CEL_BOVIN
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 03-AUG-2022, entry version 132.
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}.
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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 PaxDb; P30122; -.
DR PRIDE; P30122; -.
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:0004771; F:sterol esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 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
