CBG_RAT
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 03-AUG-2022, entry version 152.
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 GlyGen; P31211; 5 sites.
DR PaxDb; P31211; -.
DR PRIDE; P31211; -.
DR Ensembl; ENSRNOT00000012500; ENSRNOP00000012500; ENSRNOG00000009438.
DR GeneID; 299270; -.
DR KEGG; rno:299270; -.
DR UCSC; RGD:1595901; rat.
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; 1124079at2759; -.
DR PhylomeDB; P31211; -.
DR TreeFam; TF343201; -.
DR Reactome; R-RNO-194002; Glucocorticoid biosynthesis.
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 tissues.
DR Genevisible; P31211; RN.
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 GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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 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
