ID   CBG_RAT                 Reviewed;         396 AA.
AC   P31211; Q5M822;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   24-JAN-2024, entry version 157.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=2710140; DOI=10.1210/mend-3-2-420;
RA   Smith C.L., Hammond G.L.;
RT   "Rat corticosteroid binding globulin: primary structure and messenger
RT   ribonucleic acid levels in the liver under different physiological
RT   conditions.";
RL   Mol. Endocrinol. 3:420-426(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 23-60.
RX   PubMed=3347061; DOI=10.1016/0022-4731(88)90268-3;
RA   Kato E.A., Hsu B.R.-S., Kuhn R.W.;
RT   "Comparative structural analyses of corticosteroid binding globulin.";
RL   J. Steroid Biochem. 29:213-220(1988).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 27-396 IN COMPLEX WITH CORTISOL,
RP   FUNCTION, AND MUTAGENESIS OF ARG-32; PRO-36; GLN-246; PHE-256 AND ASP-278.
RX   PubMed=17644521; DOI=10.1074/jbc.m705014200;
RA   Klieber M.A., Underhill C., Hammond G.L., Muller Y.A.;
RT   "Corticosteroid-binding globulin, a structural basis for steroid transport
RT   and proteinase-triggered release.";
RL   J. Biol. Chem. 282:29594-29603(2007).
CC   -!- FUNCTION: Major transport protein for glucocorticoids and progestins in
CC       the blood of almost all vertebrate species.
CC       {ECO:0000269|PubMed:17644521}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma.
CC       {ECO:0000269|PubMed:2710140}.
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; CH473982; EDL81783.1; -; Genomic_DNA.
DR   EMBL; BC088300; AAH88300.1; -; mRNA.
DR   PIR; A40066; A40066.
DR   RefSeq; NP_001009663.1; NM_001009663.1.
DR   PDB; 2V95; X-ray; 1.93 A; A=27-396.
DR   PDBsum; 2V95; -.
DR   AlphaFoldDB; P31211; -.
DR   SMR; P31211; -.
DR   STRING; 10116.ENSRNOP00000012500; -.
DR   MEROPS; I04.954; -.
DR   GlyCosmos; P31211; 5 sites, No reported glycans.
DR   GlyGen; P31211; 5 sites.
DR   PhosphoSitePlus; P31211; -.
DR   PaxDb; 10116-ENSRNOP00000012500; -.
DR   Ensembl; ENSRNOT00000012500.8; ENSRNOP00000012500.4; ENSRNOG00000009438.8.
DR   GeneID; 299270; -.
DR   KEGG; rno:299270; -.
DR   UCSC; RGD:1595901; rat.
DR   AGR; RGD:1595901; -.
DR   CTD; 866; -.
DR   RGD; 1595901; Serpina6.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000161611; -.
DR   HOGENOM; CLU_023330_2_1_1; -.
DR   InParanoid; P31211; -.
DR   OMA; HDSELPC; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; P31211; -.
DR   TreeFam; TF343201; -.
DR   Reactome; R-RNO-194002; Glucocorticoid biosynthesis.
DR   Reactome; R-RNO-9757110; Prednisone ADME.
DR   EvolutionaryTrace; P31211; -.
DR   PRO; PR:P31211; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Proteomes; UP000234681; Chromosome 6.
DR   Bgee; ENSRNOG00000009438; Expressed in liver and 11 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
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:0008211; P:glucocorticoid metabolic process; ISO:RGD.
DR   CDD; cd19554; serpinA6_CBG; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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:SF34; CORTICOSTEROID-BINDING GLOBULIN; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   PRINTS; PR00780; LEUSERPINII.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
DR   Genevisible; P31211; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Glycoprotein; Lipid-binding;
KW   Reference proteome; Secreted; Signal; Steroid-binding; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:3347061"
FT   CHAIN           23..396
FT                   /note="Corticosteroid-binding globulin"
FT                   /id="PRO_0000032432"
FT   BINDING         246
FT                   /ligand="cortisol"
FT                   /ligand_id="ChEBI:CHEBI:17650"
FT                   /evidence="ECO:0000269|PubMed:17644521"
FT   BINDING         278
FT                   /ligand="cortisol"
FT                   /ligand_id="ChEBI:CHEBI:17650"
FT                   /evidence="ECO:0000269|PubMed:17644521"
FT   BINDING         384
FT                   /ligand="cortisol"
FT                   /ligand_id="ChEBI:CHEBI:17650"
FT                   /evidence="ECO:0000269|PubMed:17644521"
FT   SITE            242
FT                   /note="Conserved cysteine within steroid binding domain"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         32
FT                   /note="R->A: Loss of corticosteroid binding."
FT                   /evidence="ECO:0000269|PubMed:17644521"
FT   MUTAGEN         36
FT                   /note="P->A: Increased affinity for corticosteroids."
FT                   /evidence="ECO:0000269|PubMed:17644521"
FT   MUTAGEN         246
FT                   /note="Q->A: Loss of corticosteroid binding."
FT                   /evidence="ECO:0000269|PubMed:17644521"
FT   MUTAGEN         256
FT                   /note="F->A: Loss of corticosteroid binding."
FT                   /evidence="ECO:0000269|PubMed:17644521"
FT   MUTAGEN         278
FT                   /note="D->A: Loss of corticosteroid binding."
FT                   /evidence="ECO:0000269|PubMed:17644521"
FT   CONFLICT        47..48
FT                   /note="QR -> EC (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="P -> C (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163..164
FT                   /note="NQ -> TR (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="I -> M (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="M -> V (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           35..52
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           62..72
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           80..85
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           94..108
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          114..125
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           133..142
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           155..169
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   TURN            170..172
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          186..197
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          209..214
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          220..237
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   TURN            238..241
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          242..260
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           265..271
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           274..283
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          285..294
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          296..303
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           304..306
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   HELIX           313..316
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          334..345
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          366..369
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          374..380
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   TURN            381..383
FT                   /evidence="ECO:0007829|PDB:2V95"
FT   STRAND          386..393
FT                   /evidence="ECO:0007829|PDB:2V95"
SQ   SEQUENCE   396 AA;  44671 MW;  A3D12AEC876D2BA2 CRC64;
     MSLALYTCLL WLCTSGLWTA QASTNESSNS HRGLAPTNVD FAFNLYQRLV ALNPDKNTLI
     SPVSISMALA MVSLGSAQTQ SLQSLGFNLT ETSEAEIHQS FQYLNYLLKQ SDTGLEMNMG
     NAMFLLQKLK LKDSFLADVK QYYESEALAI DFEDWTKASQ QINQHVKDKT QGKIEHVFSD
     LDSPASFILV NYIFLRGIWE LPFSPENTRE EDFYVNETST VKVPMMVQSG SIGYFRDSVF
     PCQLIQMDYV GNGTAFFILP DQGQMDTVIA ALSRDTIDRW GKLMTPRQVN LYIPKFSISD
     TYDLKDMLED LNIKDLLTNQ SDFSGNTKDV PLTLTMVHKA MLQLDEGNVL PNSTNGAPLH
     LRSEPLDIKF NKPFILLLFD KFTWSSLMMS QVVNPA
//