ID   CBG_PIG                 Reviewed;         406 AA.
AC   Q9GK37;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 81.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=Large white; TISSUE=Liver;
RX   PubMed=15087473; DOI=10.1210/me.2004-0005;
RA   Ousova O., Guyonnet-Duperat V., Iannuccelli N., Bidanel J.-P., Milan D.,
RA   Genet C., Llamas B., Yerle M., Gellin J., Chardon P., Emptoz-Bonneton A.,
RA   Pugeat M., Mormede P., Moisan M.-P.;
RT   "Corticosteroid binding globulin: a new target for cortisol-driven
RT   obesity.";
RL   Mol. Endocrinol. 18:1687-1696(2004).
CC   -!- FUNCTION: Major transport protein for glucocorticoids and progestins in
CC       the blood of almost all vertebrate species.
CC       {ECO:0000269|PubMed:15087473}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15087473}.
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; AF324155; AAG45431.1; -; mRNA.
DR   RefSeq; NP_998977.1; NM_213812.1.
DR   AlphaFoldDB; Q9GK37; -.
DR   SMR; Q9GK37; -.
DR   STRING; 9823.ENSSSCP00000002680; -.
DR   ChEMBL; CHEMBL3449; -.
DR   MEROPS; I04.954; -.
DR   PaxDb; Q9GK37; -.
DR   PeptideAtlas; Q9GK37; -.
DR   GeneID; 396736; -.
DR   KEGG; ssc:396736; -.
DR   CTD; 866; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; Q9GK37; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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: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   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..406
FT                   /note="Corticosteroid-binding globulin"
FT                   /id="PRO_5000058801"
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         394
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        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   406 AA;  45189 MW;  CC9CF4C881CED40E CRC64;
     MLLTLYACLL WLSTSGLWTS QAKDPDSDLS TRSRHRNLAP NNVDFAFALY KHLVASAPGK
     DVFLSPVSIS TALAMLSLGA SGYTREQLLQ GLGFNLTETP EAEIHQDFQH LHSLLKGSNI
     TSEMTMGNAL FLDRSLELLE SFSTGSKHYY GLEALAADFQ DWAGASRQIN EYIKNKTQGK
     IVDLFLEQDS SAMLILINYI FFKGTWTHSF PPESTREENF YVNETATVKV PMMFQSRAMK
     YLNDSLLPCQ LVQLEYTGNE TAFFILPVKG EMDTVIAGLS RDTIQRWSKS LIPSQVDLYV
     PKVSISGAYD LGSILGDMGI VDLLSHPTHF SGITQNALPK MSKVVHKAVL QFDEKGMEAA
     APTTRGRSLH AAPKPVTVHF NRPFIVMVFD HFTWSSLFLG KIVNLT