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   24-JAN-2024, entry version 214.
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; 14.
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   GlyCosmos; P08185; 7 sites, 33 glycans.
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; 9606-ENSP00000342850; -.
DR   PeptideAtlas; P08185; -.
DR   ProteomicsDB; 52081; -.
DR   ABCD; P08185; 1 sequenced antibody.
DR   Antibodypedia; 59; 555 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   AGR; HGNC:1540; -.
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; 3218836at2759; -.
DR   PhylomeDB; P08185; -.
DR   TreeFam; TF343201; -.
DR   PathwayCommons; P08185; -.
DR   Reactome; R-HSA-194002; Glucocorticoid biosynthesis.
DR   Reactome; R-HSA-9757110; Prednisone ADME.
DR   SignaLink; P08185; -.
DR   BioGRID-ORCS; 866; 9 hits in 1148 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 cell types or tissues.
DR   ExpressionAtlas; P08185; baseline and differential.
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   CDD; cd19554; serpinA6_CBG; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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:SF34; CORTICOSTEROID-BINDING GLOBULIN; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   PRINTS; PR00780; LEUSERPINII.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
DR   Genevisible; P08185; HS.
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
FT                   cortisol-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
//