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Reviewed, UniProtKB/Swiss-Prot P08185 (CBG_HUMAN)

Last modified September 23, 2008. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Corticosteroid-binding globulin
      Short name=CBG
Alternative name(s):
    Transcortin
    Serpin A6
Gene names
Name: SERPINA6
Synonyms: CBG
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species.

Subcellular location

Secreted.

Tissue specificity

Plasma; synthesized in liver. Has also been identified in a number of glycocorticoid responsive cells.

Post-translational modification

N-glycosylated; binds 5 oligosaccharide chains.

Glycosylation in position Asn-260 is needed for steroid binding.

Involvement in disease

Defects in SERPINA6 are a cause of corticosteroid-binding globulin deficiency (CBG deficiency) [MIM:611489]. CBG deficiency is an extremely rare hereditary disorder characterized by reduced corticosteroid-binding capacity with normal or low plasma corticosteroid-binding globulin concentration, and normal or low basal cortisol levels associated with hypo/hypertension and muscle fatigue.

Sequence similarities

Belongs to the serpin family.

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Ontologies

Keywords

   Biological processTransport
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainSignal
   LigandLipid-binding
Steroid-binding
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Molecular functionserine-type endopeptidase inhibitor activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 2222
Chain23 – 405383Corticosteroid-binding globulin

Sites

Binding site2541Corticosteroid By similarity
Binding site2861Corticosteroid By similarity
Binding site3931Corticosteroid By similarity
Site2501Conserved cysteine within steroid binding domain

Amino acid modifications

Glycosylation311N-linked (GlcNAc...)
Glycosylation961N-linked (GlcNAc...)
Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...)
Glycosylation3301N-linked (GlcNAc...)
Glycosylation3691N-linked (GlcNAc...)

Natural variations

Natural variant1151L → H in CBG deficiency; Leuven; decreased cortisol-binding affinity. dbSNP rs28929488.
Natural variant2461S → A: dbSNP rs2228541.
Natural variant3891D → N in CBG deficiency; Lyon; decreased cortisol-binding affinity.

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Sequences

Sequence LengthMass (Da)Tools
P08185-1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: F0E36EFC3B3C08A1

FASTA40545,141
        10         20         30         40         50         60 
MPLLLYTCLL WLPTSGLWTV QAMDPNAAYV NMSNHHRGLA SANVDFAFSL YKHLVALSPK 

        70         80         90        100        110        120 
KNIFISPVSI SMALAMLSLG TCGHTRAQLL QGLGFNLTER SETEIHQGFQ HLHQLFAKSD 

       130        140        150        160        170        180 
TSLEMTMGNA LFLDGSLELL ESFSADIKHY YESEVLAMNF QDWATASRQI NSYVKNKTQG 

       190        200        210        220        230        240 
KIVDLFSGLD SPAILVLVNY IFFKGTWTQP FDLASTREEN FYVDETTVVK VPMMLQSSTI 

       250        260        270        280        290        300 
SYLHDSELPC QLVQMNYVGN GTVFFILPDK GKMNTVIAAL SRDTINRWSA GLTSSQVDLY 

       310        320        330        340        350        360 
IPKVTISGVY DLGDVLEEMG IADLFTNQAN FSRITQDAQL KSSKVVHKAV LQLNEEGVDT 

       370        380        390        400 
AGSTGVTLNL TSKPIILRFN QPFIIMIFDH FTWSSLFLAR VMNPV

« Hide

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References

« Hide 'large scale' references
[1]"Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors."
Hammond G.L., Smith C.L., Goping I.S., Underhill D.A., Harley M.J., Reventos J., Musto N.A., Gunsalus G.L., Bardin C.W.
Proc. Natl. Acad. Sci. U.S.A. 84:5153-5157(1987) [PubMed: 3299377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver and Lung.
[2]"Corticosteroid binding globulin, testosterone-estradiol binding globulin, and androgen binding protein belong to protein families distinct from steroid receptors."
Bardin C.W., Gunsalus G.L., Musto N.A., Cheng C.Y., Reventos J., Smith C., Underhill D.A., Hammond G.
J. Steroid Biochem. 30:131-139(1988) [PubMed: 3386241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-246.
[4]"Comparative structural analyses of corticosteroid binding globulin."
Kato E.A., Hsu B.R.-S., Kuhn R.W.
J. Steroid Biochem. 29:213-220(1988) [PubMed: 3347061] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-30.
[5]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed: 14760718] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96, MASS SPECTROMETRY.
Tissue: Plasma.
[6]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-31; ASN-96; ASN-330 AND ASN-369, MASS SPECTROMETRY.
Tissue: Plasma.
[7]"A Leu-->His substitution at residue 93 in human corticosteroid binding globulin results in reduced affinity for cortisol."
Smith C.L., Power S.G.A., Hammond G.L.
J. Steroid Biochem. Mol. Biol. 42:671-676(1992) [PubMed: 1504007] [Abstract]
Cited for: VARIANT CBG DEFICIENCY HIS-115.
[8]"Decreased cortisol-binding affinity of transcortin Leuven is associated with an amino acid substitution at residue-93."
van Baelen H., Power S.G.A., Hammond G.L.
Steroids 58:275-277(1993) [PubMed: 8212073] [Abstract]
Cited for: VARIANT CBG DEFICIENCY HIS-115.
[9]"Novel human corticosteroid-binding globulin variant with low cortisol-binding affinity."
Emptoz-Bonneton A., Cousin P., Seguchi K., Avvakumov G.V., Bully C., Hammond G.L., Pugeat M.
J. Clin. Endocrinol. Metab. 85:361-367(2000) [PubMed: 10634411] [Abstract]
Cited for: VARIANT CBG DEFICIENCY ASN-389.
[10]"Haploinsufficiency of the SERPINA6 gene is associated with severe muscle fatigue: A de novo mutation in corticosteroid-binding globulin deficiency."
Buss C., Schuelter U., Hesse J., Moser D., Phillips D.I., Hellhammer D., Meyer J.
J. Neural Transm. 114:563-569(2007) [PubMed: 17245537] [Abstract]
Cited for: VARIANT CBG DEFICIENCY ASN-389.
+Additional computationally mapped references.

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Web resources

Wikipedia

Transcortin entry

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Cross-references

Sequence databases

J02943 mRNA. Translation: AAB59523.1.
BC056259 mRNA. Translation: AAH56259.1.
BC058021 mRNA. Translation: AAH58021.1.
PIRA28321.
RefSeqNP_001747.2.
UniGeneHs.532635

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2VDXX-ray1.84A/B33-405[»]
2VDYX-ray2.30A/B33-405[»]
ModBaseSearch...

Protein family/group databases

MEROPSI04.954.

Proteomic databases

PeptideAtlasP08185.

Genome annotation databases

EnsemblENSG00000170099. Homo sapiens. [Contig view]
GeneID866.
KEGGhsa:866.

Organism-specific databases

HGNCHGNC:1540. SERPINA6.
MIM122500. gene.
611489. phenotype.
PharmGKBPA35033.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP08185.
HOVERGENP08185.

Gene expression databases

ArrayExpressP08185.
CleanExHS_SERPINA6.
GermOnlineENSG00000170099. Homo sapiens.

Family and domain databases

InterProIPR000295. Prot_inh_Lserp2.
IPR000215. Protease_inhib_I4_serpin.
[Graphical view]
PANTHERPTHR11461. Prot_inh_serpin. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
PRINTSPR00780. LEUSERPINII.
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
PROSITEPS00284. SERPIN. 1 hit.
[Graphical view]
ProDomP08185.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

DrugBankDB00240. Alclometasone.
DB00394. Beclomethasone.
DB01410. Ciclesonide.
DB00663. Flumethasone Pivalate.
DB00180. Flunisolide.
DB00591. Fluocinolone Acetonide.
DB01047. Fluocinonide.
DB00324. Fluorometholone.
DB00846. Flurandrenolide.
DB00588. Fluticasone Propionate.
DB00596. Halobetasol Propionate.
DB00253. Medrysone.
DB00648. Mitotane.
DB01384. Paramethasone.
DB00860. Prednisolone.
DB00896. Rimexolone.
DB00620. Triamcinolone.
LinkHubP08185.
SOURCESearch...
ProtoNetSearch...

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Entry information

Entry nameCBG_HUMAN
AccessionPrimary (citable) accession number: P08185
Secondary accession number(s): Q7Z2Q9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: September 23, 2008
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Recent format changes

Overview of recent format changes

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents