CBG_HUMAN
ID CBG_HUMAN Reviewed; 405 AA.
AC P08185; A8K456; Q7Z2Q9;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Corticosteroid-binding globulin;
DE Short=CBG;
DE AltName: Full=Serpin A6;
DE AltName: Full=Transcortin;
DE Flags: Precursor;
GN Name=SERPINA6; Synonyms=CBG;
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].
RC TISSUE=Liver, and Lung;
RX PubMed=3299377; DOI=10.1073/pnas.84.15.5153;
RA Hammond G.L., Smith C.L., Goping I.S., Underhill D.A., Harley M.J.,
RA Reventos J., Musto N.A., Gunsalus G.L., Bardin C.W.;
RT "Primary structure of human corticosteroid binding globulin, deduced from
RT hepatic and pulmonary cDNAs, exhibits homology with serine protease
RT inhibitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5153-5157(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3386241; DOI=10.1016/0022-4731(88)90085-4;
RA Bardin C.W., Gunsalus G.L., Musto N.A., Cheng C.Y., Reventos J., Smith C.,
RA Underhill D.A., Hammond G.;
RT "Corticosteroid binding globulin, testosterone-estradiol binding globulin,
RT and androgen binding protein belong to protein families distinct from
RT steroid receptors.";
RL J. Steroid Biochem. 30:131-139(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-246.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 23-30.
RX PubMed=3347061; DOI=10.1016/0022-4731(88)90268-3;
RA Kato E.A., Hsu B.R.-S., Kuhn R.W.;
RT "Comparative structural analyses of corticosteroid binding globulin.";
RL J. Steroid Biochem. 29:213-220(1988).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-31; ASN-96; ASN-330 AND
RP ASN-369.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96 AND ASN-330.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 33-405 IN COMPLEX WITH CORTISOL,
RP FUNCTION, AND DOMAIN.
RX PubMed=18513745; DOI=10.1016/j.jmb.2008.05.012;
RA Zhou A., Wei Z., Stanley P.L., Read R.J., Stein P.E., Carrell R.W.;
RT "The S-to-R transition of corticosteroid-binding globulin and the mechanism
RT of hormone release.";
RL J. Mol. Biol. 380:244-251(2008).
RN [11]
RP VARIANT CBG DEFICIENCY HIS-115.
RX PubMed=1504007; DOI=10.1016/0960-0760(92)90107-t;
RA Smith C.L., Power S.G.A., Hammond G.L.;
RT "A Leu-->His substitution at residue 93 in human corticosteroid binding
RT globulin results in reduced affinity for cortisol.";
RL J. Steroid Biochem. Mol. Biol. 42:671-676(1992).
RN [12]
RP VARIANT CBG DEFICIENCY HIS-115.
RX PubMed=8212073; DOI=10.1016/0039-128x(93)90072-u;
RA van Baelen H., Power S.G.A., Hammond G.L.;
RT "Decreased cortisol-binding affinity of transcortin Leuven is associated
RT with an amino acid substitution at residue-93.";
RL Steroids 58:275-277(1993).
RN [13]
RP VARIANT CBG DEFICIENCY ASN-389.
RX PubMed=10634411; DOI=10.1210/jcem.85.1.6315;
RA Emptoz-Bonneton A., Cousin P., Seguchi K., Avvakumov G.V., Bully C.,
RA Hammond G.L., Pugeat M.;
RT "Novel human corticosteroid-binding globulin variant with low cortisol-
RT binding affinity.";
RL J. Clin. Endocrinol. Metab. 85:361-367(2000).
RN [14]
RP VARIANT CBG DEFICIENCY ASN-389.
RX PubMed=17245537; DOI=10.1007/s00702-006-0620-5;
RA Buss C., Schuelter U., Hesse J., Moser D., Phillips D.I., Hellhammer D.,
RA Meyer J.;
RT "Haploinsufficiency of the SERPINA6 gene is associated with severe muscle
RT fatigue: A de novo mutation in corticosteroid-binding globulin
RT deficiency.";
RL J. Neural Transm. 114:563-569(2007).
CC -!- FUNCTION: Major transport protein for glucocorticoids and progestins in
CC the blood of almost all vertebrate species.
CC {ECO:0000269|PubMed:18513745}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma; synthesized in liver. Has also been
CC identified in a number of glycocorticoid responsive cells.
CC -!- DOMAIN: Proteolytic cleavage leads to an important conformation change.
CC This reduces the affinity for steroids. {ECO:0000269|PubMed:18513745}.
CC -!- PTM: N-glycosylated; binds 5 oligosaccharide chains.
CC -!- PTM: Glycosylation in position Asn-260 is needed for steroid binding.
CC -!- DISEASE: Corticosteroid-binding globulin deficiency (CBG deficiency)
CC [MIM:611489]: Extremely rare hereditary disorder characterized by
CC reduced corticosteroid-binding capacity with normal or low plasma
CC corticosteroid-binding globulin concentration, and normal or low basal
CC cortisol levels associated with hypo/hypertension and muscle fatigue.
CC {ECO:0000269|PubMed:10634411, ECO:0000269|PubMed:1504007,
CC ECO:0000269|PubMed:17245537, ECO:0000269|PubMed:8212073}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Transcortin entry;
CC URL="https://en.wikipedia.org/wiki/Transcortin";
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DR EMBL; J02943; AAB59523.1; -; mRNA.
DR EMBL; AK290821; BAF83510.1; -; mRNA.
DR EMBL; CH471061; EAW81568.1; -; Genomic_DNA.
DR EMBL; BC056259; AAH56259.1; -; mRNA.
DR EMBL; BC058021; AAH58021.1; -; mRNA.
DR CCDS; CCDS9924.1; -.
DR PIR; A28321; A28321.
DR RefSeq; NP_001747.2; NM_001756.3.
DR PDB; 2VDX; X-ray; 1.84 A; A/B=33-357, A/B=372-405.
DR PDB; 2VDY; X-ray; 2.30 A; A/B=33-405.
DR PDB; 4BB2; X-ray; 2.48 A; A=33-371, B=372-405.
DR PDB; 4C41; X-ray; 1.80 A; A=33-405.
DR PDB; 4C49; X-ray; 2.70 A; A/B/C/D=33-405.
DR PDBsum; 2VDX; -.
DR PDBsum; 2VDY; -.
DR PDBsum; 4BB2; -.
DR PDBsum; 4C41; -.
DR PDBsum; 4C49; -.
DR AlphaFoldDB; P08185; -.
DR SMR; P08185; -.
DR BioGRID; 107314; 13.
DR IntAct; P08185; 3.
DR STRING; 9606.ENSP00000342850; -.
DR BindingDB; P08185; -.
DR ChEMBL; CHEMBL2421; -.
DR DrugBank; DB00240; Alclometasone.
DR DrugBank; DB00394; Beclomethasone dipropionate.
DR DrugBank; DB00443; Betamethasone.
DR DrugBank; DB14669; Betamethasone phosphate.
DR DrugBank; DB01222; Budesonide.
DR DrugBank; DB01410; Ciclesonide.
DR DrugBank; DB01013; Clobetasol propionate.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01380; Cortisone acetate.
DR DrugBank; DB05688; CRx-119.
DR DrugBank; DB00687; Fludrocortisone.
DR DrugBank; DB00663; Flumethasone.
DR DrugBank; DB00180; Flunisolide.
DR DrugBank; DB00591; Fluocinolone acetonide.
DR DrugBank; DB01047; Fluocinonide.
DR DrugBank; DB00324; Fluorometholone.
DR DrugBank; DB00846; Flurandrenolide.
DR DrugBank; DB13867; Fluticasone.
DR DrugBank; DB08906; Fluticasone furoate.
DR DrugBank; DB00588; Fluticasone propionate.
DR DrugBank; DB00741; Hydrocortisone.
DR DrugBank; DB14538; Hydrocortisone aceponate.
DR DrugBank; DB14539; Hydrocortisone acetate.
DR DrugBank; DB14540; Hydrocortisone butyrate.
DR DrugBank; DB14541; Hydrocortisone cypionate.
DR DrugBank; DB14542; Hydrocortisone phosphate.
DR DrugBank; DB14543; Hydrocortisone probutate.
DR DrugBank; DB14544; Hydrocortisone valerate.
DR DrugBank; DB09124; Medrogestone.
DR DrugBank; DB00253; Medrysone.
DR DrugBank; DB00648; Mitotane.
DR DrugBank; DB01384; Paramethasone.
DR DrugBank; DB00860; Prednisolone.
DR DrugBank; DB15566; Prednisolone acetate.
DR DrugBank; DB14631; Prednisolone phosphate.
DR DrugBank; DB00635; Prednisone.
DR DrugBank; DB00896; Rimexolone.
DR DrugBank; DB00620; Triamcinolone.
DR DrugBank; DB00596; Ulobetasol.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR DrugCentral; P08185; -.
DR MEROPS; I04.954; -.
DR GlyConnect; 788; 20 N-Linked glycans (5 sites).
DR GlyGen; P08185; 7 sites, 32 N-linked glycans (5 sites), 2 O-linked glycans (1 site).
DR iPTMnet; P08185; -.
DR PhosphoSitePlus; P08185; -.
DR BioMuta; SERPINA6; -.
DR DMDM; 115851; -.
DR CPTAC; CPTAC-717; -.
DR CPTAC; non-CPTAC-2661; -.
DR CPTAC; non-CPTAC-2662; -.
DR jPOST; P08185; -.
DR MassIVE; P08185; -.
DR MaxQB; P08185; -.
DR PaxDb; P08185; -.
DR PeptideAtlas; P08185; -.
DR PRIDE; P08185; -.
DR ProteomicsDB; 52081; -.
DR ABCD; P08185; 1 sequenced antibody.
DR Antibodypedia; 59; 525 antibodies from 40 providers.
DR CPTC; P08185; 1 antibody.
DR DNASU; 866; -.
DR Ensembl; ENST00000341584.4; ENSP00000342850.3; ENSG00000170099.6.
DR Ensembl; ENST00000621384.2; ENSP00000484501.1; ENSG00000277405.2.
DR GeneID; 866; -.
DR KEGG; hsa:866; -.
DR MANE-Select; ENST00000341584.4; ENSP00000342850.3; NM_001756.4; NP_001747.3.
DR UCSC; uc001ycv.4; human.
DR CTD; 866; -.
DR DisGeNET; 866; -.
DR GeneCards; SERPINA6; -.
DR HGNC; HGNC:1540; SERPINA6.
DR HPA; ENSG00000170099; Tissue enriched (liver).
DR MalaCards; SERPINA6; -.
DR MIM; 122500; gene.
DR MIM; 611489; phenotype.
DR neXtProt; NX_P08185; -.
DR OpenTargets; ENSG00000170099; -.
DR Orphanet; 199247; Corticosteroid-binding globulin deficiency.
DR PharmGKB; PA35033; -.
DR VEuPathDB; HostDB:ENSG00000170099; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000161611; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; P08185; -.
DR OMA; HDSELPC; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P08185; -.
DR TreeFam; TF343201; -.
DR PathwayCommons; P08185; -.
DR Reactome; R-HSA-194002; Glucocorticoid biosynthesis.
DR SignaLink; P08185; -.
DR BioGRID-ORCS; 866; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; SERPINA6; human.
DR EvolutionaryTrace; P08185; -.
DR GeneWiki; Transcortin; -.
DR GenomeRNAi; 866; -.
DR Pharos; P08185; Tchem.
DR PRO; PR:P08185; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P08185; protein.
DR Bgee; ENSG00000170099; Expressed in liver and 46 other tissues.
DR ExpressionAtlas; P08185; baseline and differential.
DR Genevisible; P08185; HS.
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:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0005496; F:steroid binding; IDA:UniProtKB.
DR GO; GO:0008211; P:glucocorticoid metabolic process; IEA:Ensembl.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disease variant; Glycoprotein;
KW Lipid-binding; Reference proteome; Secreted; Signal; Steroid-binding;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:3347061"
FT CHAIN 23..405
FT /note="Corticosteroid-binding globulin"
FT /id="PRO_0000032429"
FT BINDING 254
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000269|PubMed:18513745,
FT ECO:0007744|PDB:2VDY"
FT BINDING 286
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000269|PubMed:18513745,
FT ECO:0007744|PDB:2VDY"
FT BINDING 390
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000269|PubMed:18513745,
FT ECO:0007744|PDB:2VDY"
FT BINDING 393
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT SITE 250
FT /note="Conserved cysteine within steroid binding domain"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT VARIANT 115
FT /note="L -> H (in CBG deficiency; Leuven; decreased
FT cortisol-binding affinity; dbSNP:rs113418909)"
FT /evidence="ECO:0000269|PubMed:1504007,
FT ECO:0000269|PubMed:8212073"
FT /id="VAR_007111"
FT VARIANT 246
FT /note="S -> A (in dbSNP:rs2228541)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024350"
FT VARIANT 389
FT /note="D -> N (in CBG deficiency; Lyon; decreased cortisol-
FT binding affinity; dbSNP:rs28929488)"
FT /evidence="ECO:0000269|PubMed:10634411,
FT ECO:0000269|PubMed:17245537"
FT /id="VAR_016223"
FT HELIX 39..57
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2VDX"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4C41"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:4C41"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:4C41"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4C41"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:4C41"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:4C49"
FT STRAND 123..134
FT /evidence="ECO:0007829|PDB:4C41"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:4C41"
FT HELIX 163..177
FT /evidence="ECO:0007829|PDB:4C41"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4BB2"
FT STRAND 194..209
FT /evidence="ECO:0007829|PDB:4C41"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 227..244
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 246..257
FT /evidence="ECO:0007829|PDB:4C41"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:4C41"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:4C41"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 293..302
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:4C41"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:4C41"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4C41"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 340..353
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 355..370
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:4C41"
FT TURN 390..393
FT /evidence="ECO:0007829|PDB:4C41"
FT STRAND 394..402
FT /evidence="ECO:0007829|PDB:4C41"
SQ SEQUENCE 405 AA; 45141 MW; F0E36EFC3B3C08A1 CRC64;
MPLLLYTCLL WLPTSGLWTV QAMDPNAAYV NMSNHHRGLA SANVDFAFSL YKHLVALSPK
KNIFISPVSI SMALAMLSLG TCGHTRAQLL QGLGFNLTER SETEIHQGFQ HLHQLFAKSD
TSLEMTMGNA LFLDGSLELL ESFSADIKHY YESEVLAMNF QDWATASRQI NSYVKNKTQG
KIVDLFSGLD SPAILVLVNY IFFKGTWTQP FDLASTREEN FYVDETTVVK VPMMLQSSTI
SYLHDSELPC QLVQMNYVGN GTVFFILPDK GKMNTVIAAL SRDTINRWSA GLTSSQVDLY
IPKVTISGVY DLGDVLEEMG IADLFTNQAN FSRITQDAQL KSSKVVHKAV LQLNEEGVDT
AGSTGVTLNL TSKPIILRFN QPFIIMIFDH FTWSSLFLAR VMNPV
