ID   CBG_SHEEP               Reviewed;         430 AA.
AC   P49920;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8477651; DOI=10.1210/endo.132.5.8477651;
RA   Berdusco E.T., Hammond G.L., Jacobs R.A., Grolla A., Akagi K., Langlois D.,
RA   Challis J.R.;
RT   "Glucocorticoid-induced increase in plasma corticosteroid-binding globulin
RT   levels in fetal sheep is associated with increased biosynthesis and
RT   alterations in glycosylation.";
RL   Endocrinology 132:2001-2008(1993).
CC   -!- FUNCTION: Major transport protein for glucocorticoids and progestins in
CC       the blood of almost all vertebrate species.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma.
CC   -!- DOMAIN: Proteolytic cleavage leads to an important conformation change.
CC       This reduces the affinity for steroids (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; X73615; CAA52000.1; -; mRNA.
DR   AlphaFoldDB; P49920; -.
DR   SMR; P49920; -.
DR   STRING; 9940.ENSOARP00000015907; -.
DR   MEROPS; I04.954; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Glycoprotein; Lipid-binding; Reference proteome; Secreted; Signal;
KW   Steroid-binding; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..430
FT                   /note="Corticosteroid-binding globulin"
FT                   /id="PRO_0000032434"
FT   BINDING         253
FT                   /ligand="cortisol"
FT                   /ligand_id="ChEBI:CHEBI:17650"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="cortisol"
FT                   /ligand_id="ChEBI:CHEBI:17650"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /ligand="cortisol"
FT                   /ligand_id="ChEBI:CHEBI:17650"
FT                   /evidence="ECO:0000250"
FT   SITE            249
FT                   /note="Conserved cysteine within steroid binding domain"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   430 AA;  48056 MW;  7E39DE8A2341E5EB CRC64;
     MLLTLYTCLL WLSTSGLWTI QAKGTDTDVS TRNPHRDLAP NNVDFAFTLY KHLVASAPGK
     NVFISPVSIS MALAMLSLGA RGYTREQLLQ GLGFSLVEMS EAEIHQAFRH LHHLLRESNT
     TLEMTMGNAL FLDHSLELLE SFSADTKHYY ELEALTTDFQ DWAGASRQIN EYIKNKTQGK
     IVDLFSESDS SAMFILVNYI FFKGMWVHSF DLESTREENF YVNEATTVWV PMMFQSNTIK
     YLNDSVLPCQ LVQLDYTGNE TVFFVLPVKG KMDSVITALS RDTIQRWSKS LTMSQVDLYI
     PKISISGAYD LGGIMGDMGI ADLLSNRTHF SGITQEALPK VSKVVHKAAL QVDEKGLEAA
     APTRVSVTAA PGPLTLRFNR PFIIMIFDDF TWSSLFLGKV VNPTEGALPG AKLRLTRAPR
     AHRKGWEGSP