ID   PRGR_NOTEU              Reviewed;         180 AA.
AC   P79373;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 141.
DE   RecName: Full=Progesterone receptor;
DE            Short=PR;
DE   AltName: Full=Nuclear receptor subfamily 3 group C member 3;
DE   Flags: Fragment;
GN   Name=PGR; Synonyms=NR3C3;
OS   Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX   NCBI_TaxID=9315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Uterus;
RX   PubMed=8807636; DOI=10.1016/0303-7207(96)03807-5;
RA   Lim-Tio S.S., Keightley M.C., Fletcher T.P., Fuller P.J.;
RT   "The molecular basis of RU486 resistance in the Tammar Wallaby, Macropus
RT   eugenii.";
RL   Mol. Cell. Endocrinol. 119:169-174(1996).
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. Transcriptional
CC       activator of several progesteron-dependent promoters in a variety of
CC       cell types. Involved in activation of SRC-dependent MAPK signaling on
CC       hormone stimulation. {ECO:0000250|UniProtKB:P06401}.
CC   -!- SUBUNIT: Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the
CC       interaction promotes ubiquitination, decreases sumoylation, and
CC       represses transcriptional activity. Interacts with PIAS3; the
CC       interaction promotes sumoylation of PR in a hormone-dependent manner,
CC       inhibits DNA-binding, and alters nuclear export. Interacts with SP1;
CC       the interaction requires ligand-induced phosphorylation by ERK1/2-MAPK.
CC       Interacts with PRMT2. Interacts with NCOA2 and NCOA1. Interacts with
CC       KLF9. Interacts with GTF2B (By similarity).
CC       {ECO:0000250|UniProtKB:P06401, ECO:0000250|UniProtKB:Q00175}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling
CC       is both hormone- and cell cycle-dependent. On hormone stimulation,
CC       retained in the cytoplasm in the G(1) and G(2)/M phases (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated on multiple serine sites. Several of these sites
CC       are hormone-dependent (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 is repressed by ubiquitination and
CC       modulated by phosphorylation (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitination is hormone-dependent and represses sumoylation.
CC       {ECO:0000250}.
CC   -!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required
CC       for plasma membrane targeting and for rapid intracellular signaling via
CC       ERK and AKT kinases and cAMP generation (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; S83227; AAB49508.2; -; mRNA.
DR   AlphaFoldDB; P79373; -.
DR   SMR; P79373; -.
DR   HOGENOM; CLU_014081_0_0_1; -.
DR   TreeFam; TF106510; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.565.10; -; 1.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   PRINTS; PR00398; STRDHORMONER.
DR   SUPFAM; SSF48508; SSF48508; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; DNA-binding; Lipid-binding; Lipoprotein; Metal-binding; Nucleus;
KW   Palmitate; Phosphoprotein; Receptor; Steroid-binding; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           <1..>180
FT                   /note="Progesterone receptor"
FT                   /id="PRO_0000053694"
FT   DOMAIN          63..>180
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        <1..16
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         <1..11
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          71..>180
FT                   /note="AF2; mediates transcriptional activation"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   NON_TER         1
FT   NON_TER         180
SQ   SEQUENCE   180 AA;  20480 MW;  D1618A89061C7BF3 CRC64;
     KNCPACRLRK CCQAGMVLGG RKFKKFNKVR VMRALDAVAV PQPVGLPNES QALTQRITFS
     PNQEIQLFPP LINLLLSIEP DVIYAGYDNT KPETSSSLLT SLNHLAERQL LSVVKWSKSL
     PGFRNLHIDD QITLIQYSWM SLMVFGLGWR SYKHVSGQML YFAPDLILNE QRMKESSFYS