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Bile salt-activated lipase (BAL) (EC 3.1.1.13) (EC 3.1.1.3) (Bile salt-stimulated lipase) (BSSL) (Bucelipase) (Carboxyl ester lipase) (Cholesterol esterase) (Pancreatic lysophospholipase) (Sterol esterase)

 CEL_HUMAN               Reviewed;         753 AA.
P19835; Q16398; Q5T7U7; Q9UCH1; Q9UP41;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 3.
20-JUN-2018, entry version 182.
RecName: Full=Bile salt-activated lipase;
Short=BAL;
EC=3.1.1.13;
EC=3.1.1.3;
AltName: Full=Bile salt-stimulated lipase;
Short=BSSL;
AltName: Full=Bucelipase;
AltName: Full=Carboxyl ester lipase;
AltName: Full=Cholesterol esterase;
AltName: Full=Pancreatic lysophospholipase;
AltName: Full=Sterol esterase;
Flags: Precursor;
Name=CEL; Synonyms=BAL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND PARTIAL PROTEIN
SEQUENCE.
TISSUE=Mammary gland;
PubMed=1698625; DOI=10.1111/j.1432-1033.1990.tb19259.x;
Nilsson J., Blaeckberg L., Carlsson P., Enerbaeck S., Hernell O.,
Bjursell G.;
"cDNA cloning of human-milk bile-salt-stimulated lipase and evidence
for its identity to pancreatic carboxylic ester hydrolase.";
Eur. J. Biochem. 192:543-550(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Pancreas;
PubMed=2265692; DOI=10.1016/0014-5793(90)80525-N;
Hui D.Y., Kissel J.A.;
"Sequence identity between human pancreatic cholesterol esterase and
bile salt-stimulated milk lipase.";
FEBS Lett. 276:131-134(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND PROTEIN SEQUENCE OF
21-81; 122-126; 190-194; 275-279; 302-306; 445-449; 485-490; 500-507;
526-528 AND 531-538.
TISSUE=Mammary gland, and Milk;
PubMed=1988041; DOI=10.1021/bi00216a028;
Baba T., Downs D., Jackson K.W., Tang J., Wang C.-S.;
"Structure of human milk bile salt activated lipase.";
Biochemistry 30:500-510(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1639390; DOI=10.1016/0888-7543(92)90134-E;
Lidberg U., Nilsson J., Stroemberg K., Stenman G., Sahlin P.,
Enerbaeck S., Bjursell G.;
"Genomic organization, sequence analysis, and chromosomal localization
of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL)
gene.";
Genomics 13:630-640(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=7578248; DOI=10.1016/0167-4781(95)00141-3;
Roudani S., Miralles F., Margotat A., Escribano M.J., Lombardo D.;
"Bile salt-dependent lipase transcripts in human fetal tissues.";
Biochim. Biophys. Acta 1264:141-150(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9530636; DOI=10.1007/s003359900762;
Madeyski K., Lidberg U., Bjursell G., Nilsson J.;
"Structure and organization of the human carboxyl ester lipase
locus.";
Mamm. Genome 9:334-338(1998).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
PROTEIN SEQUENCE OF 53-76 AND 366-374, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-455.
TISSUE=Milk;
PubMed=8471055; DOI=10.1042/bj2910065;
Hui D.Y., Hayakawa K., Oizumi J.;
"Lipoamidase activity in normal and mutagenized pancreatic cholesterol
esterase (bile salt-stimulated lipase).";
Biochem. J. 291:65-69(1993).
[10]
PARTIAL PROTEIN SEQUENCE, AND ACTIVE SITE.
PubMed=1991511; DOI=10.1016/0014-5793(91)80114-I;
Christie D.L., Cleverly D.R., O'Connor C.J.O.;
"Human milk bile-salt stimulated lipase. Sequence similarity with rat
lysophospholipase and homology with the active site region of
cholinesterases.";
FEBS Lett. 278:190-194(1991).
[11]
GLYCOSYLATION AT THR-558; THR-569; THR-579; THR-607; THR-618; THR-629;
THR-640; THR-651; THR-662 AND THR-673.
PubMed=7654718; DOI=10.1021/bi00033a039;
Wang C.S., Dashti A., Jackson K.W., Yeh J.C., Cummings R.D., Tang J.;
"Isolation and characterization of human milk bile salt-activated
lipase C-tail fragment.";
Biochemistry 34:10639-10644(1995).
[12]
STRUCTURE OF N-LINKED CARBOHYDRATES.
PubMed=10024660; DOI=10.1093/glycob/9.3.227;
Mechref Y., Chen P., Novotny M.V.;
"Structural characterization of the N-linked oligosaccharides in bile
salt-stimulated lipase originated from human breast milk.";
Glycobiology 9:227-234(1999).
[13]
INTERACTION WITH CLC, AND TISSUE SPECIFICITY.
PubMed=11834744; DOI=10.1074/jbc.M200221200;
Ackerman S.J., Liu L., Kwatia M.A., Savage M.P., Leonidas D.D.,
Swaminathan G.J., Acharya K.R.;
"Charcot-Leyden crystal protein (galectin-10) is not a dual function
galectin with lysophospholipase activity but binds a lysophospholipase
inhibitor in a novel structural fashion.";
J. Biol. Chem. 277:14859-14868(2002).
[14]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-553.
PubMed=11045623; DOI=10.1110/ps.9.9.1783;
Terzyan S., Wang C.S., Downs D., Hunter B., Zhang X.C.;
"Crystal structure of the catalytic domain of human bile salt
activated lipase.";
Protein Sci. 9:1783-1790(2000).
[15]
INVOLVEMENT IN MODY8.
PubMed=16369531; DOI=10.1038/ng1708;
Raeder H., Johansson S., Holm P.I., Haldorsen I.S., Mas E., Sbarra V.,
Nermoen I., Eide S.A., Grevle L., Bjoerkhaug L., Sagen J.V.,
Aksnes L., Soevik O., Lombardo D., Molven A., Njoelstad P.R.;
"Mutations in the CEL VNTR cause a syndrome of diabetes and pancreatic
exocrine dysfunction.";
Nat. Genet. 38:54-62(2006).
-!- FUNCTION: Catalyzes fat and vitamin absorption. Acts in concert
with pancreatic lipase and colipase for the complete digestion of
dietary triglycerides.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate. {ECO:0000269|PubMed:8471055}.
-!- CATALYTIC ACTIVITY: A steryl ester + H(2)O = a sterol + a fatty
acid. {ECO:0000269|PubMed:8471055}.
-!- ENZYME REGULATION: Activated by bile salts containing a 7-hydroxyl
group.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=24 uM for lipoyl-4-aminobenzoate
{ECO:0000269|PubMed:8471055};
KM=15 uM for triacetin {ECO:0000269|PubMed:8471055};
Vmax=45.5 pmol/min/mg enzyme toward lipoyl-4-aminobenzoate
{ECO:0000269|PubMed:8471055};
Vmax=323 pmol/min/mg enzyme toward triacetin
{ECO:0000269|PubMed:8471055};
-!- SUBUNIT: Interacts with CLC. {ECO:0000269|PubMed:11834744}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P19835-1; Sequence=Displayed;
Name=Short;
IsoId=P19835-2; Sequence=VSP_001463;
-!- TISSUE SPECIFICITY: Mammary gland and pancreas. Expressed by
eosinophils. {ECO:0000269|PubMed:11834744}.
-!- DISEASE: Maturity-onset diabetes of the young 8 with exocrine
dysfunction (MODY8) [MIM:609812]: A form of diabetes that is
characterized by an autosomal dominant mode of inheritance, onset
in childhood or early adulthood (usually before 25 years of age),
a primary defect in insulin secretion and frequent insulin-
independence at the beginning of the disease.
{ECO:0000269|PubMed:16369531}. Note=The disease is caused by
mutations affecting the gene represented in this entry. The
disease can be caused by frameshift deletions in the variable
number of tandem repeats (VNTR)-containing exon 11 of the CEL gene
(PubMed:16369531). {ECO:0000269|PubMed:16369531}.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA51973.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAA52014.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAC26514.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA38325.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAI13412.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=EAW88033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X54457; CAA38325.1; ALT_INIT; mRNA.
EMBL; M85201; AAA52014.1; ALT_INIT; mRNA.
EMBL; M54994; AAA63211.1; -; mRNA.
EMBL; M94579; AAA51973.1; ALT_INIT; Genomic_DNA.
EMBL; S79774; AAB35488.2; -; mRNA.
EMBL; AF072711; AAC26514.1; ALT_INIT; Genomic_DNA.
EMBL; AL162417; CAI13412.1; ALT_INIT; Genomic_DNA.
EMBL; CH471090; EAW88033.1; ALT_INIT; Genomic_DNA.
PIR; S13586; S13586.
UniGene; Hs.533258; -.
PDB; 1F6W; X-ray; 2.30 A; A=21-553.
PDB; 1JMY; X-ray; 2.60 A; A=21-538.
PDBsum; 1F6W; -.
PDBsum; 1JMY; -.
ProteinModelPortal; P19835; -.
SMR; P19835; -.
IntAct; P19835; 1.
STRING; 9606.ENSP00000361151; -.
BindingDB; P19835; -.
ChEMBL; CHEMBL3219; -.
DrugBank; DB04348; Taurocholic Acid.
SwissLipids; SLP:000000874; -.
ESTHER; human-CEL; Cholesterol_esterase.
MEROPS; S09.985; -.
GlyConnect; 74; -.
iPTMnet; P19835; -.
PhosphoSitePlus; P19835; -.
UniCarbKB; P19835; -.
DMDM; 251757481; -.
PaxDb; P19835; -.
PeptideAtlas; P19835; -.
PRIDE; P19835; -.
ProteomicsDB; 53692; -.
ProteomicsDB; 53693; -. [P19835-2]
Ensembl; ENST00000351304; ENSP00000342217; ENSG00000170835.
DisGeNET; 1056; -.
GeneCards; CEL; -.
HGNC; HGNC:1848; CEL.
HPA; HPA008023; -.
HPA; HPA052701; -.
MalaCards; CEL; -.
MIM; 114840; gene.
MIM; 606391; phenotype.
MIM; 609812; phenotype.
neXtProt; NX_P19835; -.
Orphanet; 552; MODY.
PharmGKB; PA26391; -.
eggNOG; KOG1516; Eukaryota.
eggNOG; COG2272; LUCA.
HOGENOM; HOG000091866; -.
HOVERGEN; HBG008839; -.
InParanoid; P19835; -.
PhylomeDB; P19835; -.
TreeFam; TF315470; -.
Reactome; R-HSA-192456; Digestion of dietary lipid.
SABIO-RK; P19835; -.
ChiTaRS; CEL; human.
EvolutionaryTrace; P19835; -.
PRO; PR:P19835; -.
Proteomes; UP000005640; Unplaced.
CleanEx; HS_CEL; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0047372; F:acylglycerol lipase activity; TAS:Reactome.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
GO; GO:0003824; F:catalytic activity; TAS:UniProtKB.
GO; GO:0008201; F:heparin binding; NAS:UniProtKB.
GO; GO:0016787; F:hydrolase activity; TAS:UniProtKB.
GO; GO:0004771; F:sterol esterase activity; TAS:Reactome.
GO; GO:0004806; F:triglyceride lipase activity; NAS:UniProtKB.
GO; GO:0006707; P:cholesterol catabolic process; IDA:UniProtKB.
GO; GO:0009062; P:fatty acid catabolic process; NAS:UniProtKB.
GO; GO:0030299; P:intestinal cholesterol absorption; NAS:UniProtKB.
GO; GO:0044258; P:intestinal lipid catabolic process; NAS:UniProtKB.
GO; GO:0044241; P:lipid digestion; TAS:Reactome.
GO; GO:0006629; P:lipid metabolic process; NAS:UniProtKB.
GO; GO:0030157; P:pancreatic juice secretion; IDA:UniProtKB.
GO; GO:0018350; P:protein esterification; NAS:UniProtKB.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR033560; BAL.
InterPro; IPR002018; CarbesteraseB.
InterPro; IPR019826; Carboxylesterase_B_AS.
InterPro; IPR019819; Carboxylesterase_B_CS.
InterPro; IPR032059; Mucin-like.
PANTHER; PTHR43903:SF1; PTHR43903:SF1; 2.
Pfam; PF00135; COesterase; 1.
Pfam; PF16058; Mucin-like; 2.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Diabetes mellitus; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
Reference proteome; Repeat; Secreted; Serine esterase; Signal.
SIGNAL 1 20 {ECO:0000269|PubMed:1988041}.
CHAIN 21 753 Bile salt-activated lipase.
/FTId=PRO_0000008631.
REPEAT 559 569 1.
REPEAT 570 580 2.
REPEAT 581 591 3.
REPEAT 592 602 4.
REPEAT 603 613 5.
REPEAT 614 624 6.
REPEAT 625 635 7.
REPEAT 636 646 8.
REPEAT 647 657 9.
REPEAT 658 668 10.
REPEAT 669 679 11.
REPEAT 680 690 12.
REPEAT 691 701 13.
REPEAT 702 712 14.
REPEAT 713 723 15.
REPEAT 724 734 16.
REPEAT 735 745 17.
REGION 21 121 Heparin-binding.
REGION 559 745 17 X 11 AA tandem repeats, glycodomain,
O-linked (mucin type).
ACT_SITE 214 214 Acyl-ester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10039,
ECO:0000269|PubMed:1991511}.
ACT_SITE 340 340 Charge relay system.
{ECO:0000269|PubMed:1991511}.
ACT_SITE 455 455 Charge relay system.
{ECO:0000269|PubMed:1991511}.
CARBOHYD 207 207 N-linked (GlcNAc...) (complex)
asparagine.
/FTId=CAR_000141.
CARBOHYD 558 558 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7654718}.
CARBOHYD 569 569 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7654718}.
CARBOHYD 579 579 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7654718}.
CARBOHYD 607 607 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7654718}.
CARBOHYD 618 618 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7654718}.
CARBOHYD 629 629 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7654718}.
CARBOHYD 640 640 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7654718}.
CARBOHYD 651 651 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7654718}.
CARBOHYD 662 662 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7654718}.
CARBOHYD 673 673 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7654718}.
DISULFID 84 100
DISULFID 266 277
VAR_SEQ 430 495 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_001463.
MUTAGEN 455 455 H->Q: Abolishes lipase activity.
Decreases Vmax for esterase activity by
2.5-fold. {ECO:0000269|PubMed:8471055}.
CONFLICT 73 73 Missing (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 235 235 R -> A (in Ref. 5; AAB35488).
{ECO:0000305}.
CONFLICT 284 288 RALTL -> AAVTV (in Ref. 5; AAB35488).
{ECO:0000305}.
CONFLICT 313 313 G -> E (in Ref. 5; AAB35488).
{ECO:0000305}.
CONFLICT 403 403 T -> I (in Ref. 5; AAB35488).
{ECO:0000305}.
CONFLICT 481 481 S -> F (in Ref. 5; AAB35488).
{ECO:0000305}.
CONFLICT 689 689 A -> P (in Ref. 5; AAB35488).
{ECO:0000305}.
STRAND 25 28 {ECO:0000244|PDB:1F6W}.
STRAND 31 34 {ECO:0000244|PDB:1F6W}.
STRAND 36 39 {ECO:0000244|PDB:1F6W}.
STRAND 41 44 {ECO:0000244|PDB:1F6W}.
STRAND 46 54 {ECO:0000244|PDB:1F6W}.
STRAND 72 76 {ECO:0000244|PDB:1F6W}.
STRAND 84 87 {ECO:0000244|PDB:1F6W}.
STRAND 91 98 {ECO:0000244|PDB:1F6W}.
STRAND 102 109 {ECO:0000244|PDB:1F6W}.
STRAND 111 113 {ECO:0000244|PDB:1F6W}.
STRAND 117 124 {ECO:0000244|PDB:1F6W}.
TURN 128 130 {ECO:0000244|PDB:1F6W}.
STRAND 137 139 {ECO:0000244|PDB:1JMY}.
STRAND 142 145 {ECO:0000244|PDB:1JMY}.
HELIX 148 154 {ECO:0000244|PDB:1F6W}.
STRAND 157 161 {ECO:0000244|PDB:1F6W}.
HELIX 166 170 {ECO:0000244|PDB:1F6W}.
STRAND 174 178 {ECO:0000244|PDB:1JMY}.
HELIX 182 197 {ECO:0000244|PDB:1F6W}.
TURN 198 202 {ECO:0000244|PDB:1F6W}.
STRAND 203 213 {ECO:0000244|PDB:1F6W}.
HELIX 215 225 {ECO:0000244|PDB:1F6W}.
HELIX 227 229 {ECO:0000244|PDB:1F6W}.
TURN 230 232 {ECO:0000244|PDB:1F6W}.
STRAND 234 240 {ECO:0000244|PDB:1F6W}.
TURN 246 248 {ECO:0000244|PDB:1F6W}.
HELIX 253 264 {ECO:0000244|PDB:1F6W}.
HELIX 271 280 {ECO:0000244|PDB:1F6W}.
HELIX 283 288 {ECO:0000244|PDB:1F6W}.
HELIX 302 304 {ECO:0000244|PDB:1F6W}.
STRAND 313 316 {ECO:0000244|PDB:1F6W}.
HELIX 320 322 {ECO:0000244|PDB:1F6W}.
HELIX 324 327 {ECO:0000244|PDB:1F6W}.
STRAND 330 337 {ECO:0000244|PDB:1F6W}.
TURN 338 341 {ECO:0000244|PDB:1F6W}.
HELIX 342 348 {ECO:0000244|PDB:1F6W}.
HELIX 350 353 {ECO:0000244|PDB:1F6W}.
STRAND 355 357 {ECO:0000244|PDB:1JMY}.
HELIX 361 371 {ECO:0000244|PDB:1F6W}.
HELIX 376 388 {ECO:0000244|PDB:1F6W}.
TURN 398 401 {ECO:0000244|PDB:1F6W}.
HELIX 402 412 {ECO:0000244|PDB:1F6W}.
HELIX 414 425 {ECO:0000244|PDB:1F6W}.
STRAND 433 438 {ECO:0000244|PDB:1F6W}.
TURN 455 458 {ECO:0000244|PDB:1F6W}.
HELIX 459 462 {ECO:0000244|PDB:1F6W}.
HELIX 465 468 {ECO:0000244|PDB:1F6W}.
HELIX 470 472 {ECO:0000244|PDB:1F6W}.
HELIX 475 494 {ECO:0000244|PDB:1F6W}.
STRAND 499 502 {ECO:0000244|PDB:1F6W}.
TURN 513 515 {ECO:0000244|PDB:1F6W}.
STRAND 518 524 {ECO:0000244|PDB:1F6W}.
HELIX 527 529 {ECO:0000244|PDB:1F6W}.
HELIX 536 544 {ECO:0000244|PDB:1F6W}.
TURN 545 548 {ECO:0000244|PDB:1F6W}.
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


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