PRGR_CHICK
ID PRGR_CHICK Reviewed; 786 AA.
AC P07812; Q90946;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Progesterone receptor;
DE Short=PR;
DE AltName: Full=Nuclear receptor subfamily 3 group C member 3;
GN Name=PGR; Synonyms=NR3C3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3443098; DOI=10.1002/j.1460-2075.1987.tb02741.x;
RA Gronemeyer H., Turcotte B., Quirin-Stricker C., Bocquel M.T., Meyer M.E.,
RA Krozowski Z., Jeltsch J.-M., Lerouge T., Garnier J.-M., Chambon P.;
RT "The chicken progesterone receptor: sequence, expression and functional
RT analysis.";
RL EMBO J. 6:3985-3994(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3153474; DOI=10.1210/mend-1-8-517;
RA Conneely O.M., Dobson A.D.W., Tsai M.-J., Beattie W.G., Toft D.O.,
RA Huckaby C.S., Zarucki T., Schrader W.T., O'Malley B.W.;
RT "Sequence and expression of a functional chicken progesterone receptor.";
RL Mol. Endocrinol. 1:517-525(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; A'; B AND B').
RX PubMed=2303488; DOI=10.1016/s0021-9258(19)39689-9;
RA Jeltsch J.-M., Turcotte B., Garnier J.-M., Lerouge T., Krozowski Z.,
RA Gronemeyer H., Chambon P.;
RT "Characterization of multiple mRNAs originating from the chicken
RT progesterone receptor gene. Evidence for a specific transcript encoding
RT form A.";
RL J. Biol. Chem. 265:3967-3974(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 128-164.
RX PubMed=2426779; DOI=10.1126/science.2426779;
RA Conneely O.M., Sullivan W.P., Toft D.O., Birnbaumer M., Cook R.G.,
RA Maxwell B.L., Zarucki-Schulz T., Greene G.L., Schrader W.T., O'Malley B.W.;
RT "Molecular cloning of the chicken progesterone receptor.";
RL Science 233:767-770(1986).
RN [5]
RP PROTEIN SEQUENCE OF 128-164 AND 546-558, AND TISSUE SPECIFICITY.
RX PubMed=3453892; DOI=10.1210/mend-1-3-249;
RA Birnbaumer M., Hinrichs-Rosello M.V., Cook R.G., Schrader W.T.,
RA O'Malley B.W.;
RT "Chemical and antigenic properties of pure 108,000 molecular weight chick
RT progesterone receptor.";
RL Mol. Endocrinol. 1:249-259(1987).
RN [6]
RP PROTEIN SEQUENCE OF 136-153; 168-174; 195-228; 526-539 AND 546-563.
RX PubMed=3653503; DOI=10.1016/0303-7207(87)90042-6;
RA Simpson R.J., Grego B., Govindan M.V., Gronemeyer H.;
RT "Peptide sequencing of the chick oviduct progesterone receptor form B.";
RL Mol. Cell. Endocrinol. 52:177-184(1987).
RN [7]
RP PROTEIN SEQUENCE OF 195-220; 258-265 AND 526-533, AND PHOSPHORYLATION AT
RP SER-210; SER-259 AND SER-529.
RX PubMed=2398063; DOI=10.1016/s0021-9258(17)46258-2;
RA Denner L.A., Schrader W.T., O'Malley B.W., Weigel N.L.;
RT "Hormonal regulation and identification of chicken progesterone receptor
RT phosphorylation sites.";
RL J. Biol. Chem. 265:16548-16555(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 417-490.
RX PubMed=2426697; DOI=10.1073/pnas.83.15.5424;
RA Jeltsch J.-M., Krozowski Z., Quirin-Stricker C., Gronemeyer H.,
RA Simpson R.J., Garnier J.-M., Krust A., Jacob F., Chambon P.;
RT "Cloning of the chicken progesterone receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5424-5428(1986).
RN [9]
RP DIFFERENCE BETWEEN FORM 1 AND FORM 2.
RX PubMed=2760059; DOI=10.1016/s0021-9258(18)71642-6;
RA Conneely O.M., Kettelberger D.M., Tsai M.-J., Schrader W.T., O'Malley B.W.;
RT "The chicken progesterone receptor A and B isoforms are products of an
RT alternate translation initiation event.";
RL J. Biol. Chem. 264:14062-14064(1989).
RN [10]
RP PHOSPHORYLATION AT SER-529, AND MUTAGENESIS OF SER-529.
RX PubMed=7877616; DOI=10.1210/mend.8.11.7877616;
RA Bai W., Tullos S., Weigel N.L.;
RT "Phosphorylation of Ser530 facilitates hormone-dependent transcriptional
RT activation of the chicken progesterone receptor.";
RL Mol. Endocrinol. 8:1465-1473(1994).
RN [11]
RP PHOSPHORYLATION AT SER-210, AND MUTAGENESIS OF SER-210 AND SER-529.
RX PubMed=8662804; DOI=10.1074/jbc.271.22.12801;
RA Bai W., Weigel N.L.;
RT "Phosphorylation of Ser211 in the chicken progesterone receptor modulates
RT its transcriptional activity.";
RL J. Biol. Chem. 271:12801-12806(1996).
RN [12]
RP UBIQUITINATION, AND SUBCELLULAR LOCATION.
RX PubMed=9808061; DOI=10.1016/s0024-3205(98)00417-2;
RA Syvaala H., Vienonen A., Zhuang Y.-H., Kivineva M., Ylikomi T.,
RA Tuohimaa P.;
RT "Evidence for enhanced ubiquitin-mediated proteolysis of the chicken
RT progesterone receptor by progesterone.";
RL Life Sci. 63:1505-1512(1998).
CC -!- FUNCTION: The steroid hormones and their receptors are involved in the
CC regulation of eukaryotic gene expression and affect cellular
CC proliferation and differentiation in target tissues.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:9808061}. Cytoplasm {ECO:0000269|PubMed:9808061}.
CC Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent.
CC On hormone stimulation, retained in the cytoplasm in the G(1) and
CC G(2)/M phases (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Nucleus. Cytoplasm. Note=Mainly
CC nuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A;
CC IsoId=P07812-1; Sequence=Displayed;
CC Name=A';
CC IsoId=P07812-2; Sequence=VSP_003708, VSP_003709;
CC Name=B;
CC IsoId=P07812-3; Sequence=VSP_003707;
CC Name=B';
CC IsoId=P07812-4; Sequence=VSP_003707, VSP_003708, VSP_003709;
CC -!- TISSUE SPECIFICITY: Oviduct and bursa of Fabricius.
CC {ECO:0000269|PubMed:3453892}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- PTM: Phosphorylation of Ser-529 is sharply increased upon progesterone
CC treatment, whereas phosphorylation of Ser-210 and Ser-259 is modestly
CC induced by progesterone. {ECO:0000269|PubMed:2398063,
CC ECO:0000269|PubMed:7877616, ECO:0000269|PubMed:8662804}.
CC -!- PTM: Ubiquitinated. Ubiquitination is increased by progesterone and
CC represses sumoylation at the same site (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylation is hormone-dependent and represses transcriptional
CC activity. Sumoylation on all three sites is enhanced by PIAS3.
CC Desumoylated by SENP1. Sumoylation on Lys-385, the main site of
CC sumoylation, is repressed by ubiquitination on the same site (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; Y00092; CAA68282.1; -; mRNA.
DR EMBL; M13972; AAA49034.1; -; mRNA.
DR EMBL; M37518; AAA49013.1; -; mRNA.
DR EMBL; M37518; AAA49014.1; -; mRNA.
DR EMBL; M14278; AAA49035.1; -; mRNA.
DR EMBL; M14279; AAA49038.1; -; mRNA.
DR EMBL; M14280; AAA49039.1; -; mRNA.
DR EMBL; M32732; AAA49011.1; -; mRNA.
DR EMBL; M31104; AAA49011.1; JOINED; mRNA.
DR EMBL; M32726; AAA49011.1; JOINED; mRNA.
DR EMBL; M32727; AAA49011.1; JOINED; mRNA.
DR EMBL; M32728; AAA49011.1; JOINED; mRNA.
DR EMBL; M32729; AAA49011.1; JOINED; mRNA.
DR EMBL; M32730; AAA49011.1; JOINED; mRNA.
DR EMBL; M32732; AAA49012.1; -; mRNA.
DR EMBL; M31104; AAA49012.1; JOINED; mRNA.
DR EMBL; M32726; AAA49012.1; JOINED; mRNA.
DR EMBL; M32727; AAA49012.1; JOINED; mRNA.
DR EMBL; M32728; AAA49012.1; JOINED; mRNA.
DR EMBL; M32729; AAA49012.1; JOINED; mRNA.
DR EMBL; M32730; AAA49012.1; JOINED; mRNA.
DR EMBL; M31104; AAA49009.1; -; mRNA.
DR EMBL; M31104; AAA49010.1; -; mRNA.
DR PIR; A35466; A35466.
DR RefSeq; NP_990593.1; NM_205262.1. [P07812-1]
DR AlphaFoldDB; P07812; -.
DR SMR; P07812; -.
DR BioGRID; 676458; 8.
DR DIP; DIP-79N; -.
DR STRING; 9031.ENSGALP00000027736; -.
DR ChEMBL; CHEMBL3304; -.
DR iPTMnet; P07812; -.
DR PaxDb; P07812; -.
DR PRIDE; P07812; -.
DR GeneID; 396198; -.
DR KEGG; gga:396198; -.
DR CTD; 5241; -.
DR VEuPathDB; HostDB:geneid_396198; -.
DR eggNOG; KOG3575; Eukaryota.
DR HOGENOM; CLU_007368_15_0_1; -.
DR InParanoid; P07812; -.
DR OrthoDB; 615449at2759; -.
DR PhylomeDB; P07812; -.
DR SABIO-RK; P07812; -.
DR PRO; PR:P07812; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000785; C:chromatin; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0016363; C:nuclear matrix; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0032993; C:protein-DNA complex; IDA:AgBase.
DR GO; GO:0043235; C:receptor complex; IDA:CAFA.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:AgBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:AgBase.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:AgBase.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:AgBase.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990239; F:steroid hormone binding; IDA:CAFA.
DR GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002071; P:glandular epithelial cell maturation; IEA:Ensembl.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
DR GO; GO:0038001; P:paracrine signaling; IEA:Ensembl.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043627; P:response to estrogen; IDA:AgBase.
DR GO; GO:0032570; P:response to progesterone; IDA:AgBase.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR000128; Progest_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF02161; Prog_receptor; 2.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00544; PROGESTRONER.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Lipid-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Steroid-binding; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..786
FT /note="Progesterone receptor"
FT /id="PRO_0000053699"
FT DOMAIN 532..766
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 421..486
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 421..441
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 457..481
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..420
FT /note="Modulating, Pro-Rich"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2398063,
FT ECO:0000269|PubMed:8662804"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2398063"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2398063,
FT ECO:0000269|PubMed:7877616"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 385
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform B and isoform B')"
FT /evidence="ECO:0000303|PubMed:2303488"
FT /id="VSP_003707"
FT VAR_SEQ 452..458
FT /note="QHNYLCA -> TISYHCS (in isoform A' and isoform B')"
FT /evidence="ECO:0000303|PubMed:2303488"
FT /id="VSP_003708"
FT VAR_SEQ 459..786
FT /note="Missing (in isoform A' and isoform B')"
FT /evidence="ECO:0000303|PubMed:2303488"
FT /id="VSP_003709"
FT MUTAGEN 210
FT /note="S->A: Decreases transcriptional activity
FT independently of hormone concentration. Does not alter
FT hormone binding affinity."
FT /evidence="ECO:0000269|PubMed:8662804"
FT MUTAGEN 529
FT /note="S->A: Decreases transcriptional activity at low
FT hormone concentration. Does not alter hormone binding
FT affinity."
FT /evidence="ECO:0000269|PubMed:7877616,
FT ECO:0000269|PubMed:8662804"
FT CONFLICT 58
FT /note="E -> DD (in Ref. 2; AAA49013)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="Q -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="Q -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="K -> N (in Ref. 2; AAA49013)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="G -> A (in Ref. 2; AAA49013)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="R -> T (in Ref. 2; AAA49013)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="M -> I (in Ref. 2; AAA49013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 786 AA; 85744 MW; 659559950BC45ED9 CRC64;
MTEVKSKETR APSSARDGAV LLQAPPSRGE AEGIDVALDG LLYPRSSDEE EEEEENEEEE
EEEEPQQREE EEEEEEEDRD CPSYRPGGGS LSKDCLDSVL DTFLAPAAHA APWSLFGPEV
PEVPVAPMSR GPEQKAVDAG PGAPGPSQPR PGAPLWPGAD SLNVAVKARP GPEDASENRA
PGLPGAEERG FPERDAGPGE GGLAPAAAAS PAAVEPGAGQ DYLHVPILPL NSAFLASRTR
QLLDVEAAYD GSAFGPRSSP SVPAADLAEY GYPPPDGKEG PFAYGEFQSA LKIKEEGVGL
PAAPPPFLGA KAAPADFAQP PRAGQEPSLE CVLYKAEPPL LPGAYGPPAA PDSLPSTSAA
PPGLYSPLGL NGHHQALGFP AAVLKEGLPQ LCPPYLGYVR PDTETSQSSQ YSFESLPQKI
CLICGDEASG CHYGVLTCGS CKVFFKRAME GQHNYLCAGR NDCIVDKIRR KNCPACRLRK
CCQAGMVLGG RKFKKLNKMK VVRTLDVALQ QPAVLQDETQ SLTQRLSFSP NQEIPFVPPM
ISVLRGIEPE VVYAGYDNTK PETPSSLLTS LNHLCERQLL CVVKWSKLLP GFRNLHIDDQ
ITLIQYSWMS LMVFAMGWRS YKHVSGQMLY FAPDLILNEQ RMKESSFYSL CLSMWQLPQE
FVRLQVSQEE FLCMKALLLL NTIPLEGLRS QSQFDEMRTS YIRELVKAIG LRQKGVVANS
QRFYQLTKLM DSMHDLVKQL HLFCLNTFLQ SRALSVEFPE MMSEVIAAQL PKILAGMVKP
LLFHKK
