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Progesterone receptor (PR) (Nuclear receptor subfamily 3 group C member 3)

 PRGR_CHICK              Reviewed;         786 AA.
P07812; Q90946;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
28-FEB-2018, entry version 179.
RecName: Full=Progesterone receptor;
Short=PR;
AltName: Full=Nuclear receptor subfamily 3 group C member 3;
Name=PGR; Synonyms=NR3C3;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3443098;
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.;
"The chicken progesterone receptor: sequence, expression and
functional analysis.";
EMBO J. 6:3985-3994(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3153474; DOI=10.1210/mend-1-8-517;
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.;
"Sequence and expression of a functional chicken progesterone
receptor.";
Mol. Endocrinol. 1:517-525(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; A'; B AND B').
PubMed=2303488;
Jeltsch J.-M., Turcotte B., Garnier J.-M., Lerouge T., Krozowski Z.,
Gronemeyer H., Chambon P.;
"Characterization of multiple mRNAs originating from the chicken
progesterone receptor gene. Evidence for a specific transcript
encoding form A.";
J. Biol. Chem. 265:3967-3974(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 128-164.
PubMed=2426779; DOI=10.1126/science.2426779;
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.;
"Molecular cloning of the chicken progesterone receptor.";
Science 233:767-770(1986).
[5]
PROTEIN SEQUENCE OF 128-164 AND 546-558, AND TISSUE SPECIFICITY.
PubMed=3453892; DOI=10.1210/mend-1-3-249;
Birnbaumer M., Hinrichs-Rosello M.V., Cook R.G., Schrader W.T.,
O'Malley B.W.;
"Chemical and antigenic properties of pure 108,000 molecular weight
chick progesterone receptor.";
Mol. Endocrinol. 1:249-259(1987).
[6]
PROTEIN SEQUENCE OF 136-153; 168-174; 195-228; 526-539 AND 546-563.
PubMed=3653503; DOI=10.1016/0303-7207(87)90042-6;
Simpson R.J., Grego B., Govindan M.V., Gronemeyer H.;
"Peptide sequencing of the chick oviduct progesterone receptor form
B.";
Mol. Cell. Endocrinol. 52:177-184(1987).
[7]
PROTEIN SEQUENCE OF 195-220; 258-265 AND 526-533, AND PHOSPHORYLATION
AT SER-210; SER-259 AND SER-529.
PubMed=2398063;
Denner L.A., Schrader W.T., O'Malley B.W., Weigel N.L.;
"Hormonal regulation and identification of chicken progesterone
receptor phosphorylation sites.";
J. Biol. Chem. 265:16548-16555(1990).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 417-490.
PubMed=2426697; DOI=10.1073/pnas.83.15.5424;
Jeltsch J.-M., Krozowski Z., Quirin-Stricker C., Gronemeyer H.,
Simpson R.J., Garnier J.-M., Krust A., Jacob F., Chambon P.;
"Cloning of the chicken progesterone receptor.";
Proc. Natl. Acad. Sci. U.S.A. 83:5424-5428(1986).
[9]
DIFFERENCE BETWEEN FORM 1 AND FORM 2.
PubMed=2760059;
Conneely O.M., Kettelberger D.M., Tsai M.-J., Schrader W.T.,
O'Malley B.W.;
"The chicken progesterone receptor A and B isoforms are products of an
alternate translation initiation event.";
J. Biol. Chem. 264:14062-14064(1989).
[10]
PHOSPHORYLATION AT SER-529, AND MUTAGENESIS OF SER-529.
PubMed=7877616; DOI=10.1210/mend.8.11.7877616;
Bai W., Tullos S., Weigel N.L.;
"Phosphorylation of Ser530 facilitates hormone-dependent
transcriptional activation of the chicken progesterone receptor.";
Mol. Endocrinol. 8:1465-1473(1994).
[11]
PHOSPHORYLATION AT SER-210, AND MUTAGENESIS OF SER-210 AND SER-529.
PubMed=8662804; DOI=10.1074/jbc.271.22.12801;
Bai W., Weigel N.L.;
"Phosphorylation of Ser211 in the chicken progesterone receptor
modulates its transcriptional activity.";
J. Biol. Chem. 271:12801-12806(1996).
[12]
UBIQUITINATION, AND SUBCELLULAR LOCATION.
PubMed=9808061; DOI=10.1016/S0024-3205(98)00417-2;
Syvaala H., Vienonen A., Zhuang Y.-H., Kivineva M., Ylikomi T.,
Tuohimaa P.;
"Evidence for enhanced ubiquitin-mediated proteolysis of the chicken
progesterone receptor by progesterone.";
Life Sci. 63:1505-1512(1998).
-!- 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 {ECO:0000255|PROSITE-
ProRule:PRU00407, ECO:0000269|PubMed:9808061}. Cytoplasm
{ECO:0000269|PubMed:9808061}. Note=Nucleoplasmic shuttling is both
hormone- and cell cycle-dependent. On hormone stimulation,
retained in the cytoplasm in the G(1) and G(2)/M phases (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform A: Nucleus. Cytoplasm. Note=Mainly
nuclear.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=A;
IsoId=P07812-1; Sequence=Displayed;
Name=A';
IsoId=P07812-2; Sequence=VSP_003708, VSP_003709;
Name=B;
IsoId=P07812-3; Sequence=VSP_003707;
Name=B';
IsoId=P07812-4; Sequence=VSP_003707, VSP_003708, VSP_003709;
-!- TISSUE SPECIFICITY: Oviduct and bursa of Fabricius.
{ECO:0000269|PubMed:3453892}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
-!- PTM: Phosphorylation of Ser-529 is sharply increased upon
progesterone treatment, whereas phosphorylation of Ser-210 and
Ser-259 is modestly induced by progesterone.
{ECO:0000269|PubMed:2398063, ECO:0000269|PubMed:7877616,
ECO:0000269|PubMed:8662804}.
-!- PTM: Ubiquitinated. Ubiquitination is increased by progesterone
and represses sumoylation at the same site (By similarity).
{ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y00092; CAA68282.1; -; mRNA.
EMBL; M13972; AAA49034.1; -; mRNA.
EMBL; M37518; AAA49013.1; -; mRNA.
EMBL; M37518; AAA49014.1; -; mRNA.
EMBL; M14278; AAA49035.1; -; mRNA.
EMBL; M14279; AAA49038.1; -; mRNA.
EMBL; M14280; AAA49039.1; -; mRNA.
EMBL; M32732; AAA49011.1; -; mRNA.
EMBL; M31104; AAA49011.1; JOINED; mRNA.
EMBL; M32726; AAA49011.1; JOINED; mRNA.
EMBL; M32727; AAA49011.1; JOINED; mRNA.
EMBL; M32728; AAA49011.1; JOINED; mRNA.
EMBL; M32729; AAA49011.1; JOINED; mRNA.
EMBL; M32730; AAA49011.1; JOINED; mRNA.
EMBL; M32732; AAA49012.1; -; mRNA.
EMBL; M31104; AAA49012.1; JOINED; mRNA.
EMBL; M32726; AAA49012.1; JOINED; mRNA.
EMBL; M32727; AAA49012.1; JOINED; mRNA.
EMBL; M32728; AAA49012.1; JOINED; mRNA.
EMBL; M32729; AAA49012.1; JOINED; mRNA.
EMBL; M32730; AAA49012.1; JOINED; mRNA.
EMBL; M31104; AAA49009.1; -; mRNA.
EMBL; M31104; AAA49010.1; -; mRNA.
PIR; A35466; A35466.
RefSeq; NP_990593.1; NM_205262.1. [P07812-1]
UniGene; Gga.705; -.
ProteinModelPortal; P07812; -.
SMR; P07812; -.
BioGrid; 676458; 8.
DIP; DIP-79N; -.
STRING; 9031.ENSGALP00000027736; -.
ChEMBL; CHEMBL3304; -.
iPTMnet; P07812; -.
PaxDb; P07812; -.
PRIDE; P07812; -.
GeneID; 396198; -.
KEGG; gga:396198; -.
CTD; 5241; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
HOGENOM; HOG000290653; -.
HOVERGEN; HBG007583; -.
InParanoid; P07812; -.
KO; K08556; -.
OrthoDB; EOG091G04YC; -.
PhylomeDB; P07812; -.
SABIO-RK; P07812; -.
PRO; PR:P07812; -.
Proteomes; UP000000539; Unplaced.
Bgee; ENSGALG00000017195; -.
GO; GO:0005829; C:cytosol; IDA:AgBase.
GO; GO:0000790; C:nuclear chromatin; IDA:AgBase.
GO; GO:0016363; C:nuclear matrix; IDA:AgBase.
GO; GO:0005634; C:nucleus; IDA:AgBase.
GO; GO:0032993; C:protein-DNA complex; IDA:AgBase.
GO; GO:0043235; C:receptor complex; IDA:CAFA.
GO; GO:0031490; F:chromatin DNA binding; IDA:AgBase.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0019899; F:enzyme binding; IPI:AgBase.
GO; GO:0030544; F:Hsp70 protein binding; IPI:AgBase.
GO; GO:0051879; F:Hsp90 protein binding; IPI:AgBase.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
GO; GO:1990239; F:steroid hormone binding; IDA:CAFA.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0043627; P:response to estrogen; IDA:AgBase.
GO; GO:0032570; P:response to progesterone; IDA:AgBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR000128; Progest_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF02161; Prog_receptor; 2.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00544; PROGESTRONER.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 2.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Isopeptide bond;
Lipid-binding; Metal-binding; Nucleus; Phosphoprotein; Receptor;
Reference proteome; Steroid-binding; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 786 Progesterone receptor.
/FTId=PRO_0000053699.
DOMAIN 532 766 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 421 486 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 421 441 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 457 481 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 420 Modulating, Pro-Rich.
COMPBIAS 48 80 Asp/Glu-rich (acidic).
MOD_RES 210 210 Phosphoserine.
{ECO:0000269|PubMed:2398063,
ECO:0000269|PubMed:8662804}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000269|PubMed:2398063}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000269|PubMed:2398063,
ECO:0000269|PubMed:7877616}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 294 294 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 294 294 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000250}.
CROSSLNK 385 385 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 127 Missing (in isoform B and isoform B').
{ECO:0000303|PubMed:2303488}.
/FTId=VSP_003707.
VAR_SEQ 452 458 QHNYLCA -> TISYHCS (in isoform A' and
isoform B').
{ECO:0000303|PubMed:2303488}.
/FTId=VSP_003708.
VAR_SEQ 459 786 Missing (in isoform A' and isoform B').
{ECO:0000303|PubMed:2303488}.
/FTId=VSP_003709.
MUTAGEN 210 210 S->A: Decreases transcriptional activity
independently of hormone concentration.
Does not alter hormone binding affinity.
{ECO:0000269|PubMed:8662804}.
MUTAGEN 529 529 S->A: Decreases transcriptional activity
at low hormone concentration. Does not
alter hormone binding affinity.
{ECO:0000269|PubMed:7877616,
ECO:0000269|PubMed:8662804}.
CONFLICT 58 58 E -> DD (in Ref. 2; AAA49013).
{ECO:0000305}.
CONFLICT 134 134 Q -> E (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 148 148 Q -> E (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 480 480 K -> N (in Ref. 2; AAA49013).
{ECO:0000305}.
CONFLICT 489 489 G -> A (in Ref. 2; AAA49013).
{ECO:0000305}.
CONFLICT 577 577 R -> T (in Ref. 2; AAA49013).
{ECO:0000305}.
CONFLICT 642 642 M -> I (in Ref. 2; AAA49013).
{ECO:0000305}.
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


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