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Database: UniProt
Entry: Q9GLW0
LinkDB: Q9GLW0
Original site: Q9GLW0 
ID   PRGR_CANFA              Reviewed;         939 AA.
AC   Q9GLW0;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   29-OCT-2014, entry version 98.
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   Canis familiaris (Dog) (Canis lupus familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615 {ECO:0000312|EMBL:AAG09282.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Mammary gland {ECO:0000269|PubMed:11282275}, and
RC   Uterus {ECO:0000269|PubMed:11282275};
RX   PubMed=11282275; DOI=10.1016/S0960-0760(00)00173-4;
RA   Lantinga-van Leeuwen I.S., van Garderen E., Rutteman G.R., Mol J.A.;
RT   "Cloning and cellular localization of the canine progesterone
RT   receptor: co-localization with growth hormone in the mammary gland.";
RL   J. Steroid Biochem. Mol. Biol. 75:219-228(2000).
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. Progesterone
CC       receptor isoform B (PRB) is involved in activation of c-SRC/MAPK
CC       signaling on hormone stimulation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with SMARD1 and UNC45A. Interacts with CUEDC2;
CC       the interaction promotes ubiquitination, decreases sumoylation,
CC       and repesses transcriptional activity. Interacts with PIAS3; the
CC       interaction promotes sumoylation of PR in a hormone-dependent
CC       manner, inhibits DNA-binding, and alters nuclear export. Interacts
CC       with SP1; the interaction requires ligand-induced phosphorylation
CC       on Ser-349 by ERK1/2-MAPK. Interacts with PRMT2 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00407, ECO:0000269|PubMed:11282275}. Cytoplasm
CC       {ECO:0000269|PubMed:11282275}. Note=Nucleoplasmic shuttling is
CC       both homone- 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B {ECO:0000269|PubMed:11282275};
CC         IsoId=Q9GLW0-1; Sequence=Displayed;
CC       Name=A {ECO:0000269|PubMed:11282275};
CC         IsoId=Q9GLW0-2; Sequence=VSP_050763;
CC   -!- TISSUE SPECIFICITY: Expressed in mammary gland and uterus.
CC       {ECO:0000269|PubMed:11282275}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
CC       a DNA-binding domain and a C-terminal ligand-binding domain.
CC   -!- PTM: Phosphorylated on multiple serine sites. Several of these
CC       sites are hormone-dependent. Phosphorylation on Ser-303 occurs
CC       preferentially on isoform B, is highly hormone-dependent and
CC       modulates ubiquitination and sumoylation on Lys-392.
CC       Phosphorylation on Ser-303 and Ser-349 also requires induction by
CC       hormone. Basal phosphorylation on Ser-200 and Ser-404 is increased
CC       in response to progesterone and can be phosphorylated in vitro by
CC       the CDK2-A1 complex. Increased levels of phosphorylation on Ser-
CC       404 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-303, but not at Ser-200, is impaired during
CC       the G(2)/M phase of the cell cycle. Phosphorylation on Ser-349 by
CC       ERK1/2 MAPK is required for interaction with SP1 (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Sumoylation is hormone-dependent and represses
CC       transcriptional activity. Sumoylation on all three sites is
CC       enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-392,
CC       the main site of sumoylation, is repressed by ubiquitination on
CC       the same site, and modulated by phosphorylation at Ser-303 (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitination is hormone-dependent and represses sumoylation
CC       on the same site. Promoted by MAPK-mediated phosphorylation on
CC       Ser-303 (By similarity). {ECO:0000250}.
CC   -!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is
CC       required for plasma membrane targeting and for rapid intracellular
CC       signaling via ERK and AKT kinases and cAMP generation (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00407}.
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DR   EMBL; AF177470; AAG09282.1; -; mRNA.
DR   RefSeq; NP_001003074.1; NM_001003074.1. [Q9GLW0-1]
DR   UniGene; Cfa.3484; -.
DR   ProteinModelPortal; Q9GLW0; -.
DR   SMR; Q9GLW0; 569-646, 688-938.
DR   STRING; 9615.ENSCAFP00000005906; -.
DR   PRIDE; Q9GLW0; -.
DR   GeneID; 403621; -.
DR   KEGG; cfa:403621; -.
DR   CTD; 5241; -.
DR   eggNOG; NOG273252; -.
DR   HOGENOM; HOG000290653; -.
DR   HOVERGEN; HBG007583; -.
DR   InParanoid; Q9GLW0; -.
DR   KO; K08556; -.
DR   NextBio; 20817126; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IC:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.565.10; -; 1.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR008946; Nucl_hormone_rcpt_ligand-bd.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
DR   InterPro; IPR000128; Progest_rcpt.
DR   InterPro; IPR001723; Str_hrmn_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; 2.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; Cytoplasm; DNA-binding;
KW   Isopeptide bond; Lipid-binding; Lipoprotein; Metal-binding; Nucleus;
KW   Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW   Steroid-binding; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    939       Progesterone receptor.
FT                                /FTId=PRO_0000053692.
FT   DNA_BIND    573    645       Nuclear receptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING     573    593       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING     609    633       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   REGION        1    572       Modulating, Ala/Pro-rich.
FT   REGION      687    939       Steroid-binding.
FT   MOTIF       193    197       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   COMPBIAS     49     59       Poly-Ala.
FT   MOD_RES      20     20       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     141    141       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     200    200       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     303    303       Phosphoserine; by MAPK1. {ECO:0000250}.
FT   MOD_RES     349    349       Phosphoserine; by MAPK. {ECO:0000250}.
FT   MOD_RES     404    404       Phosphoserine; by CDK2. {ECO:0000250}.
FT   MOD_RES     682    682       Phosphoserine. {ECO:0000250}.
FT   CROSSLNK      7      7       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   CROSSLNK    392    392       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate. {ECO:0000250}.
FT   CROSSLNK    392    392       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate. {ECO:0000250}.
FT   CROSSLNK    537    537       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   VAR_SEQ       1    174       Missing (in isoform A).
FT                                {ECO:0000303|PubMed:11282275}.
FT                                /FTId=VSP_050763.
SQ   SEQUENCE   939 AA;  98418 MW;  14AB8E535A64F239 CRC64;
     MTERTGKDAR APHVAGGAPS PAPAAEPESR RRDGGRLRAS QTSDAPRVAA AAAAAAAAAS
     AAPSAPSDRL LFSRRGQGAD PGGKAQDAQP RPDVARADPR LEAASGAGAD SPGPPRQDRG
     PLHGAPSTAL RPAGPGQGRS SPAWEPRSPR CPSGPEPPED PRGARSSQGA ACPLMSRPEG
     KAGDGCGTAG AHKGPPRGLS PSRQPLPLCP GAHAWPGAAG KAATQPAALG VEDEGGFAAE
     GSPGPLLKGK PRPPAGPAAA AGAAPAAPGT APGGTAPVPK EDSRLPAPKG SLAEQDAPAP
     GCSPLATTMM DFIHVPILPL GSAFLAARTR QLLEAETYDA GAFAPPRGSP SAPCAPLAAG
     DFPDCAYPSD AEPKDDAFPL YGDFQPPALK IKEEEEGAEA AARSPRPYLA AGPHSCVFAD
     APPALPALPP LPPRAPSSRP GEGAPAAAAA AGCSASSASS PGPALECVLY KAEGAPPPQG
     PFAAAPCRVP GAGACLLPRD GAAAAASAGA AGASPALYQP LGLGALPQLG YQAAVLKEGL
     PQVYQPYLNY LRPDSDASQS PQYSFESLPQ KICLICGDEA SGCHYGVLTC GSCKVFFKRA
     MEGQHNYLCA GRNDCIVDKI RRKNCPACRL RKCCQAGMVL GGRKFKKFNK VRVMRTLDAV
     ALPQPVGIPN ESQALSQRIS FSPSQDIQLI PPLINLLMSI EPDVIYAGHD NTKPDTSSSL
     LTSLNQLGER QLLSVVKWSK SLPGFRNLHI DDQITLIQYS WMSLMVFGLG WRSYKHVSGQ
     MLYFAPDLIL NEQRMKESSF YSLCLTMWQI PQEFVKLQVS QEEFLCMKVL LLLNTIPLEG
     LRSQNQFEEM RSSYIRELIK AIGLRQKGVV SSSQRFYQLT KLLDNLHDLV KQLHLYCLNT
     FIQSRALSVE FPEMMSEVIA AQLPKILAGM VKPLLFHKK
//
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