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CBG_URSAR
ID   CBG_URSAR               Reviewed;         405 AA.
AC   B2D1U1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 29.
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   Ursus arctos (Brown bear) (Grizzly bear).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Alsop D., Cattet M., Stenhouse G., Vijayan M.;
RT   "Serum corticosteroid-binding globulins as indicators of chronic stress in
RT   grizzly bears.";
RL   Submitted (MAR-2008) 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   -!- 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; EU571738; ACB71035.1; -; mRNA.
DR   AlphaFoldDB; B2D1U1; -.
DR   SMR; B2D1U1; -.
DR   MEROPS; I04.954; -.
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; Secreted; Signal; Steroid-binding; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..405
FT                   /note="Corticosteroid-binding globulin"
FT                   /id="PRO_0000343846"
FT   BINDING         254
FT                   /ligand="cortisol"
FT                   /ligand_id="ChEBI:CHEBI:17650"
FT                   /evidence="ECO:0000250"
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   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   405 AA;  45619 MW;  003BC2A8EB76DD56 CRC64;
     MLLALCTCFL WLSTTDLWTV QAKDPDTDVS PRTPHRDLAP NNVDFAFILY RHLVASLPGK
     NVFISPVSIS MALAMLSLGA RGYTRVQLLQ GLGFNLTKLS EAEIHQGFRH LRHLFEKESD
     TMLEMAMGNA LFLDRNLELL ESFLADTKHY YEAEALAADF KDGAGASRQI NEYIKNKTQG
     KIVDLVSKLD SSAMLILVNY IFFKGTWEHP FDPESTRQEN FYVNKTTVVR VPMMFQSGTI
     KYLHDRVLPC QLVQLEYLGN GTVFFVLPEE GKMDTVIAAL SRDTIQRWSE SLTTGQVNLY
     VPRVVISGAY DLRAILGDMG IADLFDKEAD FSGITREAPL KLSKVVHKAV LQLDEKGLEA
     ATCPRVMLEG ASEPLTFRFD RPFVLMIFDH FSWSSLFLGK VVNPN
 
 
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