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P31211

- CBG_RAT

UniProt

P31211 - CBG_RAT

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Protein

Corticosteroid-binding globulin

Gene

Serpina6

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei242 – 2421Conserved cysteine within steroid binding domain
Binding sitei246 – 2461Corticosteroid1 Publication
Binding sitei278 – 2781Corticosteroid1 Publication
Binding sitei384 – 3841Corticosteroid1 Publication

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: RefGenome
  2. steroid binding Source: UniProtKB

GO - Biological processi

  1. glucocorticoid metabolic process Source: Ensembl
  2. negative regulation of endopeptidase activity Source: RefGenome
  3. regulation of proteolysis Source: RefGenome
  4. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding, Steroid-binding

Protein family/group databases

MEROPSiI04.954.

Names & Taxonomyi

Protein namesi
Recommended name:
Corticosteroid-binding globulin
Short name:
CBG
Alternative name(s):
Serpin A6
Transcortin
Gene namesi
Name:Serpina6
Synonyms:Cbg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 6

Organism-specific databases

RGDi1595901. Serpina6.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: RefGenome
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321R → A: Loss of corticosteroid binding. 1 Publication
Mutagenesisi36 – 361P → A: Increased affinity for corticosteroids. 1 Publication
Mutagenesisi246 – 2461Q → A: Loss of corticosteroid binding. 1 Publication
Mutagenesisi256 – 2561F → A: Loss of corticosteroid binding. 1 Publication
Mutagenesisi278 – 2781D → A: Loss of corticosteroid binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 396374Corticosteroid-binding globulinPRO_0000032432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi216 – 2161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi352 – 3521N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP31211.
PRIDEiP31211.

Expressioni

Tissue specificityi

Expressed by the liver; secreted in plasma.1 Publication

Gene expression databases

GenevestigatoriP31211.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012500.

Structurei

Secondary structure

1
396
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 323
Helixi35 – 5218
Beta strandi58 – 603
Helixi62 – 7211
Turni73 – 753
Helixi80 – 856
Turni89 – 913
Helixi94 – 10815
Helixi111 – 1133
Beta strandi114 – 12512
Helixi133 – 14210
Beta strandi146 – 1494
Helixi155 – 16915
Turni170 – 1723
Beta strandi186 – 19712
Beta strandi199 – 2013
Helixi205 – 2073
Beta strandi209 – 2146
Beta strandi216 – 2183
Beta strandi220 – 23718
Turni238 – 2414
Beta strandi242 – 26019
Helixi265 – 2717
Helixi274 – 28310
Beta strandi285 – 29410
Beta strandi296 – 3038
Helixi304 – 3063
Helixi313 – 3164
Beta strandi334 – 34512
Beta strandi366 – 3694
Beta strandi374 – 3807
Turni381 – 3833
Beta strandi386 – 3938

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V95X-ray1.93A27-396[»]
ProteinModelPortaliP31211.
SMRiP31211. Positions 29-396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31211.

Family & Domainsi

Domaini

Proteolytic cleavage leads to an important conformation change. This reduces the affinity for steroids By similarity.By similarity

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP31211.
OMAiSTREENF.
OrthoDBiEOG7J446W.
PhylomeDBiP31211.
TreeFamiTF343201.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31211-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLALYTCLL WLCTSGLWTA QASTNESSNS HRGLAPTNVD FAFNLYQRLV
60 70 80 90 100
ALNPDKNTLI SPVSISMALA MVSLGSAQTQ SLQSLGFNLT ETSEAEIHQS
110 120 130 140 150
FQYLNYLLKQ SDTGLEMNMG NAMFLLQKLK LKDSFLADVK QYYESEALAI
160 170 180 190 200
DFEDWTKASQ QINQHVKDKT QGKIEHVFSD LDSPASFILV NYIFLRGIWE
210 220 230 240 250
LPFSPENTRE EDFYVNETST VKVPMMVQSG SIGYFRDSVF PCQLIQMDYV
260 270 280 290 300
GNGTAFFILP DQGQMDTVIA ALSRDTIDRW GKLMTPRQVN LYIPKFSISD
310 320 330 340 350
TYDLKDMLED LNIKDLLTNQ SDFSGNTKDV PLTLTMVHKA MLQLDEGNVL
360 370 380 390
PNSTNGAPLH LRSEPLDIKF NKPFILLLFD KFTWSSLMMS QVVNPA
Length:396
Mass (Da):44,671
Last modified:September 2, 2008 - v2
Checksum:iA3D12AEC876D2BA2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 482QR → EC AA sequence (PubMed:3347061)Curated
Sequence conflicti54 – 541P → C AA sequence (PubMed:3347061)Curated
Sequence conflicti163 – 1642NQ → TR(PubMed:2710140)Curated
Sequence conflicti298 – 2981I → M(PubMed:2710140)Curated
Sequence conflicti307 – 3071M → V(PubMed:2710140)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH473982 Genomic DNA. Translation: EDL81783.1.
BC088300 mRNA. Translation: AAH88300.1.
PIRiA40066.
RefSeqiNP_001009663.1. NM_001009663.1.
UniGeneiRn.2374.

Genome annotation databases

EnsembliENSRNOT00000012500; ENSRNOP00000012500; ENSRNOG00000009438.
GeneIDi299270.
KEGGirno:299270.
UCSCiRGD:1595901. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH473982 Genomic DNA. Translation: EDL81783.1 .
BC088300 mRNA. Translation: AAH88300.1 .
PIRi A40066.
RefSeqi NP_001009663.1. NM_001009663.1.
UniGenei Rn.2374.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V95 X-ray 1.93 A 27-396 [» ]
ProteinModelPortali P31211.
SMRi P31211. Positions 29-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000012500.

Protein family/group databases

MEROPSi I04.954.

Proteomic databases

PaxDbi P31211.
PRIDEi P31211.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000012500 ; ENSRNOP00000012500 ; ENSRNOG00000009438 .
GeneIDi 299270.
KEGGi rno:299270.
UCSCi RGD:1595901. rat.

Organism-specific databases

CTDi 866.
RGDi 1595901. Serpina6.

Phylogenomic databases

eggNOGi COG4826.
GeneTreei ENSGT00760000118839.
HOGENOMi HOG000238521.
HOVERGENi HBG005957.
InParanoidi P31211.
OMAi STREENF.
OrthoDBi EOG7J446W.
PhylomeDBi P31211.
TreeFami TF343201.

Miscellaneous databases

EvolutionaryTracei P31211.
NextBioi 645130.
PROi P31211.

Gene expression databases

Genevestigatori P31211.

Family and domain databases

InterProi IPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view ]
PANTHERi PTHR11461. PTHR11461. 1 hit.
Pfami PF00079. Serpin. 1 hit.
[Graphical view ]
SMARTi SM00093. SERPIN. 1 hit.
[Graphical view ]
SUPFAMi SSF56574. SSF56574. 1 hit.
PROSITEi PS00284. SERPIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Rat corticosteroid binding globulin: primary structure and messenger ribonucleic acid levels in the liver under different physiological conditions."
    Smith C.L., Hammond G.L.
    Mol. Endocrinol. 3:420-426(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Liver.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-60.
  5. "Corticosteroid-binding globulin, a structural basis for steroid transport and proteinase-triggered release."
    Klieber M.A., Underhill C., Hammond G.L., Muller Y.A.
    J. Biol. Chem. 282:29594-29603(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 27-396 IN COMPLEX WITH CORTICOSTEROID, FUNCTION, MUTAGENESIS OF ARG-32; PRO-36; GLN-246; PHE-256 AND ASP-278.

Entry informationi

Entry nameiCBG_RAT
AccessioniPrimary (citable) accession number: P31211
Secondary accession number(s): Q5M822
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 2, 2008
Last modified: October 29, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3