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P07812 (PRGR_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Progesterone receptor
Short name=PR
Alternative name(s):
Nuclear receptor subfamily 3 group C member 3
Gene names
Name:PGR
Synonyms:NR3C3
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length786 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

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. Ref.12

Isoform A: Nucleus. Cytoplasm. Note: Mainly nuclear. Ref.12

Tissue specificity

Oviduct and bursa of Fabricius. Ref.5

Domain

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

Post-translational modification

Phosphorylation of Ser-529 is sharply increased upon progesterone treatment, whereas phosphorylation of Ser-210 and Ser-259 is modestly induced by progesterone.

Ubiquitinated. Ubiquitination is increased by progesterone and represses sumoylation at the same site By similarity. Ref.12

Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-385, the main site of sumoylation, is repressed by ubiquitination on the same site By similarity.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR3 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Lipid-binding
Metal-binding
Steroid-binding
Zinc
   Molecular functionReceptor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processepithelial cell maturation

Inferred from electronic annotation. Source: Compara

negative regulation of gene expression

Inferred from electronic annotation. Source: Compara

ovulation from ovarian follicle

Inferred from electronic annotation. Source: Compara

progesterone receptor signaling pathway

Inferred from electronic annotation. Source: Compara

regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Compara

tertiary branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Compara

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from electronic annotation. Source: Compara

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

steroid binding

Inferred from electronic annotation. Source: UniProtKB-KW

steroid hormone receptor activity

Inferred from electronic annotation. Source: Compara

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P07812-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A' (identifier: P07812-2)

The sequence of this isoform differs from the canonical sequence as follows:
     452-458: QHNYLCA → TISYHCS
     459-786: Missing.
Isoform B (identifier: P07812-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-127: Missing.
Isoform B' (identifier: P07812-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-127: Missing.
     452-458: QHNYLCA → TISYHCS
     459-786: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 786786Progesterone receptor
PRO_0000053699

Regions

DNA binding421 – 48666Nuclear receptor
Zinc finger421 – 44121NR C4-type
Zinc finger457 – 48125NR C4-type
Region1 – 420420Modulating, Pro-Rich
Region487 – 786300Steroid-binding
Compositional bias48 – 8033Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue2101Phosphoserine Ref.7 Ref.11
Modified residue2591Phosphoserine Ref.7
Modified residue5291Phosphoserine Ref.7 Ref.10
Cross-link7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-link294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link385Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 127127Missing in isoform B and isoform B'.
VSP_003707
Alternative sequence452 – 4587QHNYLCA → TISYHCS in isoform A' and isoform B'.
VSP_003708
Alternative sequence459 – 786328Missing in isoform A' and isoform B'.
VSP_003709

Experimental info

Mutagenesis2101S → A: Decreases transcriptional activity independently of hormone concentration. Does not alter hormone binding affinity. Ref.11
Mutagenesis5291S → A: Decreases transcriptional activity at low hormone concentration. Does not alter hormone binding affinity. Ref.10 Ref.11
Sequence conflict581E → DD in AAA49013. Ref.2
Sequence conflict1341Q → E AA sequence Ref.5
Sequence conflict1481Q → E AA sequence Ref.5
Sequence conflict4801K → N in AAA49013. Ref.2
Sequence conflict4891G → A in AAA49013. Ref.2
Sequence conflict5771R → T in AAA49013. Ref.2
Sequence conflict6421M → I in AAA49013. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 659559950BC45ED9

FASTA78685,744
        10         20         30         40         50         60 
MTEVKSKETR APSSARDGAV LLQAPPSRGE AEGIDVALDG LLYPRSSDEE EEEEENEEEE 

        70         80         90        100        110        120 
EEEEPQQREE EEEEEEEDRD CPSYRPGGGS LSKDCLDSVL DTFLAPAAHA APWSLFGPEV 

       130        140        150        160        170        180 
PEVPVAPMSR GPEQKAVDAG PGAPGPSQPR PGAPLWPGAD SLNVAVKARP GPEDASENRA 

       190        200        210        220        230        240 
PGLPGAEERG FPERDAGPGE GGLAPAAAAS PAAVEPGAGQ DYLHVPILPL NSAFLASRTR 

       250        260        270        280        290        300 
QLLDVEAAYD GSAFGPRSSP SVPAADLAEY GYPPPDGKEG PFAYGEFQSA LKIKEEGVGL 

       310        320        330        340        350        360 
PAAPPPFLGA KAAPADFAQP PRAGQEPSLE CVLYKAEPPL LPGAYGPPAA PDSLPSTSAA 

       370        380        390        400        410        420 
PPGLYSPLGL NGHHQALGFP AAVLKEGLPQ LCPPYLGYVR PDTETSQSSQ YSFESLPQKI 

       430        440        450        460        470        480 
CLICGDEASG CHYGVLTCGS CKVFFKRAME GQHNYLCAGR NDCIVDKIRR KNCPACRLRK 

       490        500        510        520        530        540 
CCQAGMVLGG RKFKKLNKMK VVRTLDVALQ QPAVLQDETQ SLTQRLSFSP NQEIPFVPPM 

       550        560        570        580        590        600 
ISVLRGIEPE VVYAGYDNTK PETPSSLLTS LNHLCERQLL CVVKWSKLLP GFRNLHIDDQ 

       610        620        630        640        650        660 
ITLIQYSWMS LMVFAMGWRS YKHVSGQMLY FAPDLILNEQ RMKESSFYSL CLSMWQLPQE 

       670        680        690        700        710        720 
FVRLQVSQEE FLCMKALLLL NTIPLEGLRS QSQFDEMRTS YIRELVKAIG LRQKGVVANS 

       730        740        750        760        770        780 
QRFYQLTKLM DSMHDLVKQL HLFCLNTFLQ SRALSVEFPE MMSEVIAAQL PKILAGMVKP 


LLFHKK

« Hide

Isoform A' [UniParc].

Checksum: 1042584A8BFE8C09
Show »

FASTA45847,884
Isoform B [UniParc].

Checksum: 2692CFA136FE3D47
Show »

FASTA65971,805
Isoform B' [UniParc].

Checksum: D595D251E509B094
Show »

FASTA33133,945

References

[1]"The chicken progesterone receptor: sequence, expression and functional analysis."
Gronemeyer H., Turcotte B., Quirin-Stricker C., Bocquel M.T., Meyer M.E., Krozowski Z., Jeltsch J.-M., Lerouge T., Garnier J.-M., Chambon P.
EMBO J. 6:3985-3994(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and expression of a functional chicken progesterone receptor."
Conneely O.M., Dobson A.D.W., Tsai M.-J., Beattie W.G., Toft D.O., Huckaby C.S., Zarucki T., Schrader W.T., O'Malley B.W.
Mol. Endocrinol. 1:517-525(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Characterization of multiple mRNAs originating from the chicken progesterone receptor gene. Evidence for a specific transcript encoding form A."
Jeltsch J.-M., Turcotte B., Garnier J.-M., Lerouge T., Krozowski Z., Gronemeyer H., Chambon P.
J. Biol. Chem. 265:3967-3974(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; A'; B AND B').
[4]"Molecular cloning of the chicken progesterone receptor."
Conneely O.M., Sullivan W.P., Toft D.O., Birnbaumer M., Cook R.G., Maxwell B.L., Zarucki-Schulz T., Greene G.L., Schrader W.T., O'Malley B.W.
Science 233:767-770(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 128-164.
[5]"Chemical and antigenic properties of pure 108,000 molecular weight chick progesterone receptor."
Birnbaumer M., Hinrichs-Rosello M.V., Cook R.G., Schrader W.T., O'Malley B.W.
Mol. Endocrinol. 1:249-259(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 128-164 AND 546-558, TISSUE SPECIFICITY.
[6]"Peptide sequencing of the chick oviduct progesterone receptor form B."
Simpson R.J., Grego B., Govindan M.V., Gronemeyer H.
Mol. Cell. Endocrinol. 52:177-184(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 136-153; 168-174; 195-228; 526-539 AND 546-563.
[7]"Hormonal regulation and identification of chicken progesterone receptor phosphorylation sites."
Denner L.A., Schrader W.T., O'Malley B.W., Weigel N.L.
J. Biol. Chem. 265:16548-16555(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 195-220; 258-265 AND 526-533, PHOSPHORYLATION AT SER-210; SER-259 AND SER-529.
[8]"Cloning of the chicken progesterone receptor."
Jeltsch J.-M., Krozowski Z., Quirin-Stricker C., Gronemeyer H., Simpson R.J., Garnier J.-M., Krust A., Jacob F., Chambon P.
Proc. Natl. Acad. Sci. U.S.A. 83:5424-5428(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 417-490.
[9]"The chicken progesterone receptor A and B isoforms are products of an alternate translation initiation event."
Conneely O.M., Kettelberger D.M., Tsai M.-J., Schrader W.T., O'Malley B.W.
J. Biol. Chem. 264:14062-14064(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DIFFERENCE BETWEEN FORM 1 AND FORM 2.
[10]"Phosphorylation of Ser530 facilitates hormone-dependent transcriptional activation of the chicken progesterone receptor."
Bai W., Tullos S., Weigel N.L.
Mol. Endocrinol. 8:1465-1473(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-529, MUTAGENESIS OF SER-529.
[11]"Phosphorylation of Ser211 in the chicken progesterone receptor modulates its transcriptional activity."
Bai W., Weigel N.L.
J. Biol. Chem. 271:12801-12806(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-210, MUTAGENESIS OF SER-210 AND SER-529.
[12]"Evidence for enhanced ubiquitin-mediated proteolysis of the chicken progesterone receptor by progesterone."
Syvaala H., Vienonen A., Zhuang Y.-H., Kivineva M., Ylikomi T., Tuohimaa P.
Life Sci. 63:1505-1512(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y00092 mRNA. Translation: CAA68282.1.
M13972 mRNA. Translation: AAA49034.1.
M37518 mRNA. Translation: AAA49013.1.
M37518 mRNA. Translation: AAA49014.1.
M14278 mRNA. Translation: AAA49035.1.
M14279 mRNA. Translation: AAA49038.1.
M14280 mRNA. Translation: AAA49039.1.
M32732 expand/collapse EMBL AC list , M31104, M32726, M32727, M32728, M32729, M32730 mRNA. Translation: AAA49011.1.
M32732 expand/collapse EMBL AC list , M31104, M32726, M32727, M32728, M32729, M32730 mRNA. Translation: AAA49012.1.
M31104 mRNA. Translation: AAA49009.1.
M31104 mRNA. Translation: AAA49010.1.
IPIIPI00576936.
IPI00590382.
IPI00594799.
IPI00601371.
PIRA35466.
RefSeqNP_990593.1. NM_205262.1.
UniGeneGga.705.

3D structure databases

ProteinModelPortalP07812.
SMRP07812. Positions 417-494, 536-785.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-79N.
STRING9031.ENSGALP00000027736.

Proteomic databases

PaxDbP07812.
PRIDEP07812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396198.
KEGGgga:396198.

Organism-specific databases

CTD5241.

Phylogenomic databases

eggNOGNOG273252.
HOGENOMHOG000290653.
HOVERGENHBG007583.
InParanoidP07812.
KOK08556.
OrthoDBEOG4TQM93.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. 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]
PfamPF00104. Hormone_recep. 1 hit.
PF02161. Prog_receptor. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00544. PROGESTRONER.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. Str_ncl_receptor. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP07812.
ChEMBLCHEMBL3304.
NextBio20816250.

Entry information

Entry namePRGR_CHICK
AccessionPrimary (citable) accession number: P07812
Secondary accession number(s): Q90946
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 3, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents