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A7X8D2

- PRGR_COLGU

UniProt

A7X8D2 - PRGR_COLGU

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Protein

Progesterone receptor

Gene

PGR

Organism
Colobus guereza (Mantled guereza) (Eastern black-and-white colobus monkey)
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 bindingi568 – 64073Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri568 – 58821NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri604 – 62825NR 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
OrganismiColobus guereza (Mantled guereza) (Eastern black-and-white colobus monkey)
Taxonomic identifieri33548 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeColobinaeColobus

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 – 934934Progesterone receptorPRO_0000375853Add
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-linki532 – 532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei677 – 6771PhosphoserineBy 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).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

Proteomic databases

PRIDEiA7X8D2.

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

ProteinModelPortaliA7X8D2.
SMRiA7X8D2. Positions 564-641, 683-933.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 567567Modulating, Pro-RichAdd
BLAST
Regioni682 – 934253Steroid-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 fingeri568 – 58821NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri604 – 62825NR 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.

A7X8D2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTELKSKGPR APHVAGGPPS PEVGSPLLCR PAAGPFQGSQ TSDTLPEVSA
60 70 80 90 100
IPISLDGLLF PRLCQGQDPP DKKTQNQQSL SDVEGAYSRA EATRGTGGSS
110 120 130 140 150
SRPPEKDSGL LDSVLDTLLA PSGPGQSQPS PPACEVTSSW CLFGPELPED
160 170 180 190 200
PPAAPATQRV LSPLMSRSGG KTEDSSGTAA AHKVLPRGLS PSRQLLLPTS
210 220 230 240 250
GSPHWSGAPV KPSPQPTAVE VEEEDGSESE DSAGPLLKGK SRVLGGAAAG
260 270 280 290 300
GGAAAVPPGA AAGGVGLVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTM
310 320 330 340 350
MDFIHVPIVP LNHALLAART RQLLEDESYD GGAGAASAFA PPQSSPSASS
360 370 380 390 400
TPVAVGDFPD CAYPPDAEPK DNAYPLYGDF QPLALKIKEE EEGAEASARS
410 420 430 440 450
PGSYLVAGAN PAAFPDFPLG PPPQLPPRAP PSRPGEAAVT AAPASASVSS
460 470 480 490 500
ASSPGSTLEC ILYKAEGALP QQGQFAPPPC KAPGAGGCLL PRDGLPSTSA
510 520 530 540 550
SAAAAAGAAP TLYPALGLNG LPQLGYQAAV LKEGLQQVYP 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 VGIPNESQVL SQRFTFSPGQ DIQLIPPLIK LLMSIEPDVI
710 720 730 740 750
YAGHDNSKPD TSSSLLTSLN QLGERQLLSV VKWSKSLPGF RNLHIDDQIT
760 770 780 790 800
LIQYSWMSLM VFGLGWRSYK HVSGQMLYFA PDLILNEQRM KESSFYSLCL
810 820 830 840 850
TMWQIPQEFV KLQVSQEEFL CMKVLLLLNT IPLEGLRSQT QFEEMRSSYI
860 870 880 890 900
RELIKAIGLR QKGVVSSSQR FYQLTKLLDN LHDLVKQLHL YCLNTFIQSR
910 920 930
ALSVEFPEMM SEVIAAQLPK ILAGMVKPLL FHKK
Length:934
Mass (Da):99,320
Last modified:October 23, 2007 - v1
Checksum:i7E1A300E9CA44696
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ234988 Genomic DNA. Translation: ABB72148.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ234988 Genomic DNA. Translation: ABB72148.1 .

3D structure databases

ProteinModelPortali A7X8D2.
SMRi A7X8D2. Positions 564-641, 683-933.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi A7X8D2.

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_COLGU
AccessioniPrimary (citable) accession number: A7X8D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: October 23, 2007
Last modified: October 29, 2014
This is version 35 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