ID G7PNJ1_MACFA Unreviewed; 785 AA.
AC G7PNJ1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Progesterone receptor {ECO:0000256|ARBA:ARBA00013488, ECO:0000256|RuleBase:RU368037};
DE Short=PR {ECO:0000256|RuleBase:RU368037};
DE AltName: Full=Nuclear receptor subfamily 3 group C member 3 {ECO:0000256|ARBA:ARBA00031166, ECO:0000256|RuleBase:RU368037};
GN ORFNames=EGM_06148 {ECO:0000313|EMBL:EHH56686.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH56686.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH56686.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- FUNCTION: Steroid hormone receptor involved in the regulation of
CC eukaryotic gene expression which affects cellular proliferation and
CC differentiation in target tissues. {ECO:0000256|RuleBase:RU368037}.
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:0000256|ARBA:ARBA00003111}.
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 on Ser-345 by
CC ERK1/2-MAPK. Interacts with PRMT2. Interacts with NCOA2 and NCOA1.
CC Interacts with KLF9. Interacts with GTF2B.
CC {ECO:0000256|ARBA:ARBA00025942}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368037}.
CC Cytoplasm {ECO:0000256|RuleBase:RU368037}.
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:0000256|RuleBase:RU368037}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family.
CC {ECO:0000256|ARBA:ARBA00005993, ECO:0000256|RuleBase:RU004334}.
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DR EMBL; CM001289; EHH56686.1; -; Genomic_DNA.
DR AlphaFoldDB; G7PNJ1; -.
DR eggNOG; KOG3575; Eukaryota.
DR Proteomes; UP000009130; Chromosome 14.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd07172; NR_DBD_GR_PR; 1.
DR CDD; cd07074; NR_LBD_PR; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.565.10; Retinoid X Receptor; 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 PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1.
DR PANTHER; PTHR48092:SF6; PROGESTERONE RECEPTOR; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF02161; Prog_receptor; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU368037};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004334};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121,
KW ECO:0000256|RuleBase:RU368037};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004334};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004334};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004334};
KW Steroid-binding {ECO:0000256|ARBA:ARBA00022665,
KW ECO:0000256|RuleBase:RU368037};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004334};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU004334};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004334};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU004334}.
FT DOMAIN 416..491
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 531..765
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 1..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 84462 MW; 13B349AC551D0E25 CRC64;
MTELKAKSPR APHVAGGPPS PEVGSPLLCR PAAGPFQGSQ TSDTLPEVSA IPISLDGLLF
PRPCQGQDPL DEKTQDQQSL SDVEGAYSRA EATRGTGGSS SRPPEKDSGL LDSVLDTLLA
PSGPGQSQPS PPASEVTSSW CLFGPELPED PPAAPATPAT QRVLSPLMSR SGGKAGDSSE
TAAAHKVLPR GLSPSRQLLL PASGSPHWSG APVKPSPLPT AVEVEEEDGS ESEDSAGPLL
KGKPRALGGA AAGGGAAAVP PGAAAGGVAL VPKEDSRFSA PRVALVEQDA PMAPGRSPLA
TTTMDFTHVP ILPLNHALLA ARTRQLLEEE SYDGGAGAAS AFAPPRSSPS ASSTPVAVGD
FPDCAYPPDA DPKDDAYPLY GDFQPPALKI KEEEEGARPD SEASQSPQYS FESLPQKICL
ICGDEASGCH YGVLTCGSCK VFFKRAMEGQ HNYLCAGRND CIVDKIRRKN CPACRLRKCC
QAGMVLGGRK FKKFNKVRVM RALDAVALPQ PVGIPNESQA LSQRFTFSPG QDIQLIPPLI
NLLVSIEPDV IYAGHDNSKP DTSSSLLTSL NQLGERQLLS VVKWSKLLPG FRNLHIDDQI
TLIQYSWMSL MVFGLGWRSY KHVSGQMLYF APDLILNEQR MKESSFYSLC LTMWQIPQEF
VKLQVSQEEF LCMKVLLLLN TIPLEGLRSQ TQFEEMRSSY IRELIKAIGL RQKGVVSSSQ
RFYQLTKLLD NLHDLVKQLH LYCLNTFIQS RALSVEFPEM MSEVIAAQLP KILAGMVKPL
LFHKK
//