CBG_RABIT
ID CBG_RABIT Reviewed; 383 AA.
AC P23775;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Corticosteroid-binding globulin;
DE Short=CBG;
DE AltName: Full=Serpin A6;
DE AltName: Full=Transcortin;
GN Name=SERPINA6; Synonyms=CBG;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE OF 15-383, AND PROTEIN SEQUENCE OF 1-24.
RC TISSUE=Liver;
RX PubMed=2293023; DOI=10.1210/mend-4-8-1166;
RA Seralini G.-E., Smith C.L., Hammond G.L.;
RT "Rabbit corticosteroid-binding globulin: primary structure and biosynthesis
RT during pregnancy.";
RL Mol. Endocrinol. 4:1166-1172(1990).
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: Produced and secreted by hepatocytes, but has also
CC been identified in a number of glycocorticoid responsive cells (it is
CC found in maternal lung, spleen, and ovary and fetal kidney).
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 PIR; A36117; A36117.
DR AlphaFoldDB; P23775; -.
DR SMR; P23775; -.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; P23775; -.
DR Proteomes; UP000001811; 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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Lipid-binding; Reference proteome;
KW Secreted; Steroid-binding; Transport.
FT CHAIN 1..383
FT /note="Corticosteroid-binding globulin"
FT /id="PRO_0000094099"
FT BINDING 232
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="cortisol"
FT /ligand_id="ChEBI:CHEBI:17650"
FT /evidence="ECO:0000250"
FT SITE 228
FT /note="Conserved cysteine within steroid binding domain"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 383 AA; 42326 MW; 2DD85B5D37BE8EDE CRC64;
ADPPGGDIST RSPPRGLAPA NVDFAFSLYR QLVSSAPDRN ICISPVSVSM ALAMLSLGAS
GHTRTQLLQG LGFNLTEMPE AEIHQGFQYL HHLLGESDTS LEMTMGNALF LDHSLELLES
FSADIRRYYE SEALATDFQD WPRACRQINE YIENKTQGKI ADLFLGLENP AILILVNYIF
FKGTWAHPFD PQSTEEKSFY VDDTTTVMVP MMFQSSTVKY LHDPVLPCRL VQLDYVGNGT
AFFILPDKGK VDTVIAALSR DTIQRWSKSL TYRLVHLYIP KASISGAYEL RGALAAMGIA
DLFTNQANFS SISQEGPLKV SKVLHKAVLQ LDEHGGVEVA ATGGPLQLVS EPLTLNFNRP
FLILIFDDFT WSSLFLGKVV IPA
