Swiss-Prot entry

ID   PRGR_MOUSE     STANDARD;      PRT;   923 AA.
AC   Q00175;
DT   01-DEC-1992 (Rel. 24, Created)
DT   01-DEC-1992 (Rel. 24, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Progesterone receptor (PR).
GN   Name=Pgr; Synonyms=Nr3c3, Pr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; 
OC   Muridae; Murinae; Mus. 
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=91299759; PubMed=2069958 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Schott D.R., Shyamala G., Schneider W., Parry G.;
RT   "Molecular cloning, sequence analyses, and expression of complementary
RT   DNA encoding murine progesterone receptor.";
RL   Biochemistry 30:7014-7020(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 1-9.
RC   STRAIN=129/Sv;
RX   MEDLINE=95100931; PubMed=7802637 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Hagihara K., Wu-Peng X.S., Funabashi T., Kato J., Pfaff D.W.;
RT   "Nucleic acid sequence and DNase hypersensitive sites of the 5' region
RT   of the mouse progesterone receptor gene.";
RL   Biochem. Biophys. Res. Commun. 205:1093-1101(1994).
CC   -!- FUNCTION: The steroid hormones and their receptors are involved in
CC       the regulation of eukaryotic gene expression and affect cellular
CC       proliferation and differentiation in target tissues.
CC   -!- SUBCELLULAR LOCATION: Nuclear.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
CC       a DNA-binding domain and a C-terminal steroid-binding domain.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M68915; AAA39971.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; U12644; AAA66067.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; A39596; A39596.
DR   HSSP; P06401; 1A28. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; Q00175; 553-627, 673-921.
DR   TRANSFAC; T04680; -.
DR   Ensembl; ENSMUSG00000031870; Mus_musculus
DR   MGD; MGI:97567; Pgr.
DR   GeneLynx; Pgr..
DR   SOURCE; Pgr..
DR   GO; GO:0005515; F:protein binding; IPI.
DR   GO; GO:0030879; P:mammary gland development; IMP.
DR   GO; GO:0001542; P:ovulation (sensu Mammalia); IMP.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP.
DR   InterPro; IPR000536; Hrmon_recept_lig.
DR   InterPro; IPR000128; Progest_receptor.
DR   InterPro; IPR001723; Stdhrmn_receptor.
DR   InterPro; IPR008946; Str_ncl_receptor.
DR   InterPro; IPR001628; Znf_C4steroid.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF02161; Prog_receptor; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR00544; PROGESTRONER.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   ProDom; PD000035; Znf_C4steroid; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   CMR; Q00175.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; Q00175.
DR   ProtoNet; Q00175.
DR   ProtoMap; Q00175.
DR   PRESAGE; Q00175.
DR   DIP; Q00175.
DR   ModBase; Q00175.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   DNA-binding; Nuclear protein; Phosphorylation; Receptor;
KW   Steroid-binding; Transcription; Transcription regulation; Zinc-finger.
FT   DOMAIN        1    556       Modulating, Pro-Rich.
FT   DNA_BIND    557    629       Nuclear receptor-type.
FT   ZN_FING     557    577       C4-type.
FT   ZN_FING     593    617       C4-type.
FT   DOMAIN      671    923       Steroid-binding.
FT   DOMAIN      184    188       Nuclear localization signal (Potential).
FT   MOD_RES     233    233       Phosphoserine (by CK) (By similarity).
FT   MOD_RES     542    542       Phosphoserine (by CK) (By similarity).
FT   MOD_RES     666    666       Phosphoserine (By similarity).
FT   MOD_RES     783    783       Phosphoserine (by CK) (By similarity).
SQ   SEQUENCE   923 AA;  99074 MW;  9415F1ED343BEE3F CRC64;
     MTELQAKDPQ VLHTSGASPS PPHIGSPLLA RLDSGPFQGS QHSDVSSVVS PIPISLDGLL
     FPRSCRGPEL PDGKTGDQQS LSDVEGAFSG VEATHREGGR NSRPPEKDSR LLDSVLDSLL
     TPSGPEQSHA SPPACEAITS WCLFGPELPE DPRSVPATKG LLSPLMSRPE IKVGDQSGTG
     RGQKVLPKGL SPPRQLLLPT SGSAHWPGAG VKPSPQPAAG EVEEDSGLET EGSASPLLKS
     KPRALEGTGQ GGGVAANAPS AAPGGVTLVP KEDSRFSAPR VSLEQDSPIA PGRSPLATTV
     VDFIHVPILP LNHALLAART RQLLEGESYD GGATAGPFCP PRSPSAPSTP VPRGDFPDCT
     YPLEGDPKED VFPLYGDFQT PGLKIKEEEE GADAAVRSPR PYLSAGASSS TFPDFPLAPA
     PQAAPSSRPG EAAVAGGPSS AAVSPASSSG SALECILYKA EAPPTQGSFA PLPCKPPAAA
     SCLLPRDSLP AAPGTAAAPA IYQPLGLNGL PQLGYQAAVL KDSLPQVYPP YLNYLRPDSE
     ASQSPQYGFD SLPQKICLIC GDEASGCHYG VLTCGSCKVF FKRAMEGQHN YLCAGRNDCI
     VDKIRRKNCP ACRLRKCCQA GMVLGGRKFK KFNKVRVMRT LDGVALPQSV GLPNESQALS
     QRITFSPNQE IQLVPPLINL LMSIEPDVIY AGHDNTKPDT SSSLLTSLNQ LGERQLLSVV
     KWSKSLPGFR NLHIDDQITL IQYSWMSLMV FGLGWRSYKH VSGQMLYFAP DLILNEQRMK
     ELSFYSLCLT MWQIPQEFVK LQVTHEEFLC MKVLLLLNTI PLEGLRSQSQ FEEMRSSYIR
     ELIKAIGLRQ KGVVPTSQRF YQLTKLLDSL HDLVKQLHLY CLNTFIQSRT LAVEFPEMMS
     EVIAAQLPKI LAGMVKPLLF HKK
//