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P31211

- CBG_RAT

UniProt

P31211 - CBG_RAT

Protein

Corticosteroid-binding globulin

Gene

Serpina6

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (02 Sep 2008)
      Previous versions | rss
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    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

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Lipid-binding, Steroid-binding

    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

    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.
    GeneTreeiENSGT00740000115120.
    HOGENOMiHOG000238521.
    HOVERGENiHBG005957.
    InParanoidiQ5M822.
    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

    MSLALYTCLL WLCTSGLWTA QASTNESSNS HRGLAPTNVD FAFNLYQRLV    50
    ALNPDKNTLI SPVSISMALA MVSLGSAQTQ SLQSLGFNLT ETSEAEIHQS 100
    FQYLNYLLKQ SDTGLEMNMG NAMFLLQKLK LKDSFLADVK QYYESEALAI 150
    DFEDWTKASQ QINQHVKDKT QGKIEHVFSD LDSPASFILV NYIFLRGIWE 200
    LPFSPENTRE EDFYVNETST VKVPMMVQSG SIGYFRDSVF PCQLIQMDYV 250
    GNGTAFFILP DQGQMDTVIA ALSRDTIDRW GKLMTPRQVN LYIPKFSISD 300
    TYDLKDMLED LNIKDLLTNQ SDFSGNTKDV PLTLTMVHKA MLQLDEGNVL 350
    PNSTNGAPLH LRSEPLDIKF NKPFILLLFD KFTWSSLMMS QVVNPA 396
    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.

    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 ENSGT00740000115120.
    HOGENOMi HOG000238521.
    HOVERGENi HBG005957.
    InParanoidi Q5M822.
    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

    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 1, 2014
    This is version 109 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