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Protein

Progesterone receptor

Gene

PGR

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi566 – 64075Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri568 – 58821NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri604 – 62825NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 1

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3456.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 930930Progesterone receptorPRO_0000053696Add
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 residuei20 – 201PhosphoserineBy similarity
Modified residuei82 – 821PhosphoserineBy similarity
Modified residuei131 – 1311PhosphoserineBy similarity
Modified residuei191 – 1911PhosphoserineBy similarity
Modified residuei212 – 2121PhosphoserineBy similarity
Modified residuei293 – 2931Phosphoserine; by MAPK1By similarity
Modified residuei344 – 3441Phosphoserine; by MAPKBy similarity
Cross-linki387 – 387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki387 – 387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei399 – 3991Phosphoserine; by CDK2By similarity
Cross-linki532 – 532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei673 – 6731PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-293 is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-387. Phosphorylation on Ser-102 and Ser-344 also requires induction by hormone. Basal phosphorylation on Ser-82, Ser-191 and Ser-399 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-399 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-293, but not at Ser-191, is impaired during the G2/M phase of the cell cycle. Phosphorylation on Ser-344 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-387, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-293 (By similarity).By similarity
Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-293 (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

PRIDEiP06186.

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-344. Interacts with PRMT2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000012634.

Chemistry

BindingDBiP06186.

Structurei

3D structure databases

ProteinModelPortaliP06186.
SMRiP06186. Positions 564-641, 679-929.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 565565Modulating, Pro-RichAdd
BLAST
Regioni678 – 930253Steroid-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi184 – 1885Nuclear localization signalSequence analysis

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 fingeri568 – 58821NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri604 – 62825NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000290653.
HOVERGENiHBG007583.
InParanoidiP06186.
KOiK08556.

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.

P06186-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTELKAKEPR APHVAGGAPS PTEVGSQLLG RPDPGPFQGS QTSEASSVVS
60 70 80 90 100
AIPISLDGLL FPRPCQGQNP PDGKTQDPPS LSDVEGAFPG VEAPEGAGDS
110 120 130 140 150
SSRPPEKDSG LLDSVLDTLL APSGPGQSHA SPATCEAISP WCLFGPDLPE
160 170 180 190 200
DPRAAPATKG VLAPLMSRPE DKAGDSSGTA AAHKVLPRGL SPSRQLLLPS
210 220 230 240 250
SGSPHWPAVK PSPQPAAVQV DEEDSSESEG TVGPLLKGQP RALGGTAAGG
260 270 280 290 300
GAAPVASGAA AGGVALVPKE DSRFSAPRVS LAEQDAPVAP GRSPLATSVV
310 320 330 340 350
DFIHVPILPL NHAFLATRTR QLLEGESYDG GAAAASPFVP QRGSPSASST
360 370 380 390 400
PVAGGDFPDC TYPPDAEPKD DAFPLYGDFQ PPALKIKEEE EAAEAAARSP
410 420 430 440 450
RTYLVAGANP AAFPDFQLAA PPPPSLPPRV PSSRPGEAAV AASPGSASVS
460 470 480 490 500
SSSSSGSTLE CILYKAEGAP PQQGPFAPLP CKPPGAGACL LPRDGLPSTS
510 520 530 540 550
ASGAAAGAAP ALYPTLGLNG LPQLGYQAAV LKEGLPQVYT PYLNYLRPDS
560 570 580 590 600
EASQSPQYSF ESLPQKICLI CGDEASGCHY GVLTCGSCKV FFKRAMEGQH
610 620 630 640 650
NYLCAGRNDC IVDKIRRKNC PACRLRKCCQ AGMVLGGRKF KKFNKVRVMR
660 670 680 690 700
ALDAVALPQP VGIPNESQRI TFSPSQEIQL IPPLINLLMS IEPDVIYAGH
710 720 730 740 750
DNTKPDTSSS LLTSLNQLGE RQLLSVVKWS KSLPGFRNLH IDDQITLIQY
760 770 780 790 800
SWMSLMVFGL GWRSYKHVSG QMLYFAPDLI LNEQRMKESS FYSLCLTMWQ
810 820 830 840 850
IPQEFVKLQV SQEEFLCMKV LLLLNTIPLE GLRSQSQFEE MRSSYIRELI
860 870 880 890 900
KAIGLRQKGV VSSSQRFYQL TKLLDNLHDL VKQLHLYCLN TFIQSRALSV
910 920 930
EFPEMMSEVI AAQLPKILAG MVKPLLFHKK
Length:930
Mass (Da):98,667
Last modified:January 1, 1988 - v1
Checksum:i644FF4C13BF2F883
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14547 mRNA. Translation: AAA31443.1.
PIRiA25923.
RefSeqiNP_001075736.1. NM_001082267.1.
UniGeneiOcu.1947.

Genome annotation databases

EnsembliENSOCUT00000014695; ENSOCUP00000012634; ENSOCUG00000014693.
GeneIDi100009094.
KEGGiocu:100009094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14547 mRNA. Translation: AAA31443.1.
PIRiA25923.
RefSeqiNP_001075736.1. NM_001082267.1.
UniGeneiOcu.1947.

3D structure databases

ProteinModelPortaliP06186.
SMRiP06186. Positions 564-641, 679-929.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000012634.

Chemistry

BindingDBiP06186.
ChEMBLiCHEMBL3456.

Proteomic databases

PRIDEiP06186.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000014695; ENSOCUP00000012634; ENSOCUG00000014693.
GeneIDi100009094.
KEGGiocu:100009094.

Organism-specific databases

CTDi5241.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000290653.
HOVERGENiHBG007583.
InParanoidiP06186.
KOiK08556.

Miscellaneous databases

PROiP06186.

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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPRGR_RABIT
AccessioniPrimary (citable) accession number: P06186
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 8, 2016
This is version 138 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. 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.