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PRGR_RABIT
ID   PRGR_RABIT              Reviewed;         930 AA.
AC   P06186;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 171.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3538016; DOI=10.1073/pnas.83.23.9045;
RA   Loosfelt H., Atger M., Misrahi M., Guiochon-Mantel A., Meriel C.,
RA   Logeat F., Benarous R., Milgrom E.;
RT   "Cloning and sequence analysis of rabbit progesterone-receptor
RT   complementary DNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:9045-9049(1986).
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 on Ser-344 by
CC       ERK1/2-MAPK. Interacts with PRMT2. Interacts with NCOA2 and NCOA1.
CC       Interacts with 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   -!- PTM: Phosphorylated on multiple serine sites. Several of these sites
CC       are hormone-dependent. Phosphorylation on Ser-293 is highly hormone-
CC       dependent and modulates ubiquitination and sumoylation on Lys-387.
CC       Phosphorylation on Ser-102 and Ser-344 also requires induction by
CC       hormone. Basal phosphorylation on Ser-82, Ser-191 and Ser-399 is
CC       increased in response to progesterone and can be phosphorylated in
CC       vitro by the CDK2-A1 complex. Increased levels of phosphorylation on
CC       Ser-399 also in the presence of EGF, heregulin, IGF, PMA and FBS.
CC       Phosphorylation at this site by CDK2 is ligand-independent, and
CC       increases nuclear translocation and transcriptional activity.
CC       Phosphorylation at Ser-293, but not at Ser-191, is impaired during the
CC       G(2)/M phase of the cell cycle. Phosphorylation on Ser-344 by ERK1/2
CC       MAPK is required for interaction with SP1 (By similarity).
CC       {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-387, the main site of
CC       sumoylation, is repressed by ubiquitination on the same site, and
CC       modulated by phosphorylation at Ser-293 (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitination is hormone-dependent and represses sumoylation on
CC       the same site. Promoted by MAPK-mediated phosphorylation on Ser-293 (By
CC       similarity). {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}.
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DR   EMBL; M14547; AAA31443.1; -; mRNA.
DR   PIR; A25923; A25923.
DR   RefSeq; NP_001075736.1; NM_001082267.1.
DR   AlphaFoldDB; P06186; -.
DR   SMR; P06186; -.
DR   STRING; 9986.ENSOCUP00000012634; -.
DR   BindingDB; P06186; -.
DR   ChEMBL; CHEMBL3456; -.
DR   DrugCentral; P06186; -.
DR   PRIDE; P06186; -.
DR   Ensembl; ENSOCUT00000014695; ENSOCUP00000012634; ENSOCUG00000014693.
DR   GeneID; 100009094; -.
DR   KEGG; ocu:100009094; -.
DR   CTD; 5241; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000159713; -.
DR   HOGENOM; CLU_014081_0_0_1; -.
DR   InParanoid; P06186; -.
DR   OMA; YPKSSDE; -.
DR   OrthoDB; 615449at2759; -.
DR   PRO; PR:P06186; -.
DR   Proteomes; UP000001811; Chromosome 1.
DR   Bgee; ENSOCUG00000014693; Expressed in uterus and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
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: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:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
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; 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; 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   2: Evidence at transcript level;
KW   Cytoplasm; DNA-binding; Isopeptide bond; Lipid-binding; Lipoprotein;
KW   Metal-binding; Nucleus; Palmitate; Phosphoprotein; Receptor;
KW   Reference proteome; Steroid-binding; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..930
FT                   /note="Progesterone receptor"
FT                   /id="PRO_0000053696"
FT   DOMAIN          676..910
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        566..640
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         568..588
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         604..628
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..565
FT                   /note="Modulating, Pro-Rich"
FT   REGION          1..165
FT                   /note="AF3; mediates transcriptional activation"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..304
FT                   /note="Mediates transcriptional transrepression"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   REGION          334..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..547
FT                   /note="AF1; mediates transcriptional activation"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   REGION          684..930
FT                   /note="AF2; mediates transcriptional activation"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOTIF           56..60
FT                   /note="LXXL motif 1"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOTIF           116..120
FT                   /note="LXXL motif 2"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOTIF           184..188
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        36..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..431
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOD_RES         293
FT                   /note="Phosphoserine; by MAPK1"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOD_RES         344
FT                   /note="Phosphoserine; by MAPK"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOD_RES         399
FT                   /note="Phosphoserine; by CDK2"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   MOD_RES         673
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   CROSSLNK        7
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        387
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        387
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P06401"
FT   CROSSLNK        532
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   930 AA;  98667 MW;  644FF4C13BF2F883 CRC64;
     MTELKAKEPR APHVAGGAPS PTEVGSQLLG RPDPGPFQGS QTSEASSVVS AIPISLDGLL
     FPRPCQGQNP PDGKTQDPPS LSDVEGAFPG VEAPEGAGDS SSRPPEKDSG LLDSVLDTLL
     APSGPGQSHA SPATCEAISP WCLFGPDLPE DPRAAPATKG VLAPLMSRPE DKAGDSSGTA
     AAHKVLPRGL SPSRQLLLPS SGSPHWPAVK PSPQPAAVQV DEEDSSESEG TVGPLLKGQP
     RALGGTAAGG GAAPVASGAA AGGVALVPKE DSRFSAPRVS LAEQDAPVAP GRSPLATSVV
     DFIHVPILPL NHAFLATRTR QLLEGESYDG GAAAASPFVP QRGSPSASST PVAGGDFPDC
     TYPPDAEPKD DAFPLYGDFQ PPALKIKEEE EAAEAAARSP RTYLVAGANP AAFPDFQLAA
     PPPPSLPPRV PSSRPGEAAV AASPGSASVS SSSSSGSTLE CILYKAEGAP PQQGPFAPLP
     CKPPGAGACL LPRDGLPSTS ASGAAAGAAP ALYPTLGLNG LPQLGYQAAV LKEGLPQVYT
     PYLNYLRPDS EASQSPQYSF ESLPQKICLI CGDEASGCHY GVLTCGSCKV FFKRAMEGQH
     NYLCAGRNDC IVDKIRRKNC PACRLRKCCQ AGMVLGGRKF KKFNKVRVMR ALDAVALPQP
     VGIPNESQRI TFSPSQEIQL IPPLINLLMS IEPDVIYAGH DNTKPDTSSS LLTSLNQLGE
     RQLLSVVKWS KSLPGFRNLH IDDQITLIQY SWMSLMVFGL GWRSYKHVSG QMLYFAPDLI
     LNEQRMKESS FYSLCLTMWQ IPQEFVKLQV SQEEFLCMKV LLLLNTIPLE GLRSQSQFEE
     MRSSYIRELI KAIGLRQKGV VSSSQRFYQL TKLLDNLHDL VKQLHLYCLN TFIQSRALSV
     EFPEMMSEVI AAQLPKILAG MVKPLLFHKK
 
 
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