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A7XW20

- PRGR_PITIR

UniProt

A7XW20 - PRGR_PITIR

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Protein

Progesterone receptor

Gene

PGR

Organism
Pithecia irrorata (Gray monk saki)
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.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi569 – 64173Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri569 – 58921NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri605 – 62925NR C4-typePROSITE-ProRule annotationAdd
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
OrganismiPithecia irrorata (Gray monk saki)
Taxonomic identifieri30598 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniPlatyrrhiniPitheciidaePitheciinaePithecia

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

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 935935Progesterone receptorPRO_0000375860Add
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 – 201PhosphoserineBy similarity
Modified residuei81 – 811PhosphoserineBy similarity
Modified residuei130 – 1301PhosphoserineBy similarity
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei190 – 1901PhosphoserineBy similarity
Modified residuei213 – 2131PhosphoserineBy similarity
Modified residuei294 – 2941Phosphoserine; by MAPK1By similarity
Modified residuei345 – 3451Phosphoserine; by MAPKBy similarity
Cross-linki388 – 388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki388 – 388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei400 – 4001Phosphoserine; by CDK2By similarity
Cross-linki533 – 533Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei678 – 6781PhosphoserineBy 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 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.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.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

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.By similarity

Structurei

3D structure databases

ProteinModelPortaliA7XW20.
SMRiA7XW20. Positions 565-642, 684-934.
ModBaseiSearch...
MobiDBiSearch...

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 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

Belongs to the nuclear hormone receptor family.Curated
Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri569 – 58921NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri605 – 62925NR C4-typePROSITE-ProRule annotationAdd
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.

A7XW20-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTELKAKGPR APHVAGSPSS PKVGSPLPCS QAAGPFPGSQ TSDTLPEASA
60 70 80 90 100
LPISLDGLLF PRICQGQDPT DEKTQDQQSL SDVZGAYSRV EATRGAGGSS
110 120 130 140 150
SRPPEKDSGL LDSVLDTLWE PSGPGQSQPS PPACEVTSSW CLFGPELPED
160 170 180 190 200
PPAAPATQRV LSPLMSRSGG KAGDSSGMAA AHKVLPRGLS PSRQLLLPTS
210 220 230 240 250
GSPHWSGAPV KPSPQPAAVE VEEEDGSESE DSAGPLLKGK PRALGGAAAG
260 270 280 290 300
GGVAAVPPGA AAGGLSLVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTV
310 320 330 340 350
TDFIHVPILP LSHALLAART RQLLEDESYD GGAGAASAFA PPRSSPSASS
360 370 380 390 400
TPVPGGDFPD CAYAPEAEPK DDAYPLYGDF QPPALKIKEE EEGAEASARS
410 420 430 440 450
PRSYLVAGAS PAAFPDFPLG PPPSLPPRAP PPRPGEAAVT AAPASASVSS
460 470 480 490 500
ASSSGSTLEC ILYKAEGAPS QQGQFAPPPC KAPGAGGCLL PRDSLPSTSA
510 520 530 540 550
SAAATAAGAA PGLYPALGLN GLPQLGYQAA VLKEGLPQVY PPYLNYLRPD
560 570 580 590 600
SEASQSPQYS FESLPQKICL ICGDEASGCH YGVLTCGSCK VFFKRAMEGQ
610 620 630 640 650
HNYLCAGRND CIVDKIRRKN CPACRLRKCC QAGMVLGGRK FKKFNKVRVM
660 670 680 690 700
RALDAVALPQ PVGIPNENQA LSQRFTFSPS QDIQLIPPLI NLLLSIEPDV
710 720 730 740 750
IFAGHDNTKP DTSSSLLTSL NQLGERQLLS VVKWSKSLPG FRNLHIDDQI
760 770 780 790 800
TLIQYSWMSL MVFGLGWRSY KHVSGQMLYF APDLILNEQR MKESSFYSLC
810 820 830 840 850
LTMWQIPQEF VKLQVSQEEF LCMKVLLLLN TIPLEGLRSQ TQFEEMRSSY
860 870 880 890 900
IRELIKAIGL RQKGVVSSSQ RFYQLTKLLD NLHDLVKQLH LYCLNTFIQS
910 920 930
RALSVEFPEM MSEVIAAQLP KILAGMVKPL LFHKK
Length:935
Mass (Da):99,262
Last modified:October 23, 2007 - v1
Checksum:iB70975933E487790
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ485134 Genomic DNA. Translation: ABE73085.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ485134 Genomic DNA. Translation: ABE73085.1 .

3D structure databases

ProteinModelPortali A7XW20.
SMRi A7XW20. Positions 565-642, 684-934.
ModBasei Search...
MobiDBi Search...

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_PITIR
AccessioniPrimary (citable) accession number: A7XW20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: October 23, 2007
Last modified: October 29, 2014
This is version 33 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