CBG_SAISC
ID CBG_SAISC Reviewed; 406 AA.
AC P50451;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Saimiri sciureus (Common squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=9521;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8299584; DOI=10.1210/endo.134.2.8299584;
RA Hammond G.L., Smith C.L., Lahteenmaki P., Grolla A., Warmels-Rodenhiser S.,
RA Hodgert H., Murai J.T., Siiteri P.K.;
RT "Squirrel monkey corticosteroid-binding globulin: primary structure and
RT comparison with the human protein.";
RL Endocrinology 134:891-898(1994).
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; S68757; AAC60614.1; -; mRNA.
DR PIR; I53281; I53281.
DR AlphaFoldDB; P50451; -.
DR SMR; P50451; -.
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..406
FT /note="Corticosteroid-binding globulin"
FT /id="PRO_0000032433"
FT BINDING 255
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000250"
FT BINDING 287
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 251
FT /note="Conserved cysteine within steroid binding domain"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 406 AA; 45358 MW; F5D8527AE5703728 CRC64;
MPLLLYTCLL WLLSSGLWTV QAMDPNAAYM NTSRHHRVLA SVNADFAFSL YKHLVALSPK
KNVFISPVSI SMALAMLSLG TCGHTRAQLL HGLGFNLTEK SEAEIHQSFQ HLHQLLAESD
SSLEMTLGNA LFLDGSLELL ESFSADIKHY YESEVLTLNF QDWATTASRQ INGYVKSKTQ
GKIDDLFSGL NSPAVLILIN YIFFKGTWKQ PFDLASTREE NFYVDETTVV KVPMMFQSGT
IRYLHDSELP CQLVQLNYAG NGTVFFILPE KGKMNIVITA LSRNTIDRWS AGLTRSQVDL
YIPKVTISGA YDFGGVLEDM GIADLFTNHA NFSRITQDAQ LKLSKVFHKA VLQLSEEGVN
TTGSTGVTLN PMSKPIIMRF NQPFLIMVFD HFTWSSLFLG RVVNPA
