CBG_URSAR
ID CBG_URSAR Reviewed; 405 AA.
AC B2D1U1;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 29.
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 Ursus arctos (Brown bear) (Grizzly bear).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9644;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Alsop D., Cattet M., Stenhouse G., Vijayan M.;
RT "Serum corticosteroid-binding globulins as indicators of chronic stress in
RT grizzly bears.";
RL Submitted (MAR-2008) 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 -!- 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; EU571738; ACB71035.1; -; mRNA.
DR AlphaFoldDB; B2D1U1; -.
DR SMR; B2D1U1; -.
DR MEROPS; I04.954; -.
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; Secreted; Signal; Steroid-binding; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..405
FT /note="Corticosteroid-binding globulin"
FT /id="PRO_0000343846"
FT BINDING 254
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000250"
FT SITE 250
FT /note="Conserved cysteine within steroid binding domain"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 405 AA; 45619 MW; 003BC2A8EB76DD56 CRC64;
MLLALCTCFL WLSTTDLWTV QAKDPDTDVS PRTPHRDLAP NNVDFAFILY RHLVASLPGK
NVFISPVSIS MALAMLSLGA RGYTRVQLLQ GLGFNLTKLS EAEIHQGFRH LRHLFEKESD
TMLEMAMGNA LFLDRNLELL ESFLADTKHY YEAEALAADF KDGAGASRQI NEYIKNKTQG
KIVDLVSKLD SSAMLILVNY IFFKGTWEHP FDPESTRQEN FYVNKTTVVR VPMMFQSGTI
KYLHDRVLPC QLVQLEYLGN GTVFFVLPEE GKMDTVIAAL SRDTIQRWSE SLTTGQVNLY
VPRVVISGAY DLRAILGDMG IADLFDKEAD FSGITREAPL KLSKVVHKAV LQLDEKGLEA
ATCPRVMLEG ASEPLTFRFD RPFVLMIFDH FSWSSLFLGK VVNPN