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Protein

Progesterone receptor

Gene

Pgr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Progesterone receptor is involved in activation of c-SRC/MAPK signaling on hormone stimulation (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi557 – 629Nuclear receptorPROSITE-ProRule annotationAdd BLAST73
Zinc fingeri557 – 577NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri593 – 617NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

GO - Biological processi

  • epithelial cell maturation Source: MGI
  • lung alveolus development Source: MGI
  • mammary gland development Source: MGI
  • ovulation from ovarian follicle Source: MGI
  • paracrine signaling Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • progesterone receptor signaling pathway Source: MGI
  • regulation of epithelial cell proliferation Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • tertiary branching involved in mammary gland duct morphogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Progesterone receptor
Short name:
PR
Alternative name(s):
Nuclear receptor subfamily 3 group C member 3
Gene namesi
Name:Pgr
Synonyms:Nr3c3, Pr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:97567. Pgr.

Subcellular locationi

  • Nucleus
  • Cytoplasm

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

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4969.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000536951 – 923Progesterone receptorAdd BLAST923

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei20PhosphoserineBy similarity1
Modified residuei82PhosphoserineBy similarity1
Modified residuei131PhosphoserineBy similarity1
Modified residuei163PhosphoserineBy similarity1
Modified residuei191PhosphoserineBy similarity1
Modified residuei214PhosphoserineBy similarity1
Modified residuei294Phosphoserine; by MAPK1By similarity1
Modified residuei343Phosphoserine; by MAPKBy similarity1
Cross-linki386Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki386Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei398Phosphoserine; by CDK2By similarity1
Cross-linki521Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei666PhosphoserineBy similarity1

Post-translational modificationi

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-386. Phosphorylation on Ser-343 also requires induction by hormone. Basal phosphorylation on Ser-82, Ser-163, Ser-191 and Ser-398 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-398 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-163 and Ser-294, but not at Ser-191, is impaired during the G2/M phase of the cell cycle. Phosphorylation on Ser-343 by ERK1/2 MAPK is required for interaction with SP1 (By similarity).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-386, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294 (By similarity).By similarity
Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294 (By similarity).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).By similarity

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ00175.
PRIDEiQ00175.

PTM databases

iPTMnetiQ00175.
PhosphoSitePlusiQ00175.

Expressioni

Gene expression databases

CleanExiMM_PGR.

Interactioni

Subunit structurei

Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the interaction promotes ubiquitination, decreases sumoylation, and repesses 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-294 by ERK1/2 MAPK. Interacts with PRMT2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Stat3P422274EBI-346821,EBI-602878

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ00175. 2 interactors.
STRINGi10090.ENSMUSP00000063562.

Structurei

3D structure databases

ProteinModelPortaliQ00175.
SMRiQ00175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 556Modulating, Pro-RichAdd BLAST556
Regioni671 – 923Steroid-bindingAdd BLAST253

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi184 – 188Nuclear localization signalSequence analysis5

Domaini

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

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri557 – 577NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri593 – 617NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000290653.
HOVERGENiHBG007583.
InParanoidiQ00175.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR000128. Progest_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF02161. Prog_receptor. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00544. PROGESTRONER.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 2 hits.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00175-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTELQAKDPQ VLHTSGASPS PPHIGSPLLA RLDSGPFQGS QHSDVSSVVS
60 70 80 90 100
PIPISLDGLL FPRSCRGPEL PDGKTGDQQS LSDVEGAFSG VEATHREGGR
110 120 130 140 150
NSRPPEKDSR LLDSVLDSLL TPSGPEQSHA SPPACEAITS WCLFGPELPE
160 170 180 190 200
DPRSVPATKG LLSPLMSRPE IKVGDQSGTG RGQKVLPKGL SPPRQLLLPT
210 220 230 240 250
SGSAHWPGAG VKPSPQPAAG EVEEDSGLET EGSASPLLKS KPRALEGTGQ
260 270 280 290 300
GGGVAANAPS AAPGGVTLVP KEDSRFSAPR VSLEQDSPIA PGRSPLATTV
310 320 330 340 350
VDFIHVPILP LNHALLAART RQLLEGESYD GGATAGPFCP PRSPSAPSTP
360 370 380 390 400
VPRGDFPDCT YPLEGDPKED VFPLYGDFQT PGLKIKEEEE GADAAVRSPR
410 420 430 440 450
PYLSAGASSS TFPDFPLAPA PQAAPSSRPG EAAVAGGPSS AAVSPASSSG
460 470 480 490 500
SALECILYKA EAPPTQGSFA PLPCKPPAAA SCLLPRDSLP AAPGTAAAPA
510 520 530 540 550
IYQPLGLNGL PQLGYQAAVL KDSLPQVYPP YLNYLRPDSE ASQSPQYGFD
560 570 580 590 600
SLPQKICLIC GDEASGCHYG VLTCGSCKVF FKRAMEGQHN YLCAGRNDCI
610 620 630 640 650
VDKIRRKNCP ACRLRKCCQA GMVLGGRKFK KFNKVRVMRT LDGVALPQSV
660 670 680 690 700
GLPNESQALS QRITFSPNQE IQLVPPLINL LMSIEPDVIY AGHDNTKPDT
710 720 730 740 750
SSSLLTSLNQ LGERQLLSVV KWSKSLPGFR NLHIDDQITL IQYSWMSLMV
760 770 780 790 800
FGLGWRSYKH VSGQMLYFAP DLILNEQRMK ELSFYSLCLT MWQIPQEFVK
810 820 830 840 850
LQVTHEEFLC MKVLLLLNTI PLEGLRSQSQ FEEMRSSYIR ELIKAIGLRQ
860 870 880 890 900
KGVVPTSQRF YQLTKLLDSL HDLVKQLHLY CLNTFIQSRT LAVEFPEMMS
910 920
EVIAAQLPKI LAGMVKPLLF HKK
Length:923
Mass (Da):99,074
Last modified:December 1, 1992 - v1
Checksum:i9415F1ED343BEE3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68915 mRNA. Translation: AAA39971.1.
U12644 Genomic DNA. Translation: AAA66067.1.
PIRiA39596.
UniGeneiMm.12798.
Mm.437703.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68915 mRNA. Translation: AAA39971.1.
U12644 Genomic DNA. Translation: AAA66067.1.
PIRiA39596.
UniGeneiMm.12798.
Mm.437703.

3D structure databases

ProteinModelPortaliQ00175.
SMRiQ00175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ00175. 2 interactors.
STRINGi10090.ENSMUSP00000063562.

Chemistry databases

ChEMBLiCHEMBL4969.

PTM databases

iPTMnetiQ00175.
PhosphoSitePlusiQ00175.

Proteomic databases

PaxDbiQ00175.
PRIDEiQ00175.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:97567. Pgr.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000290653.
HOVERGENiHBG007583.
InParanoidiQ00175.

Miscellaneous databases

PROiQ00175.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PGR.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR000128. Progest_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF02161. Prog_receptor. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00544. PROGESTRONER.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 2 hits.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRGR_MOUSE
AccessioniPrimary (citable) accession number: Q00175
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 2, 2016
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.