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Protein

Corticosteroid-binding globulin

Gene

Serpina6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Sitei242Conserved cysteine within steroid binding domain1
Binding sitei246Corticosteroid1 Publication1
Binding sitei278Corticosteroid1 Publication1
Binding sitei384Corticosteroid1 Publication1

GO - Molecular functioni

Keywordsi

Biological processTransport
LigandLipid-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi1595901 Serpina6

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi32R → A: Loss of corticosteroid binding. 1 Publication1
Mutagenesisi36P → A: Increased affinity for corticosteroids. 1 Publication1
Mutagenesisi246Q → A: Loss of corticosteroid binding. 1 Publication1
Mutagenesisi256F → A: Loss of corticosteroid binding. 1 Publication1
Mutagenesisi278D → A: Loss of corticosteroid binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000003243223 – 396Corticosteroid-binding globulinAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi88N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi216N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi252N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi319N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi352N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP31211
PRIDEiP31211

Expressioni

Tissue specificityi

Expressed by the liver; secreted in plasma.1 Publication

Gene expression databases

BgeeiENSRNOG00000009438
GenevisibleiP31211 RN

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012500

Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 32Combined sources3
Helixi35 – 52Combined sources18
Beta strandi58 – 60Combined sources3
Helixi62 – 72Combined sources11
Turni73 – 75Combined sources3
Helixi80 – 85Combined sources6
Turni89 – 91Combined sources3
Helixi94 – 108Combined sources15
Helixi111 – 113Combined sources3
Beta strandi114 – 125Combined sources12
Helixi133 – 142Combined sources10
Beta strandi146 – 149Combined sources4
Helixi155 – 169Combined sources15
Turni170 – 172Combined sources3
Beta strandi186 – 197Combined sources12
Beta strandi199 – 201Combined sources3
Helixi205 – 207Combined sources3
Beta strandi209 – 214Combined sources6
Beta strandi216 – 218Combined sources3
Beta strandi220 – 237Combined sources18
Turni238 – 241Combined sources4
Beta strandi242 – 260Combined sources19
Helixi265 – 271Combined sources7
Helixi274 – 283Combined sources10
Beta strandi285 – 294Combined sources10
Beta strandi296 – 303Combined sources8
Helixi304 – 306Combined sources3
Helixi313 – 316Combined sources4
Beta strandi334 – 345Combined sources12
Beta strandi366 – 369Combined sources4
Beta strandi374 – 380Combined sources7
Turni381 – 383Combined sources3
Beta strandi386 – 393Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V95X-ray1.93A27-396[»]
ProteinModelPortaliP31211
SMRiP31211
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

eggNOGiKOG2392 Eukaryota
COG4826 LUCA
GeneTreeiENSGT00760000118839
HOGENOMiHOG000238521
HOVERGENiHBG005957
InParanoidiP31211
KOiK04525
OMAiLPCQLVQ
OrthoDBiEOG091G0ION
PhylomeDBiP31211
TreeFamiTF343201

Family and domain databases

InterProiView protein in InterPro
IPR023795 Serpin_CS
IPR023796 Serpin_dom
IPR000215 Serpin_fam
IPR036186 Serpin_sf
PANTHERiPTHR11461 PTHR11461, 1 hit
PfamiView protein in Pfam
PF00079 Serpin, 1 hit
SMARTiView protein in SMART
SM00093 SERPIN, 1 hit
SUPFAMiSSF56574 SSF56574, 1 hit
PROSITEiView protein in PROSITE
PS00284 SERPIN, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti47 – 48QR → EC AA sequence (PubMed:3347061).Curated2
Sequence conflicti54P → C AA sequence (PubMed:3347061).Curated1
Sequence conflicti163 – 164NQ → TR (PubMed:2710140).Curated2
Sequence conflicti298I → M (PubMed:2710140).Curated1
Sequence conflicti307M → V (PubMed:2710140).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiCBG_RAT
AccessioniPrimary (citable) accession number: P31211
Secondary accession number(s): Q5M822
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 2, 2008
Last modified: May 23, 2018
This is version 134 of the entry and version 2 of the sequence. See 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

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