ID A0A2K5LBA7_CERAT Unreviewed; 831 AA.
AC A0A2K5LBA7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Progesterone receptor {ECO:0000256|RuleBase:RU368037};
DE Short=PR {ECO:0000256|RuleBase:RU368037};
DE AltName: Full=Nuclear receptor subfamily 3 group C member 3 {ECO:0000256|RuleBase:RU368037};
GN Name=PGR {ECO:0000313|Ensembl:ENSCATP00000010238.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000010238.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000010238.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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|RuleBase:RU368037}.
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DR AlphaFoldDB; A0A2K5LBA7; -.
DR Ensembl; ENSCATT00000034347.1; ENSCATP00000010238.1; ENSCATG00000029370.1.
DR GeneTree; ENSGT00940000159713; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000029370; Expressed in heart.
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:1990837; F:sequence-specific double-stranded DNA binding; IEA:UniProt.
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 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; 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; 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:RU368037};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Lipid-binding {ECO:0000256|RuleBase:RU368037};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368037};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU368037};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Steroid-binding {ECO:0000256|RuleBase:RU368037};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU368037};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU368037};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368037};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU368037}.
FT DOMAIN 564..639
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 586..811
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 1..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..437
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 87806 MW; DB1219DCEFC855AD CRC64;
MTELKAKGPR APHVASGPPS PEVGSPLLCR PAAGPFQGSQ TSDTLPEVSA IPISLDGLLF
PRPCQGQDPL DEKTQDQQSL LDVEGAYSRA EATRGTGGSS SRPPEKDSGL LDSVLDTLLA
PSGPGQSQPS PPACEVTSSW CLFGPELPED PPAAPATQRV LSPLMSRSGG KAGDSSGTAA
AHKVLPRGLS PSRQLLLPAS GSPHWSGAPV KPSPQPTAVE VEEEDGSESE DSAGPLLKGK
PRALGGAAAG GGAAAVPPGA AAGGVALVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTT
MDFTHVPILP LNHALLAART RQLLEEESYD GGAGAASAFA PPRSSPSASS TPVAVGDFPD
CAYPPDADPK DDAYPLYGDF QPPALKIKEE EEGAEVSARS PRSYLVAGAN PAAFPDFPLG
PPPPLPPRGP PPRPGEAAVT AAPAGASVSS ASSSGSTLEC ILYKAEGAPP QQGPFAPPPC
KAPGAGGCLL PRDGLPSTSA SAAAAGAAPA LYPALGLNGL PQLGYQAAVL KEGLQQVYPP
YLNYLRPDSE ASQSPQYSFE SLPQKICLIC GDEASGCHYG VLTCGSCKVF FKRAMEGQHN
YLCAGRNDCI VDKIRRKNCP ACRLRKCCQA GMVLGGFRNL HIDDQITLIQ YSWMSLMVFG
LGWRSYKHVS GQMLYFAPDL ILNEQRMKES SFYSLCLTMW QIPQEFVKLQ VSQEEFLCMK
VLLLLNTIPL EGLRSQTQFE EMRSSYIREL IKAIGLRQKG VVSSSQRFYQ LTKLLDNLHD
LVKQLHLYCL NTFIQSRALS VEFPEMMSEV IAAQLPKILA GMVKPLLFHK K
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