ID   CBG_PONAB               Reviewed;         405 AA.
AC   Q5R9E3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Corticosteroid-binding globulin;
DE            Short=CBG;
DE   AltName: Full=Serpin A6;
DE   AltName: Full=Transcortin;
DE   Flags: Precursor;
GN   Name=SERPINA6;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR859446; CAH91617.1; -; mRNA.
DR   RefSeq; NP_001125953.1; NM_001132481.1.
DR   AlphaFoldDB; Q5R9E3; -.
DR   SMR; Q5R9E3; -.
DR   STRING; 9601.ENSPPYP00000006937; -.
DR   MEROPS; I04.954; -.
DR   GeneID; 100172888; -.
DR   KEGG; pon:100172888; -.
DR   CTD; 866; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; Q5R9E3; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000001595; 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..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..405
FT                   /note="Corticosteroid-binding globulin"
FT                   /id="PRO_0000230781"
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                   /evidence="ECO:0000250"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   405 AA;  44995 MW;  07FDB129129F24F2 CRC64;
     MPLLLYTCLL WLSTSGLWTV QAMDPNTTYV NMSNHHRGLA SANVDFAFSL YKHLVALSPK
     KNIFISPVSI SMALAMLSLG TCGHTRAQLL QGLGFNLTGR SETEIHQGFQ HLHQLFAESD
     TSLEMTMGNA LFLDGSLELL ESFSADIKHY YESEVLAMNF QDWATASRQI NSYVKSKTQG
     KIADLLSGLD SPAILVLVNY IFFKGTWTQP FDLASTREEN FYVDETTVVK VPMMLQSSTI
     SYLHDSELPC QLVRLNYVGN GTVFFILPEK GKMNTVIAAL SRDTINRWSA GLTSSQVDLY
     IPKVTISGVY DLGDVLEEMG IADLFTNQAN FSRITQDAQL KSSKVVHKAV LQLNEEGVDT
     AGSTGVTLNL TSKPIILRFN QPFIIMIFDH FTWSSLFLAR VVNPA