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Cholesteryl ester transfer protein (Lipid transfer protein I)

 CETP_HUMAN              Reviewed;         493 AA.
P11597; Q13987; Q13988; Q53YZ1;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 2.
25-OCT-2017, entry version 181.
RecName: Full=Cholesteryl ester transfer protein {ECO:0000303|PubMed:3600759};
AltName: Full=Lipid transfer protein I {ECO:0000312|MIM:118470};
Flags: Precursor;
Name=CETP {ECO:0000312|HGNC:HGNC:1869};
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 1), PARTIAL PROTEIN SEQUENCE,
FUNCTION, TISSUE SPECIFICITY, AND VARIANT ILE-422.
PubMed=3600759; DOI=10.1038/327632a0;
Drayna D., Jarnagin A.S., McLean J., Henzel W., Kohr W., Fielding C.,
Lawn R.;
"Cloning and sequencing of human cholesteryl ester transfer protein
cDNA.";
Nature 327:632-634(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2334701; DOI=10.1021/bi00458a004;
Agellon L.B., Quinet E.M., Gillette T.G., Drayna D.T., Brown M.L.,
Tall A.R.;
"Organization of the human cholesteryl ester transfer protein gene.";
Biochemistry 29:1372-1376(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-422.
Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D.,
Toth E.J., Nickerson D.A.;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ILE-422.
TISSUE=Pancreas, and Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
PubMed=8943225; DOI=10.1074/jbc.271.50.31831;
Oliveira C.F.O., Chouinard R.A., Agellon L.B., Bruce C., Ma L.,
Walsh A., Breslow J.L., Tall A.R.;
"Human cholesteryl ester transfer protein gene proximal promoter
contains dietary cholesterol positive responsive elements and mediates
expression in small intestine and periphery while predominant liver
and spleen expression is controlled by 5'-distal sequences. Cis-acting
sequences mapped in transgenic mice.";
J. Biol. Chem. 271:31831-31838(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
PubMed=9332354; DOI=10.1016/S0378-1119(97)00247-3;
Williams S., Hayes L., Elsenboss L., Williams A., Andre C.,
Abramson R., Thompson J.F., Milos P.M.;
"Sequencing of the cholesteryl ester transfer protein 5' regulatory
region using artificial transposons.";
Gene 197:101-107(1997).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-493 (ISOFORM 2), AND VARIANT ILE-422.
TISSUE=Liver;
Dinchuk J.E., Hart J.T., Wirak D.O.;
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-257 AND ASN-358.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[9]
INVOLVEMENT IN HDLCQ10, AND POLYMORPHISM.
PubMed=17952847; DOI=10.1086/522497;
Spirin V., Schmidt S., Pertsemlidis A., Cooper R.S., Cohen J.C.,
Sunyaev S.R.;
"Common single-nucleotide polymorphisms act in concert to affect
plasma levels of high-density lipoprotein cholesterol.";
Am. J. Hum. Genet. 81:1298-1303(2007).
[10]
GLYCOSYLATION AT ASN-105.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24293641; DOI=10.1194/jlr.M043646;
Morton R.E., Izem L.;
"Cholesteryl ester transfer proteins from different species do not
have equivalent activities.";
J. Lipid Res. 55:258-265(2014).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-493 IN COMPLEX WITH LIPID,
FUNCTION, DISULFIDE BOND, AND MUTAGENESIS OF THR-155; VAL-215;
ARG-218; SER-247; PHE-282; PHE-287; PHE-309; LEU-313; TYR-392; LEU-399
AND VAL-433.
PubMed=17237796; DOI=10.1038/nsmb1197;
Qiu X., Mistry A., Ammirati M.J., Chrunyk B.A., Clark R.W., Cong Y.,
Culp J.S., Danley D.E., Freeman T.B., Geoghegan K.F., Griffor M.C.,
Hawrylik S.J., Hayward C.M., Hensley P., Hoth L.R., Karam G.A.,
Lira M.E., Lloyd D.B., McGrath K.M., Stutzman-Engwall K.J.,
Subashi A.K., Subashi T.A., Thompson J.F., Wang I.-K., Zhao H.,
Seddon A.P.;
"Crystal structure of cholesteryl ester transfer protein reveals a
long tunnel and four bound lipid molecules.";
Nat. Struct. Mol. Biol. 14:106-113(2007).
[13]
INVOLVEMENT IN HALP1.
PubMed=2215607; DOI=10.1056/NEJM199011013231803;
Inazu A., Brown M.L., Hesler C.B., Agellon L.B., Koizumi J.,
Takata K., Maruhama Y., Mabuchi H., Tall A.R.;
"Increased high-density lipoprotein levels caused by a common
cholesteryl-ester transfer protein gene mutation.";
N. Engl. J. Med. 323:1234-1238(1990).
[14]
VARIANT HALP1 GLY-459.
PubMed=8408659; DOI=10.1172/JCI116802;
Takahashi K., Jiang X.-C., Sakai N., Yamashita S., Hirano K., Bujo H.,
Yamazaki H., Kusunoki J., Miura T., Kussie P., Matsuzawa Y., Saito Y.,
Tall A.;
"A missense mutation in the cholesteryl ester transfer protein gene
with possible dominant effects on plasma high density lipoproteins.";
J. Clin. Invest. 92:2060-2064(1993).
[15]
VARIANTS SER-331; PRO-390; ILE-422 AND MET-486.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[16]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[17]
VARIANTS HALP1 PRO-168 AND CYS-299, AND CHARACTERIZATION OF VARIANTS
HALP1 PRO-168 AND CYS-299.
PubMed=12091484; DOI=10.1194/jlr.M200024-JLR200;
Nagano M., Yamashita S., Hirano K., Ito M., Maruyama T., Ishihara M.,
Sagehashi Y., Oka T., Kujiraoka T., Hattori H., Nakajima N.,
Egashira T., Kondo M., Sakai N., Matsuzawa Y.;
"Two novel missense mutations in the CETP gene in Japanese
hyperalphalipoproteinemic subjects: high-throughput assay by Invader
assay.";
J. Lipid Res. 43:1011-1018(2002).
[18]
VARIANTS GLY-15; MET-385; PRO-390; ILE-422 AND GLN-468.
PubMed=12966036; DOI=10.1093/hmg/ddg314;
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
Alvin G.B., Das K., Gilliam T.C.;
"Association of extreme blood lipid profile phenotypic variation with
11 reverse cholesterol transport genes and 10 non-genetic
cardiovascular disease risk factors.";
Hum. Mol. Genet. 12:2733-2743(2003).
-!- FUNCTION: Involved in the transfer of neutral lipids, including
cholesteryl ester and triglyceride, among lipoprotein particles.
Allows the net movement of cholesteryl ester from high density
lipoproteins/HDL to triglyceride-rich very low density
lipoproteins/VLDL, and the equimolar transport of triglyceride
from VLDL to HDL (PubMed:3600759, PubMed:24293641). Regulates the
reverse cholesterol transport, by which excess cholesterol is
removed from peripheral tissues and returned to the liver for
elimination (PubMed:17237796). {ECO:0000269|PubMed:24293641,
ECO:0000303|PubMed:17237796, ECO:0000305|PubMed:3600759}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space
{ECO:0000269|PubMed:24293641}. Note=Secreted in plasma.
{ECO:0000250|UniProtKB:P47896}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11597-1; Sequence=Displayed;
Name=2;
IsoId=P11597-2; Sequence=VSP_023645;
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- POLYMORPHISM: Genetic variations in CETP define the high density
lipoprotein cholesterol level quantitative trait locus 10
(HDLCQ10) [MIM:143470]. {ECO:0000269|PubMed:17952847}.
-!- DISEASE: Hyperalphalipoproteinemia 1 (HALP1) [MIM:143470]: A
condition characterized by high levels of high density lipoprotein
(HDL) and increased HDL cholesterol levels.
{ECO:0000269|PubMed:12091484, ECO:0000269|PubMed:2215607,
ECO:0000269|PubMed:8408659}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=CETP";
-!- WEB RESOURCE: Name=Wikipedia; Note=Cholesterylester transfer
protein entry;
URL="https://en.wikipedia.org/wiki/Cholesterylester_transfer_protein";
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EMBL; M30185; AAA51977.1; -; mRNA.
EMBL; M32998; AAA51978.1; -; Genomic_DNA.
EMBL; M32992; AAA51978.1; JOINED; Genomic_DNA.
EMBL; M32993; AAA51978.1; JOINED; Genomic_DNA.
EMBL; M32994; AAA51978.1; JOINED; Genomic_DNA.
EMBL; M32995; AAA51978.1; JOINED; Genomic_DNA.
EMBL; M32996; AAA51978.1; JOINED; Genomic_DNA.
EMBL; M32997; AAA51978.1; JOINED; Genomic_DNA.
EMBL; AY422211; AAR03500.1; -; Genomic_DNA.
EMBL; BC025739; AAH25739.1; -; mRNA.
EMBL; U71187; AAD14876.1; -; Genomic_DNA.
EMBL; AF027656; AAB86604.1; -; Genomic_DNA.
EMBL; M83573; AAB59388.1; -; mRNA.
CCDS; CCDS10772.1; -. [P11597-1]
CCDS; CCDS67032.1; -. [P11597-2]
PIR; A26941; A26941.
RefSeq; NP_000069.2; NM_000078.2. [P11597-1]
UniGene; Hs.89538; -.
PDB; 2OBD; X-ray; 2.10 A; A=18-493.
PDB; 4EWS; X-ray; 2.59 A; A=18-493.
PDB; 4F2A; X-ray; 3.11 A; A=18-493.
PDBsum; 2OBD; -.
PDBsum; 4EWS; -.
PDBsum; 4F2A; -.
ProteinModelPortal; P11597; -.
SMR; P11597; -.
BioGrid; 107498; 2.
IntAct; P11597; 3.
STRING; 9606.ENSP00000200676; -.
BindingDB; P11597; -.
ChEMBL; CHEMBL3572; -.
SwissLipids; SLP:000000472; -.
TCDB; 1.C.40.1.8; the bactericidal permeability increasing protein (bpip) family.
iPTMnet; P11597; -.
PhosphoSitePlus; P11597; -.
SwissPalm; P11597; -.
BioMuta; CETP; -.
DMDM; 71153497; -.
PaxDb; P11597; -.
PeptideAtlas; P11597; -.
PRIDE; P11597; -.
DNASU; 1071; -.
Ensembl; ENST00000200676; ENSP00000200676; ENSG00000087237. [P11597-1]
Ensembl; ENST00000379780; ENSP00000369106; ENSG00000087237. [P11597-2]
GeneID; 1071; -.
KEGG; hsa:1071; -.
UCSC; uc002eki.3; human. [P11597-1]
CTD; 1071; -.
DisGeNET; 1071; -.
EuPathDB; HostDB:ENSG00000087237.10; -.
GeneCards; CETP; -.
HGNC; HGNC:1869; CETP.
MalaCards; CETP; -.
MIM; 118470; gene.
MIM; 143470; phenotype.
neXtProt; NX_P11597; -.
OpenTargets; ENSG00000087237; -.
Orphanet; 79506; Cholesterol-ester transfer protein deficiency.
PharmGKB; PA108; -.
eggNOG; KOG4160; Eukaryota.
eggNOG; ENOG410Z88E; LUCA.
GeneTree; ENSGT00390000008226; -.
HOGENOM; HOG000111553; -.
HOVERGEN; HBG005310; -.
InParanoid; P11597; -.
KO; K16835; -.
OMA; MADFVQT; -.
OrthoDB; EOG091G08KX; -.
PhylomeDB; P11597; -.
TreeFam; TF333484; -.
Reactome; R-HSA-8964041; LDL remodeling.
Reactome; R-HSA-8964058; HDL remodeling.
SIGNOR; P11597; -.
EvolutionaryTrace; P11597; -.
GeneWiki; Cholesterylester_transfer_protein; -.
GenomeRNAi; 1071; -.
PRO; PR:P11597; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000087237; -.
CleanEx; HS_CETP; -.
ExpressionAtlas; P11597; baseline and differential.
Genevisible; P11597; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
GO; GO:0017127; F:cholesterol transporter activity; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
GO; GO:0005319; F:lipid transporter activity; IDA:BHF-UCL.
GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
GO; GO:0005548; F:phospholipid transporter activity; IDA:BHF-UCL.
GO; GO:0017129; F:triglyceride binding; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
GO; GO:0030301; P:cholesterol transport; IDA:UniProtKB.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:UniProtKB.
GO; GO:0055088; P:lipid homeostasis; IDA:BHF-UCL.
GO; GO:0006869; P:lipid transport; IDA:BHF-UCL.
GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:BHF-UCL.
GO; GO:0055091; P:phospholipid homeostasis; IDA:BHF-UCL.
GO; GO:0015914; P:phospholipid transport; IDA:BHF-UCL.
GO; GO:0010874; P:regulation of cholesterol efflux; IMP:BHF-UCL.
GO; GO:0043691; P:reverse cholesterol transport; IC:BHF-UCL.
GO; GO:0070328; P:triglyceride homeostasis; IDA:BHF-UCL.
GO; GO:0006641; P:triglyceride metabolic process; IDA:BHF-UCL.
GO; GO:0034197; P:triglyceride transport; IDA:UniProtKB.
GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:UniProtKB.
InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
InterPro; IPR032942; BPI/LBP/Plunc.
InterPro; IPR017130; Cholesteryl_ester_transfer.
InterPro; IPR001124; Lipid-bd_serum_glycop_C.
InterPro; IPR017954; Lipid-bd_serum_glycop_CS.
InterPro; IPR017942; Lipid-bd_serum_glycop_N.
PANTHER; PTHR10504; PTHR10504; 1.
PANTHER; PTHR10504:SF12; PTHR10504:SF12; 1.
Pfam; PF01273; LBP_BPI_CETP; 1.
Pfam; PF02886; LBP_BPI_CETP_C; 1.
PIRSF; PIRSF037185; Cholesteryl_ester_transf; 1.
SMART; SM00328; BPI1; 1.
SMART; SM00329; BPI2; 1.
SUPFAM; SSF55394; SSF55394; 2.
PROSITE; PS00400; LBP_BPI_CETP; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Atherosclerosis;
Cholesterol metabolism; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Lipid metabolism;
Lipid transport; Polymorphism; Reference proteome; Secreted; Signal;
Steroid metabolism; Sterol metabolism; Transport.
SIGNAL 1 17
CHAIN 18 493 Cholesteryl ester transfer protein.
/FTId=PRO_0000017155.
CARBOHYD 105 105 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000269|PubMed:19139490}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 358 358 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 160 201 {ECO:0000269|PubMed:17237796}.
VAR_SEQ 251 310 Missing (in isoform 2).
{ECO:0000303|Ref.7}.
/FTId=VSP_023645.
VARIANT 15 15 A -> G (in dbSNP:rs34065661).
{ECO:0000269|PubMed:12966036}.
/FTId=VAR_017018.
VARIANT 154 154 R -> W (in dbSNP:rs34716057).
/FTId=VAR_033098.
VARIANT 168 168 L -> P (in HALP1; reduced secretion into
plasma). {ECO:0000269|PubMed:12091484}.
/FTId=VAR_033099.
VARIANT 299 299 R -> C (in HALP1; reduced secretion into
plasma; dbSNP:rs142459781).
{ECO:0000269|PubMed:12091484}.
/FTId=VAR_033100.
VARIANT 331 331 G -> S (in dbSNP:rs5881).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013919.
VARIANT 385 385 V -> M (in dbSNP:rs34855278).
{ECO:0000269|PubMed:12966036}.
/FTId=VAR_017019.
VARIANT 390 390 A -> P (in dbSNP:rs5880).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:12966036}.
/FTId=VAR_013920.
VARIANT 422 422 V -> I (in dbSNP:rs5882).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3600759,
ECO:0000269|Ref.3, ECO:0000269|Ref.7}.
/FTId=VAR_013921.
VARIANT 455 455 V -> M (in dbSNP:rs2228667).
/FTId=VAR_031127.
VARIANT 459 459 D -> G (in HALP1; dbSNP:rs2303790).
{ECO:0000269|PubMed:8408659}.
/FTId=VAR_004172.
VARIANT 468 468 R -> Q (in dbSNP:rs1800777).
{ECO:0000269|PubMed:12966036}.
/FTId=VAR_013922.
VARIANT 486 486 V -> M (in dbSNP:rs5887).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013923.
MUTAGEN 155 155 T->Y: Reduces triglyceride transfer and
cholesteryl ester transfer 5-fold.
{ECO:0000269|PubMed:17237796}.
MUTAGEN 215 215 V->W: Reduces triglyceride transfer 10-
fold. No effect on cholesteryl ester
transfer. {ECO:0000269|PubMed:17237796}.
MUTAGEN 218 218 R->S: Reduces triglyceride transfer 10-
fold. Slight reduction of cholesteryl
ester transfer.
{ECO:0000269|PubMed:17237796}.
MUTAGEN 247 247 S->A: Reduces triglyceride transfer 5-
fold. Slight reduction of cholesteryl
ester transfer.
{ECO:0000269|PubMed:17237796}.
MUTAGEN 282 282 F->R: Not secreted.
{ECO:0000269|PubMed:17237796}.
MUTAGEN 287 287 F->R: Not secreted.
{ECO:0000269|PubMed:17237796}.
MUTAGEN 309 309 F->D: Not secreted.
{ECO:0000269|PubMed:17237796}.
MUTAGEN 313 313 L->Q: Reduces cholesteryl ester transfer
by 60%. {ECO:0000269|PubMed:17237796}.
MUTAGEN 392 392 Y->S: Not secreted.
{ECO:0000269|PubMed:17237796}.
MUTAGEN 399 399 L->W: Not secreted.
{ECO:0000269|PubMed:17237796}.
MUTAGEN 433 433 V->R: Reduces activity by 60%.
{ECO:0000269|PubMed:17237796}.
STRAND 27 33 {ECO:0000244|PDB:2OBD}.
HELIX 34 40 {ECO:0000244|PDB:2OBD}.
HELIX 41 43 {ECO:0000244|PDB:2OBD}.
HELIX 44 54 {ECO:0000244|PDB:2OBD}.
STRAND 60 66 {ECO:0000244|PDB:2OBD}.
TURN 67 69 {ECO:0000244|PDB:2OBD}.
STRAND 70 94 {ECO:0000244|PDB:2OBD}.
TURN 95 97 {ECO:0000244|PDB:2OBD}.
STRAND 98 120 {ECO:0000244|PDB:2OBD}.
HELIX 122 124 {ECO:0000244|PDB:2OBD}.
STRAND 128 149 {ECO:0000244|PDB:2OBD}.
STRAND 152 171 {ECO:0000244|PDB:2OBD}.
HELIX 172 174 {ECO:0000244|PDB:4EWS}.
HELIX 180 187 {ECO:0000244|PDB:2OBD}.
HELIX 189 222 {ECO:0000244|PDB:2OBD}.
STRAND 228 231 {ECO:0000244|PDB:2OBD}.
STRAND 234 236 {ECO:0000244|PDB:2OBD}.
STRAND 242 249 {ECO:0000244|PDB:2OBD}.
STRAND 252 255 {ECO:0000244|PDB:2OBD}.
HELIX 269 271 {ECO:0000244|PDB:2OBD}.
STRAND 274 283 {ECO:0000244|PDB:2OBD}.
HELIX 284 296 {ECO:0000244|PDB:2OBD}.
STRAND 300 304 {ECO:0000244|PDB:2OBD}.
HELIX 306 315 {ECO:0000244|PDB:2OBD}.
HELIX 323 325 {ECO:0000244|PDB:2OBD}.
HELIX 326 329 {ECO:0000244|PDB:2OBD}.
HELIX 333 335 {ECO:0000244|PDB:2OBD}.
STRAND 337 344 {ECO:0000244|PDB:2OBD}.
STRAND 347 351 {ECO:0000244|PDB:2OBD}.
STRAND 354 367 {ECO:0000244|PDB:2OBD}.
HELIX 372 374 {ECO:0000244|PDB:2OBD}.
STRAND 378 393 {ECO:0000244|PDB:2OBD}.
STRAND 396 416 {ECO:0000244|PDB:2OBD}.
HELIX 420 432 {ECO:0000244|PDB:2OBD}.
HELIX 434 451 {ECO:0000244|PDB:2OBD}.
TURN 452 454 {ECO:0000244|PDB:2OBD}.
HELIX 455 457 {ECO:0000244|PDB:2OBD}.
STRAND 458 468 {ECO:0000244|PDB:2OBD}.
STRAND 471 479 {ECO:0000244|PDB:2OBD}.
HELIX 482 490 {ECO:0000244|PDB:2OBD}.
SEQUENCE 493 AA; 54756 MW; CD7762766A9B062E CRC64;
MLAATVLTLA LLGNAHACSK GTSHEAGIVC RITKPALLVL NHETAKVIQT AFQRASYPDI
TGEKAMMLLG QVKYGLHNIQ ISHLSIASSQ VELVEAKSID VSIQNVSVVF KGTLKYGYTT
AWWLGIDQSI DFEIDSAIDL QINTQLTCDS GRVRTDAPDC YLSFHKLLLH LQGEREPGWI
KQLFTNFISF TLKLVLKGQI CKEINVISNI MADFVQTRAA SILSDGDIGV DISLTGDPVI
TASYLESHHK GHFIYKNVSE DLPLPTFSPT LLGDSRMLYF WFSERVFHSL AKVAFQDGRL
MLSLMGDEFK AVLETWGFNT NQEIFQEVVG GFPSQAQVTV HCLKMPKISC QNKGVVVNSS
VMVKFLFPRP DQQHSVAYTF EEDIVTTVQA SYSKKKLFLS LLDFQITPKT VSNLTESSSE
SVQSFLQSMI TAVGIPEVMS RLEVVFTALM NSKGVSLFDI INPEIITRDG FLLLQMDFGF
PEHLLVDFLQ SLS


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