A7X8B7 · PRGR_GORGO

Function

function

The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation.

Features

Showing features for dna binding, binding site.

1933100200300400500600700800900
TypeIDPosition(s)Description
DNA binding567-639Nuclear receptor
Binding site766progesterone (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromatin
Cellular Componentcytoplasm
Cellular Componentnucleoplasm
Cellular Componentplasma membrane
Molecular FunctionATPase binding
Molecular FunctionDNA-binding transcription activator activity, RNA polymerase II-specific
Molecular Functionestrogen response element binding
Molecular Functionidentical protein binding
Molecular Functionnuclear receptor activity
Molecular Functionnuclear steroid receptor activity
Molecular Functionsteroid binding
Molecular Functiontranscription coactivator binding
Molecular Functionzinc ion binding
Biological Processglandular epithelial cell maturation
Biological Processlung alveolus development
Biological Processmaintenance of protein location in nucleus
Biological Processnegative regulation of gene expression
Biological Processnegative regulation of phosphorylation
Biological Processnuclear receptor-mediated steroid hormone signaling pathway
Biological Processovulation from ovarian follicle
Biological Processparacrine signaling
Biological Processprogesterone receptor signaling pathway
Biological Processregulation of epithelial cell proliferation
Biological Processregulation of transcription by RNA polymerase II
Biological Processtertiary branching involved in mammary gland duct morphogenesis

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Progesterone receptor
  • Short names
    PR
  • Alternative names
    • Nuclear receptor subfamily 3 group C member 3

Gene names

    • Name
      PGR
    • Synonyms
      NR3C3

Organism names

Accessions

  • Primary accession
    A7X8B7

Proteomes

Subcellular Location

Note: Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G1 and G2/M phases (By similarity).

Keywords

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00003758541-933Progesterone receptor
Modified residue20Phosphoserine
Modified residue81Phosphoserine
Modified residue130Phosphoserine
Modified residue162Phosphoserine
Modified residue190Phosphoserine
Modified residue213Phosphoserine
Modified residue294Phosphoserine; by MAPK1
Modified residue345Phosphoserine; by MAPK
Cross-link388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-link388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residue400Phosphoserine; by CDK2
Cross-link531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residue676Phosphoserine

Post-translational modification

Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162, Ser-190 and Ser-400 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G2/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1 (By similarity).
Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294 (By similarity).
Ubiquitination is hormone-dependent and represses sumoylation on the same site (By similarity).
Promoted by MAPK-mediated phosphorylation on Ser-294 (By similarity).
Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound PGR when it is not associated with coactivators (NCOAs) (By similarity).
In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation (By similarity).
Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation (By similarity).

Keywords

Expression

Gene expression databases

Interaction

Subunit

Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the interaction promotes ubiquitination, decreases sumoylation, and represses transcriptional activity. Interacts with PIAS3; the interaction promotes sumoylation of PR in a hormone-dependent manner, inhibits DNA-binding, and alters nuclear export. Interacts with SP1; the interaction requires ligand-induced phosphorylation on Ser-345 by ERK1/2-MAPK. Interacts with PRMT2. Interacts with NCOA2 and NCOA1. Interacts with KLF9. Interacts with GTF2B (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, motif, compositional bias, zinc finger, domain.

TypeIDPosition(s)Description
Region1-164AF3; mediates transcriptional activation
Region1-256Disordered
Region1-566Modulating, Pro-Rich
Motif55-59LXXL motif 1
Compositional bias68-84Polar residues
Motif115-119LXXL motif 2
Compositional bias120-135Polar residues
Region165-305Mediates transcriptional transrepression
Motif183-187Nuclear localization signal
Region331-378Disordered
Compositional bias415-433Pro residues
Region415-452Disordered
Region456-546AF1; mediates transcriptional activation
Zinc finger567-587NR C4-type
Zinc finger603-627NR C4-type
Domain679-913NR LBD
Region687-933AF2; mediates transcriptional activation

Domain

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

Sequence similarities

Belongs to the nuclear hormone receptor family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    933
  • Mass (Da)
    98,830
  • Last updated
    2007-10-23 v1
  • Checksum
    9C1080538291E6E6
MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPYPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLETLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQGVLSPLMSRSGGKAGDSSGTAAAHKVLPRGLSPSRQLLLPVSGSPHWSGAPVKPSPQPAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPSASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRAPPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGIPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
G3RJR5G3RJR5_GORGO831
A0A2I2YH06A0A2I2YH06_GORGO764

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias68-84Polar residues
Compositional bias120-135Polar residues
Compositional bias415-433Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ234982
EMBL· GenBank· DDBJ
ABB72142.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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