CBG_MESAU
ID CBG_MESAU Reviewed; 404 AA.
AC Q60543;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Park C.G., Leavitt W.W.;
RT "Alternative signal peptide cleavage of corticosteroid binding globulin.";
RL Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Major transport protein for glucocorticoids and progestins in
CC the blood of almost all vertebrate species. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; M74776; AAA37065.1; -; mRNA.
DR PIR; A60577; A60577.
DR RefSeq; NP_001268882.1; NM_001281953.1.
DR AlphaFoldDB; Q60543; -.
DR SMR; Q60543; -.
DR STRING; 10036.XP_005068330.1; -.
DR MEROPS; I04.954; -.
DR GeneID; 101838201; -.
DR CTD; 866; -.
DR eggNOG; KOG2392; Eukaryota.
DR Proteomes; UP000189706; 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..30
FT /evidence="ECO:0000250"
FT CHAIN 31..404
FT /note="Corticosteroid-binding globulin"
FT /id="PRO_0000032430"
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 /evidence="ECO:0000250"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
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 404 AA; 45900 MW; 1D20F4DF92359B2F CRC64;
MAWSTRTMMS LALYTCFLWL LTSGLKTVQS LHDSHRGLAP TNVDFAFNMY RHLSTLDPHK
NILISPVSVS MALAMMSLVA VGSKKNQFFQ DVGFNLTEIS KEEIYQSFEK LSHLLSKADS
SLEMRMGNTM FLDQSLNMRD SFLTDIEHYH ESEALTTDFK DGADAREHIN RHVETKTQGE
ITHVFSDQDS PAPLTLVNYN VLKGMWELPI SPENTRDEDF HVSENSTVRV PMMFQSGVIG
YLHDSEIPCQ LVQMQYLKNG TTFFILPDEG QMDAVTAALH RDTVERWDKL LTKRLVNLYI
PRVYMSGTYN LEDVLEGMGI TGLFTNQTDF LDISQDPPQK ASKIVHKVML QLDEKDEPPV
TTTEAPPQTT SEPLTLTFNK PFIIMMFDSF TWSSLLLGKI MNPA
