CBG_MOUSE
ID CBG_MOUSE Reviewed; 397 AA.
AC Q06770;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7916682; DOI=10.1210/endo.132.2.7916682;
RA Scrocchi L.A., Orava M., Smith C.L., Han V.K.M., Hammond G.L.;
RT "Spatial and temporal distribution of corticosteroid-binding globulin and
RT its messenger ribonucleic acid in embryonic and fetal mice.";
RL Endocrinology 132:903-909(1993).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-89; ASN-217 AND ASN-232.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-89.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; X70533; CAA49934.1; -; mRNA.
DR CCDS; CCDS26135.1; -.
DR PIR; S33415; S33415.
DR RefSeq; NP_031644.1; NM_007618.3.
DR AlphaFoldDB; Q06770; -.
DR SMR; Q06770; -.
DR STRING; 10090.ENSMUSP00000044033; -.
DR MEROPS; I04.954; -.
DR GlyConnect; 2236; 1 N-Linked glycan (1 site).
DR GlyGen; Q06770; 6 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q06770; -.
DR PhosphoSitePlus; Q06770; -.
DR CPTAC; non-CPTAC-3374; -.
DR CPTAC; non-CPTAC-5584; -.
DR MaxQB; Q06770; -.
DR PaxDb; Q06770; -.
DR PeptideAtlas; Q06770; -.
DR PRIDE; Q06770; -.
DR ProteomicsDB; 283689; -.
DR Antibodypedia; 59; 525 antibodies from 40 providers.
DR DNASU; 12401; -.
DR Ensembl; ENSMUST00000044159; ENSMUSP00000044033; ENSMUSG00000060807.
DR GeneID; 12401; -.
DR KEGG; mmu:12401; -.
DR UCSC; uc007owa.1; mouse.
DR CTD; 866; -.
DR MGI; MGI:88278; Serpina6.
DR VEuPathDB; HostDB:ENSMUSG00000060807; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000161611; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; Q06770; -.
DR OMA; HDSELPC; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q06770; -.
DR TreeFam; TF343201; -.
DR Reactome; R-MMU-194002; Glucocorticoid biosynthesis.
DR BioGRID-ORCS; 12401; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Serpina6; mouse.
DR PRO; PR:Q06770; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q06770; protein.
DR Bgee; ENSMUSG00000060807; Expressed in dorsal pancreas and 51 other tissues.
DR ExpressionAtlas; Q06770; baseline and differential.
DR Genevisible; Q06770; MM.
DR GO; GO:0005615; C:extracellular space; IMP:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0005496; F:steroid binding; IDA:MGI.
DR GO; GO:0008211; P:glucocorticoid metabolic process; IMP:MGI.
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 Glycoprotein; Lipid-binding; Reference proteome; Secreted; Signal;
KW Steroid-binding; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..397
FT /note="Corticosteroid-binding globulin"
FT /id="PRO_0000032431"
FT BINDING 247
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000250"
FT SITE 243
FT /note="Conserved cysteine within steroid binding domain"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 397 AA; 44769 MW; F44255FE690458AF CRC64;
MSLALYTCLF WLCTSGLWTT QAVTDEDSSS HRDLAPTNVD FAFNLYKRLV ALNSDKNTLI
SPVSISMALA MLSLSTRGST QYLENLGFNM SKMSEAEIHQ GFQYLNSLLQ QSDTGLEMNM
GNVMFLLQNL KLKDSFLADT KHYYESEALT IPSKDWTKAG EQINNHVKNK TQGKIEHVVS
DLDSSATLIL INYIFLKGIW KLPFSPENTR EEDFYVNETS TVKVPMMVQS GNISYFRDSA
IPCQMVQMNY VGNGTTFIIL PDQGQMDTVV AALNRDTIDR WGKLMIPRQM NLYIPKFSMS
DTYDLQDVLA DVGIKDLFTN QSDFADTTKD TPLTLTVLHK AMLQLDEGNV LPAATNGPPV
HLPSESFTLK YNRPFIFLAF DKYTWSSLMM SQVMNPA
