Progesterone receptor - Chlorocebus aethiops (Green monkey)

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A7X8C9 (PRGR_CHLAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 29. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Progesterone receptor
Short name=PR

Alternative name(s):
Nuclear receptor subfamily 3 group C member 3

Gene names

Name:	PGR
Synonyms:	NR3C3

Organism

Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)

Taxonomic identifier

9534 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Chlorocebus

Protein attributes

Sequence length	933 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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.
Subunit structure	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.
Subcellular location	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.
Domain	Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Post-translational modification	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-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.
Sequence similarities	Belongs to the nuclear hormone receptor family. Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Lipid-binding Metal-binding Steroid-binding Zinc
Molecular function	Receptor
PTM	Isopeptide bond Lipoprotein Palmitate Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological_process	transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro steroid binding Inferred from electronic annotation. Source: UniProtKB-KW steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 933

933

Progesterone receptor

PRO_0000375852

Regions

DNA binding

567 – 639

Nuclear receptor

Zinc finger

567 – 587

NR C4-type

Zinc finger

603 – 627

NR C4-type

Region

1 – 566

566

Modulating, Pro-Rich

Region

681 – 933

253

Steroid-binding

Motif

183 – 187

Nuclear localization signal Potential

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

130

Phosphoserine By similarity

Modified residue

162

Phosphoserine By similarity

Modified residue

190

Phosphoserine By similarity

Modified residue

213

Phosphoserine By similarity

Modified residue

294

Phosphoserine; by MAPK1 By similarity

Modified residue

345

Phosphoserine; by MAPK By similarity

Modified residue

400

Phosphoserine; by CDK2 By similarity

Modified residue

676

Phosphoserine By similarity

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Cross-link

388

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Cross-link

388

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Cross-link

531

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A7X8C9 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 981D4237AD06312B
Show »

FASTA

933

99,225

        10         20         30         40         50         60 
MTELKAKGPR APHVAGGPPS PEVGSPLLXR PAAGPFQGSQ TSDTLPEVPA IPISLDGLLF 

        70         80         90        100        110        120 
PRPCQGQDPL DEKTQDQQSL TDVEGAYSRA EATRGTGGSS SRPPEKDSGL LDSVLDTLLA 

       130        140        150        160        170        180 
PSGPGQSQPS PPACEVTSSW CLFGPELPED PPAAPATQRV LSPLMSRSGG KAGDSSGTAA 

       190        200        210        220        230        240 
AHKVLPRGLS PSRQLLLPAS GSPHWSGVPV KPSPQPTAVE VEEEDGSESE DSAGPLLKGN 

       250        260        270        280        290        300 
PRALGGAAAG GGAAAVPPGA AAGGVALVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTT 

       310        320        330        340        350        360 
MDFIHVPIRP LNHALLAART RHLLEEESYD GGAGAASAFA PPRSSPSASS TPVAVGDFPD 

       370        380        390        400        410        420 
CAYPPDADPK DDAYPLYGDF QPPALKIKEE EEGAEASARS PRSYLVAGAN PAAFPDFPLG 

       430        440        450        460        470        480 
PPPPLPPRAP PSRPGEAAVT AAPASASVSS SSSSGSTLEC ILYKAEGAPP QQGPFAPPPC 

       490        500        510        520        530        540 
KAPGAGGCLL PRDGLPSTSA SAAXAGAAPA LYPALGLNGL PQLGYQAAVL KEGLQQVYPP 

       550        560        570        580        590        600 
YLNYLRPDSE ASQSPQYSFE SLPQKICLIC GDEASGCHYG VLTCGSCKVF FKRAMEGQHN 

       610        620        630        640        650        660 
YLCAGRNDCI VDKIRRKNCP ACRLRKCCQA GMVLGGRKFK KFNKVRVMRA LDAVALPQPV 

       670        680        690        700        710        720 
GIPNESQALS QRFTFSPGQD IQFFPPLINL LVSIEPDVIY AGHDNSKPDT SSSLLTSLNQ 

       730        740        750        760        770        780 
LGERQLLSVV KWSKSLPGFR NLHIDDQITL IQYSWMSLMV FGLGWRSYKH VSGQMLYFAP 

       790        800        810        820        830        840 
DLILNEQRMK ESSFYSLCLT MWQIPQEFVK LQVSQEEFLC MKVLLLLNTI PLEGLRSQTQ 

       850        860        870        880        890        900 
FEEMRSSYIR ELIKAIGLRQ KGVVSSSQRF YQLTKLLDNL HDLVKQLHLY CLNTFIQSRA 

       910        920        930 
LSVEFPEMMS EVIAAQLPKI LAGMVKPLLF HKK

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References

[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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ234987 Genomic DNA. Translation: ABB72147.1.
3D structure databases
ProteinModelPortal	A7X8C9.
SMR	A7X8C9. Positions 563-640, 682-932.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.10.565.10. 1 hit. 3.30.50.10. 1 hit.
InterPro	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]
Pfam	PF00104. Hormone_recep. 1 hit. PF02161. Prog_receptor. 1 hit. PF00105. zf-C4. 1 hit. [Graphical view]
PRINTS	PR00544. PROGESTRONER. PR00398. STRDHORMONER. PR00047. STROIDFINGER.
SMART	SM00430. HOLI. 1 hit. SM00399. ZnF_C4. 1 hit. [Graphical view]
SUPFAM	SSF48508. Str_ncl_receptor. 1 hit.
PROSITE	PS00031. NUCLEAR_REC_DBD_1. 1 hit. PS51030. NUCLEAR_REC_DBD_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRGR_CHLAE

Accession

Primary (citable) accession number: A7X8C9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	October 23, 2007
Last modified:	April 3, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents