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Protein

Progesterone receptor

Gene

PGR

Organism
Gallus gallus (Chicken)
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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi421 – 48666Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri421 – 44121NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri457 – 48125NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin DNA binding Source: AgBase
  • enzyme binding Source: AgBase
  • Hsp70 protein binding Source: AgBase
  • Hsp90 protein binding Source: AgBase
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  • steroid hormone binding Source: AgBase
  • steroid hormone receptor activity Source: InterPro
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: Ensembl
  • zinc ion binding Source: InterPro

GO - Biological processi

  • negative regulation of gene expression Source: Ensembl
  • response to estrogen Source: AgBase
  • response to progesterone Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-GGA-1251985. Nuclear signaling by ERBB4.
R-GGA-383280. Nuclear Receptor transcription pathway.
SABIO-RKP07812.

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
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication
  • Cytoplasm 1 Publication

  • 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
Isoform A :

GO - Cellular componenti

  • cytosol Source: AgBase
  • extracellular region Source: AgBase
  • nuclear chromatin Source: AgBase
  • nuclear matrix Source: AgBase
  • nucleus Source: AgBase
  • protein-DNA complex Source: AgBase
  • receptor complex Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi210 – 2101S → A: Decreases transcriptional activity independently of hormone concentration. Does not alter hormone binding affinity. 1 Publication
Mutagenesisi529 – 5291S → A: Decreases transcriptional activity at low hormone concentration. Does not alter hormone binding affinity. 2 Publications

Chemistry

ChEMBLiCHEMBL3304.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 786786Progesterone receptorPRO_0000053699Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei210 – 2101Phosphoserine2 Publications
Modified residuei259 – 2591Phosphoserine1 Publication
Cross-linki294 – 294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki294 – 294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki385 – 385Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei529 – 5291Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation of Ser-529 is sharply increased upon progesterone treatment, whereas phosphorylation of Ser-210 and Ser-259 is modestly induced by progesterone.3 Publications
Ubiquitinated. Ubiquitination is increased by progesterone and represses sumoylation at the same site (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-385, the main site of sumoylation, is repressed by ubiquitination on the same site (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP07812.
PRIDEiP07812.

PTM databases

iPTMnetiP07812.

Expressioni

Tissue specificityi

Oviduct and bursa of Fabricius.1 Publication

Gene expression databases

ExpressionAtlasiP07812. baseline and differential.

Interactioni

GO - Molecular functioni

  • enzyme binding Source: AgBase
  • Hsp70 protein binding Source: AgBase
  • Hsp90 protein binding Source: AgBase

Protein-protein interaction databases

BioGridi676458. 8 interactions.
DIPiDIP-79N.
STRINGi9031.ENSGALP00000027736.

Structurei

3D structure databases

ProteinModelPortaliP07812.
SMRiP07812. Positions 417-494, 536-785.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 420420Modulating, Pro-RichAdd
BLAST
Regioni487 – 786300Steroid-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi48 – 8033Asp/Glu-rich (acidic)Add
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri421 – 44121NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri457 – 48125NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000290653.
HOVERGENiHBG007583.
InParanoidiP07812.
KOiK08556.
PhylomeDBiP07812.

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. 2 hits.
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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P07812-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTEVKSKETR APSSARDGAV LLQAPPSRGE AEGIDVALDG LLYPRSSDEE
60 70 80 90 100
EEEEENEEEE EEEEPQQREE EEEEEEEDRD CPSYRPGGGS LSKDCLDSVL
110 120 130 140 150
DTFLAPAAHA APWSLFGPEV PEVPVAPMSR GPEQKAVDAG PGAPGPSQPR
160 170 180 190 200
PGAPLWPGAD SLNVAVKARP GPEDASENRA PGLPGAEERG FPERDAGPGE
210 220 230 240 250
GGLAPAAAAS PAAVEPGAGQ DYLHVPILPL NSAFLASRTR QLLDVEAAYD
260 270 280 290 300
GSAFGPRSSP SVPAADLAEY GYPPPDGKEG PFAYGEFQSA LKIKEEGVGL
310 320 330 340 350
PAAPPPFLGA KAAPADFAQP PRAGQEPSLE CVLYKAEPPL LPGAYGPPAA
360 370 380 390 400
PDSLPSTSAA PPGLYSPLGL NGHHQALGFP AAVLKEGLPQ LCPPYLGYVR
410 420 430 440 450
PDTETSQSSQ YSFESLPQKI CLICGDEASG CHYGVLTCGS CKVFFKRAME
460 470 480 490 500
GQHNYLCAGR NDCIVDKIRR KNCPACRLRK CCQAGMVLGG RKFKKLNKMK
510 520 530 540 550
VVRTLDVALQ QPAVLQDETQ SLTQRLSFSP NQEIPFVPPM ISVLRGIEPE
560 570 580 590 600
VVYAGYDNTK PETPSSLLTS LNHLCERQLL CVVKWSKLLP GFRNLHIDDQ
610 620 630 640 650
ITLIQYSWMS LMVFAMGWRS YKHVSGQMLY FAPDLILNEQ RMKESSFYSL
660 670 680 690 700
CLSMWQLPQE FVRLQVSQEE FLCMKALLLL NTIPLEGLRS QSQFDEMRTS
710 720 730 740 750
YIRELVKAIG LRQKGVVANS QRFYQLTKLM DSMHDLVKQL HLFCLNTFLQ
760 770 780
SRALSVEFPE MMSEVIAAQL PKILAGMVKP LLFHKK
Length:786
Mass (Da):85,744
Last modified:August 1, 1988 - v1
Checksum:i659559950BC45ED9
GO
Isoform A' (identifier: P07812-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     452-458: QHNYLCA → TISYHCS
     459-786: Missing.

Show »
Length:458
Mass (Da):47,884
Checksum:i1042584A8BFE8C09
GO
Isoform B (identifier: P07812-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-127: Missing.

Show »
Length:659
Mass (Da):71,805
Checksum:i2692CFA136FE3D47
GO
Isoform B' (identifier: P07812-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-127: Missing.
     452-458: QHNYLCA → TISYHCS
     459-786: Missing.

Show »
Length:331
Mass (Da):33,945
Checksum:iD595D251E509B094
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581E → DD in AAA49013 (PubMed:3153474).Curated
Sequence conflicti134 – 1341Q → E AA sequence (PubMed:3453892).Curated
Sequence conflicti148 – 1481Q → E AA sequence (PubMed:3453892).Curated
Sequence conflicti480 – 4801K → N in AAA49013 (PubMed:3153474).Curated
Sequence conflicti489 – 4891G → A in AAA49013 (PubMed:3153474).Curated
Sequence conflicti577 – 5771R → T in AAA49013 (PubMed:3153474).Curated
Sequence conflicti642 – 6421M → I in AAA49013 (PubMed:3153474).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 127127Missing in isoform B and isoform B'. 1 PublicationVSP_003707Add
BLAST
Alternative sequencei452 – 4587QHNYLCA → TISYHCS in isoform A' and isoform B'. 1 PublicationVSP_003708
Alternative sequencei459 – 786328Missing in isoform A' and isoform B'. 1 PublicationVSP_003709Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00092 mRNA. Translation: CAA68282.1.
M13972 mRNA. Translation: AAA49034.1.
M37518 mRNA. Translation: AAA49013.1.
M37518 mRNA. Translation: AAA49014.1.
M14278 mRNA. Translation: AAA49035.1.
M14279 mRNA. Translation: AAA49038.1.
M14280 mRNA. Translation: AAA49039.1.
M32732
, M31104, M32726, M32727, M32728, M32729, M32730 mRNA. Translation: AAA49011.1.
M32732
, M31104, M32726, M32727, M32728, M32729, M32730 mRNA. Translation: AAA49012.1.
M31104 mRNA. Translation: AAA49009.1.
M31104 mRNA. Translation: AAA49010.1.
PIRiA35466.
RefSeqiNP_990593.1. NM_205262.1. [P07812-1]
UniGeneiGga.705.

Genome annotation databases

GeneIDi396198.
KEGGigga:396198.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00092 mRNA. Translation: CAA68282.1.
M13972 mRNA. Translation: AAA49034.1.
M37518 mRNA. Translation: AAA49013.1.
M37518 mRNA. Translation: AAA49014.1.
M14278 mRNA. Translation: AAA49035.1.
M14279 mRNA. Translation: AAA49038.1.
M14280 mRNA. Translation: AAA49039.1.
M32732
, M31104, M32726, M32727, M32728, M32729, M32730 mRNA. Translation: AAA49011.1.
M32732
, M31104, M32726, M32727, M32728, M32729, M32730 mRNA. Translation: AAA49012.1.
M31104 mRNA. Translation: AAA49009.1.
M31104 mRNA. Translation: AAA49010.1.
PIRiA35466.
RefSeqiNP_990593.1. NM_205262.1. [P07812-1]
UniGeneiGga.705.

3D structure databases

ProteinModelPortaliP07812.
SMRiP07812. Positions 417-494, 536-785.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676458. 8 interactions.
DIPiDIP-79N.
STRINGi9031.ENSGALP00000027736.

Chemistry

ChEMBLiCHEMBL3304.

PTM databases

iPTMnetiP07812.

Proteomic databases

PaxDbiP07812.
PRIDEiP07812.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396198.
KEGGigga:396198.

Organism-specific databases

CTDi5241.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000290653.
HOVERGENiHBG007583.
InParanoidiP07812.
KOiK08556.
PhylomeDBiP07812.

Enzyme and pathway databases

ReactomeiR-GGA-1251985. Nuclear signaling by ERBB4.
R-GGA-383280. Nuclear Receptor transcription pathway.
SABIO-RKP07812.

Miscellaneous databases

PROiP07812.

Gene expression databases

ExpressionAtlasiP07812. baseline and differential.

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. 2 hits.
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...

Publicationsi

  1. "The chicken progesterone receptor: sequence, expression and functional analysis."
    Gronemeyer H., Turcotte B., Quirin-Stricker C., Bocquel M.T., Meyer M.E., Krozowski Z., Jeltsch J.-M., Lerouge T., Garnier J.-M., Chambon P.
    EMBO J. 6:3985-3994(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Characterization of multiple mRNAs originating from the chicken progesterone receptor gene. Evidence for a specific transcript encoding form A."
    Jeltsch J.-M., Turcotte B., Garnier J.-M., Lerouge T., Krozowski Z., Gronemeyer H., Chambon P.
    J. Biol. Chem. 265:3967-3974(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; A'; B AND B').
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 128-164.
  5. "Chemical and antigenic properties of pure 108,000 molecular weight chick progesterone receptor."
    Birnbaumer M., Hinrichs-Rosello M.V., Cook R.G., Schrader W.T., O'Malley B.W.
    Mol. Endocrinol. 1:249-259(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 128-164 AND 546-558, TISSUE SPECIFICITY.
  6. "Peptide sequencing of the chick oviduct progesterone receptor form B."
    Simpson R.J., Grego B., Govindan M.V., Gronemeyer H.
    Mol. Cell. Endocrinol. 52:177-184(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 136-153; 168-174; 195-228; 526-539 AND 546-563.
  7. "Hormonal regulation and identification of chicken progesterone receptor phosphorylation sites."
    Denner L.A., Schrader W.T., O'Malley B.W., Weigel N.L.
    J. Biol. Chem. 265:16548-16555(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 195-220; 258-265 AND 526-533, PHOSPHORYLATION AT SER-210; SER-259 AND SER-529.
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 417-490.
  9. "The chicken progesterone receptor A and B isoforms are products of an alternate translation initiation event."
    Conneely O.M., Kettelberger D.M., Tsai M.-J., Schrader W.T., O'Malley B.W.
    J. Biol. Chem. 264:14062-14064(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: DIFFERENCE BETWEEN FORM 1 AND FORM 2.
  10. "Phosphorylation of Ser530 facilitates hormone-dependent transcriptional activation of the chicken progesterone receptor."
    Bai W., Tullos S., Weigel N.L.
    Mol. Endocrinol. 8:1465-1473(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-529, MUTAGENESIS OF SER-529.
  11. "Phosphorylation of Ser211 in the chicken progesterone receptor modulates its transcriptional activity."
    Bai W., Weigel N.L.
    J. Biol. Chem. 271:12801-12806(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-210, MUTAGENESIS OF SER-210 AND SER-529.
  12. "Evidence for enhanced ubiquitin-mediated proteolysis of the chicken progesterone receptor by progesterone."
    Syvaala H., Vienonen A., Zhuang Y.-H., Kivineva M., Ylikomi T., Tuohimaa P.
    Life Sci. 63:1505-1512(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPRGR_CHICK
AccessioniPrimary (citable) accession number: P07812
Secondary accession number(s): Q90946
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 8, 2016
This is version 166 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, Direct protein sequencing, Reference proteome

Documents

  1. 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.