Swiss-Prot entry

ID   Q8HXA4_RABIT PRELIMINARY;      PRT;   475 AA.
AC   Q8HXA4;
DT   01-MAR-2003 (TrEMBLrel. 23, Created)
DT   01-MAR-2003 (TrEMBLrel. 23, Last sequence update)
DT   01-FEB-2005 (TrEMBLrel. 29, Last annotation update)
DE   PPAR gamma 1 (PPAR gamma 3).
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. 
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Guan Y., Zhang Y., Schneider A., Davis L., Breyer R.M., Breyer M.D.;
RT   "PPAR gamma activity is associated with renal microvasculature.";
RL   Am. J. Physiol. 281:F1036-F1046(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Guan Y., Zhang Y., Schneider A., Davis L., Breyer R.M., Breyer M.D.;
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor that binds peroxisome proliferators such as
CC       hypolipidemic drugs and fatty acids. Once activated by a ligand,
CC       the receptor binds to a promoter element in the gene for acyl-CoA
CC       oxidase and activates its transcription. It therefore controls the
CC       peroxisomal beta-oxidation pathway of fatty acids. Key regulator
CC       of adipocyte differentiation and glucose homeostasis (By
CC       similarity).
CC   -!- SUBUNIT: Forms a heterodimer with the retinoic acid receptor RXR-
CC       alpha called adipocyte-specific transcription factor ARF6.
CC       Interacts with NCOA6 coactivator, leading to a strong increase in
CC       transcription of target genes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nuclear (By similarity).
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family.
DR   EMBL; AY166780; AAO13014.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AY166781; AAO13015.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; Q96J12; 1NYX. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   GO; GO:0005634; C:nucleus; IEA.
DR   GO; GO:0003707; F:steroid hormone receptor activity; IEA.
DR   GO; GO:0003700; F:transcription factor activity; IEA.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA.
DR   GO; GO:0006350; P:transcription; IEA.
DR   InterPro; IPR003074; 1Cnucl_receptor.
DR   InterPro; IPR003077; 1Cnucl_receptorG.
DR   InterPro; IPR000536; Hrmon_recept_lig.
DR   InterPro; IPR001723; Stdhrmn_receptor.
DR   InterPro; IPR001628; Znf_C4steroid.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR01288; PROXISOMEPAR.
DR   PRINTS; PR01291; PROXISOMPAGR.
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_RECEPTOR; 1.
DR   HOVERGEN [Family / Alignment / Tree]
DR   ProtoMap; Q8HXA4.
DR   PRESAGE; Q8HXA4.
DR   ModBase; Q8HXA4.
DR   SMR; Q8HXA4.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   DNA-binding; Metal-binding; Nuclear protein; Receptor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
SQ   SEQUENCE   475 AA;  54259 MW;  3AA0155A717CC564 CRC64;
     MVDTEMPFWP TNFGIGSVDL SVMDDHSHSF DIKPFTTVDF SSISAPHYED LPFARADPMV
     ADYKYDLKLQ EYQSAIKVEP ASPPYYSEKT QLYNKTHEEP SNSLMAIECR VCGDKASGFH
     YGVHACEGCK GFFRRPIRLK LIYDRCDLNC RIHKKSRNKC QYCRFQKCLA VGMSHNAIRF
     GRMPGAEKEK LLAEISSDID QLNPESADLR ALAKHLYDSY IKSFPLTKAK ARAILTGKTT
     DKSPFVIYDM NSLMMGEDKI KFKHITPLQE QSKEVAIRIF QGCQFRSVEA VQEITEYAKN
     IPGFVSLDLN DQVTLLKYGV HEIIYTMLAS LMNKDGVLIS EGQGFMTREF LKSLRKPFGD
     FMEPKFEFAV KFNALELDDS DLAIFIAVII LSGDRPGLLN VKPIEDIQDN LLQALELQLK
     LNHPEASQLF AKLLQKMTDL RQIVTEHVQL LQVIKKTETD MSLHPLLQEI YKDLY
//