ID   CBG_BOVIN               Reviewed;         404 AA.
AC   E1BF81;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 62.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
CC   -!- FUNCTION: Major transport protein for glucocorticoids and progestins in
CC       the blood of almost all vertebrate species.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: Proteolytic cleavage leads to an important conformation change.
CC       This reduces the affinity for steroids (By similarity). {ECO:0000250}.
CC   -!- PTM: Glycosylation in position Asn-259 is needed for steroid binding.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; DAAA02053054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_010815611.1; XM_010817309.1.
DR   RefSeq; XP_010823257.1; XM_010824955.1.
DR   AlphaFoldDB; E1BF81; -.
DR   SMR; E1BF81; -.
DR   STRING; 9913.ENSBTAP00000023402; -.
DR   PaxDb; E1BF81; -.
DR   PRIDE; E1BF81; -.
DR   Ensembl; ENSBTAT00000023402; ENSBTAP00000023402; ENSBTAG00000039808.
DR   GeneID; 513746; -.
DR   KEGG; bta:513746; -.
DR   CTD; 866; -.
DR   VEuPathDB; HostDB:ENSBTAG00000039808; -.
DR   VGNC; VGNC:34468; SERPINA6.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000161611; -.
DR   HOGENOM; CLU_023330_2_1_1; -.
DR   InParanoid; E1BF81; -.
DR   OMA; HDSELPC; -.
DR   OrthoDB; 1124079at2759; -.
DR   TreeFam; TF343201; -.
DR   Reactome; R-BTA-194002; Glucocorticoid biosynthesis.
DR   Proteomes; UP000009136; Chromosome 21.
DR   Bgee; ENSBTAG00000039808; Expressed in liver and 11 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0005496; F:steroid binding; ISS: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   3: Inferred from homology;
KW   Glycoprotein; Lipid-binding; Reference proteome; Secreted; Signal;
KW   Steroid-binding; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..404
FT                   /note="Corticosteroid-binding globulin"
FT                   /id="PRO_0000419662"
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        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   404 AA;  45102 MW;  2C4B067E74C89823 CRC64;
     MLPTLYTCLL WLSTSGLWTV QAKGSDTDMS TRNPHRDLAP NNVDFAFTLY KHLVASAPGK
     NVFISPVSIS TALAMLSLGA RGYTREQLLQ GLGFNLTEMS EGEIHRAFRH LHHLLRESNT
     TLDMTMGNAL FLDHSLELLE SFSADTKHYY ELEALTTDFQ DWAGASRQIN EYIKNKTQGN
     IVDLFSESDS SATLILVNYI FFKGMWAHSF DLESTREENF HVNEATTVQV PMMFQSNTIK
     YLNDSVLPCQ LVQLDYTGNE TVFFVLPVKG KMDSVITALS RDTIQRWSKS LTMSQVDLYI
     PKISISGAYD LGGIMGDMGI ADLLSNRTHF SGITQEALPK VSKVVHKAAL QVDEKGLEAD
     APTRVSLSAA PGPLTLRFNR PFIIMIFDDF TWSSLFLGKV VNPT