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A7X8C4

- PRGR_MACSY

UniProt

A7X8C4 - PRGR_MACSY

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Protein

Progesterone receptor

Gene
PGR, NR3C3
Organism
Macaca sylvanus (Barbary macaque)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi569 – 64173Nuclear receptorAdd
BLAST
Zinc fingeri569 – 58921NR C4-typeAdd
BLAST
Zinc fingeri605 – 62925NR C4-typeAdd
BLAST

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro
  2. sequence-specific DNA binding transcription factor activity Source: InterPro
  3. steroid binding Source: UniProtKB-KW
  4. steroid hormone receptor activity Source: InterPro
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. transcription, DNA-templated Source: UniProtKB-KW
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
OrganismiMacaca sylvanus (Barbary macaque)
Taxonomic identifieri9546 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 935935Progesterone receptorPRO_0000375856Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei20 – 201Phosphoserine By similarity
Modified residuei81 – 811Phosphoserine By similarity
Modified residuei130 – 1301Phosphoserine By similarity
Modified residuei162 – 1621Phosphoserine By similarity
Modified residuei190 – 1901Phosphoserine By similarity
Modified residuei213 – 2131Phosphoserine By similarity
Modified residuei294 – 2941Phosphoserine; by MAPK1 By similarity
Modified residuei345 – 3451Phosphoserine; by MAPK By similarity
Cross-linki388 – 388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-linki388 – 388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Modified residuei400 – 4001Phosphoserine; by CDK2 By similarity
Cross-linki533 – 533Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei678 – 6781Phosphoserine By similarity

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-388. Phosphorylation on 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. Promoted by MAPK-mediated phosphorylation on Ser-294 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 - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiA7X8C4.

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-345 by ERK1/2 MAPK. Interacts with PRMT2 By similarity.

Structurei

3D structure databases

ProteinModelPortaliA7X8C4.
SMRiA7X8C4. Positions 565-642, 684-934.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 568568Modulating, Pro-RichAdd
BLAST
Regioni683 – 935253Steroid-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi183 – 1875Nuclear localization signal Reviewed prediction

Domaini

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

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri569 – 58921NR C4-typeAdd
BLAST
Zinc fingeri605 – 62925NR C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR000128. Progest_rcpt.
IPR001723. Str_hrmn_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.

A7X8C4-1 [UniParc]FASTAAdd to Basket

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MTELKAKGPR APHVAGGPPS PEVGSPLLCR PAAGPFQGSQ TSDTLPEVSA    50
TPISLDGLLF PRPCQGQDPL DEKTQDQQSL SDVEGAYSRA EATRGTGGSS 100
SRPPEKDSGL LDSVLDTLLA PSGPGQSQPS PPACEVTSSW CLFGPELPED 150
PPAAPATQRV LSPLMSRSGG KAGDSSGTAA AHKVLPRGLS PSRQLLLPAS 200
GSPHWSGAPV KPSPQPAAVE VEEEDGSESE DSAGPLLKGK PRALGGAAAG 250
GGAAAVPPGA AAGGVALVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTT 300
MDFTHVPILP LNHALLAART RQLLEEESYD GGAGAASAFA PPRSSPSASS 350
TPVAVGDFPD CAYPPDAHPK DDAYPLYGDF QPPALKIKEE EEGAEVSARS 400
PRSYLVAGAN PAAFPDFPLG PPPPLPPRAP PSRPGEAAVT AAPAGASVSS 450
ASSSGSTLEC ILYKAEGAPP QQGPFAPPPC KAQGAGGCLL PRDGLPSTST 500
SASAAAAGAA PALYPALGLN GLPQLGYQAA VLKEGLQQVY PPYLNYLRPD 550
SEASQSPQYS FESLPQKICL ICGDEASGCH YGVLTCGSCK VFFKRAMEGQ 600
HNYLCAGRND CIVDKIRRKN CPACRLRKCC QAGMVLGGRK FKKFNKVRVM 650
RALDAVALPQ PVGIPNESQA LSQRFTFSPG QDIQLIPPLI NLLVSIEPDV 700
IYAGHDNSKP DTSSSLLTSL NQLGERQLLS VVKWSKLLPG FRNLHIDDQI 750
TLIQYSWMSL MVFGLGWRSY KHVSGQMLYF APDLILNEQR MKESSFYSLC 800
LTMWQIPQEF VKLQVSQEEF LCMKVLLLLN TIPLEGLRSQ TQFEEMRSSY 850
IRELIKAIGL RQKGVVSSSQ RFYQLTKLLD NLHDLVKQLH LYCLNTFIQS 900
RALSVEFPEM MSEVIAAQLP KILAGMVKPL LFHKK 935
Length:935
Mass (Da):99,213
Last modified:October 23, 2007 - v1
Checksum:iC88AE9A96872330A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ234985 Genomic DNA. Translation: ABB72145.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ234985 Genomic DNA. Translation: ABB72145.1 .

3D structure databases

ProteinModelPortali A7X8C4.
SMRi A7X8C4. Positions 565-642, 684-934.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi A7X8C4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR000128. Progest_rcpt.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view ]
Pfami PF00104. Hormone_recep. 1 hit.
PF02161. Prog_receptor. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR00544. PROGESTRONER.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 2 hits.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The human progesterone receptor shows evidence of adaptive evolution associated with its ability to act as a transcription factor."
    Chen C., Opazo J.C., Erez O., Uddin M., Santolaya-Forgas J., Goodman M., Grossman L.I., Romero R., Wildman D.E.
    Mol. Phylogenet. Evol. 47:637-649(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiPRGR_MACSY
AccessioniPrimary (citable) accession number: A7X8C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: October 23, 2007
Last modified: February 19, 2014
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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