Pfam; PF00135; COesterase; 1. 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; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome; KW Secreted; Serine esterase; Signal. FT SIGNAL <1..18 FT /evidence="ECO:0000269|PubMed:10220579" FT CHAIN 19..597 FT /note="Bile salt-activated lipase" FT /id="PRO_0000008630" FT REGION 553..591 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 553..572 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 212 FT /note="Acyl-ester intermediate" FT ACT_SITE 338 FT /note="Charge relay system" FT ACT_SITE 453 FT /note="Charge relay system" FT CARBOHYD 205 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 379 FT /note="N-linked (GlcNAc...) asparagine" FT DISULFID 82..98 FT DISULFID 264..275 FT CONFLICT 30 FT /note="F -> P (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 45 FT /note="I -> V (in Ref. 1; AAA56788)" FT /evidence="ECO:0000305" FT NON_TER 1 FT STRAND 23..26 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 34..37 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:1AQL" FT STRAND 44..55 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 70..74 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:1AKN" FT STRAND 90..94 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 100..107 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 115..121 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 126..129 FT /evidence="ECO:0007829|PDB:2BCE" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:1AKN" FT HELIX 141..143 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 146..152 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 155..159 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 164..168 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 180..195 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 196..199 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 201..211 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 213..223 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:2BCE" FT TURN 228..230 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 232..238 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 251..261 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 269..278 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 281..286 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 299..302 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 311..314 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 322..325 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 328..335 FT /evidence="ECO:0007829|PDB:2BCE" FT TURN 336..339 FT /evidence="ECO:0007829|PDB:1AKN" FT HELIX 340..346 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 348..350 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 353..355 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 359..369 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 370..373 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 374..386 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 387..389 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 395..410 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 412..425 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 431..436 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 443..445 FT /evidence="ECO:0007829|PDB:2BCE" FT TURN 453..456 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 457..460 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 463..466 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 468..470 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 473..492 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 497..500 FT /evidence="ECO:0007829|PDB:2BCE" FT TURN 511..513 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 515..521 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 525..527 FT /evidence="ECO:0007829|PDB:1AKN" FT STRAND 528..530 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 534..541 FT /evidence="ECO:0007829|PDB:2BCE" FT HELIX 543..546 FT /evidence="ECO:0007829|PDB:2BCE" FT STRAND 557..559 FT /evidence="ECO:0007829|PDB:1AKN" FT STRAND 593..595 FT /evidence="ECO:0007829|PDB:2BCE" SQ SEQUENCE 597 AA; 65162 MW; B23EB7AED90EBFD1 CRC64; LGASRLGPSP GCLAVASAAK LGSVYTEGGF VEGVNKKLSL FGDSIDIFKG IPFAAAPKAL EKPERHPGWQ GTLKAKSFKK RCLQATLTQD STYGNEDCLY LNIWVPQGRK EVSHDLPVMI WIYGGAFLMG ASQGANFLSN YLYDGEEIAT RGNVIVVTFN YRVGPLGFLS TGDSNLPGNY GLWDQHMAIA WVKRNIEAFG GDPDNITLFG ESAGGASVSL QTLSPYNKGL IKRAISQSGV GLCPWAIQQD PLFWAKRIAE KVGCPVDDTS KMAGCLKITD PRALTLAYKL PLGSTEYPKL HYLSFVPVID GDFIPDDPVN LYANAADVDY IAGTNDMDGH LFVGMDVPAI NSNKQDVTEE DFYKLVSGLT VTKGLRGANA TYEVYTEPWA QDSSQETRKK TMVDLETDIL FLIPTKIAVA QHKSHAKSAN TYTYLFSQPS RMPIYPKWMG ADHADDLQYV FGKPFATPLG YRAQDRTVSK AMIAYWTNFA RTGDPNTGHS TVPANWDPYT LEDDNYLEIN KQMDSNSMKL HLRTNYLQFW TQTYQALPTV TSAGASLLPP EDNSQASPVP PADNSGAPTE PSAGDSEVAQ MPVVIGF //