Swiss-Prot entry
ID ANDR_EULFC STANDARD; PRT; 884 AA.
AC O97776;
DT 30-MAY-2000 (Rel. 39, Created)
DT 30-MAY-2000 (Rel. 39, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Androgen receptor (Dihydrotestosterone receptor).
GN Name=AR; Synonyms=NR3C4;
OS Eulemur fulvus collaris (Collared brown lemur).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirhini;
OC Lemuridae; Eulemur.
OX NCBI_TaxID=47178;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=98404153; PubMed=9732460 [NCBI, ExPASy, EBI, Israel, Japan];
RA Choong C.S., Kemppainen J.A., Wilson E.M.;
RT "Evolution of the primate androgen receptor: a structural basis for
RT disease.";
RL J. Mol. Evol. 47:334-342(1998).
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. Activated,
CC but not phosphorylated, by HIPK3.
CC -!- SUBUNIT: Binds DNA as a homodimer. Interacts with HIPK3 in the
CC presence of androgen. The AR N-terminal poly-Gln region binds Ran
CC resulting in enhancement of AR-mediated transactivation. Ran-
CC binding decreases as the poly-Gln length increases. Interacts with
CC RANBP9 (By similarity).
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 Interaction with RANBP9 is mediated by both the N-terminal domain
CC and the DNA-binding domain.
CC -!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors
CC are thought to be weakly associated with nuclear components;
CC hormone binding greatly increases receptor affinity. The hormone-
CC receptor complex appears to recognize discrete DNA sequences
CC upstream of transcriptional start sites.
CC -!- MISCELLANEOUS: Transcriptional activity is enhanced by binding to
CC RANBP9.
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; U94178; AAC73049.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P10275; 1E3G. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; O97776; 520-593, 634-883.
DR TRANSFAC; T04655; -.
DR InterPro; IPR001103; Andrgn_receptor.
DR InterPro; IPR000536; Hrmon_recept_lig.
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; PF02166; Androgen_recep; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR00521; ANDROGENR.
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 HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; O97776.
DR ProtoNet; O97776.
DR ProtoMap; O97776.
DR PRESAGE; O97776.
DR DIP; O97776.
DR ModBase; O97776.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Receptor; Steroid-binding;
KW Transcription; Transcription regulation; Zinc-finger.
FT DOMAIN 1 522 Modulating (By similarity).
FT DNA_BIND 523 596 Nuclear receptor-type.
FT ZN_FING 524 544 C4-type.
FT DOMAIN 536 626 Interaction with HIPK3 (By similarity).
FT ZN_FING 560 584 C4-type.
FT DOMAIN 655 884 Ligand-binding.
FT DOMAIN 55 58 Poly-Gln.
FT DOMAIN 64 70 Poly-Gln.
FT DOMAIN 116 120 Poly-Ala.
FT DOMAIN 174 178 Poly-Gln.
FT DOMAIN 353 362 Poly-Pro.
FT DOMAIN 379 383 Poly-Ala.
FT DOMAIN 408 411 Poly-Ala.
FT DOMAIN 430 435 Poly-Gly.
SQ SEQUENCE 884 AA; 95611 MW; 18F570E352F4D2BD CRC64;
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAASAAPP GARLQQQQET
SPPQQQQQQQ GEDGSPQAQS RGPTGYLALD EEQQPSQQQS ALECHPESGC VPEPGAAAAA
SKGLQQQPPA PSDEDDSAVP STLSLLGPTF PGLSSCSADL KDILSEAGTM QLLQQQQQEA
VSEGSSSGRA REAAGAPTSS KDSYLGGTST ISDSAKELCK AVSVSMGLGV ETLEHLSPGE
QLRGDCMYAP LLGGPPAVRP TPCAPLAECK GSLLDDSADK GTEEPAEYTP FKGSYTQGLE
GESLGCSGSS EAGSSGTLEL PSTLSLYKSG ALEEAASYQS RDYYNFPLAL AGPPPPPLPP
HPHARIKLEN PLDYGSSWAA AAAQCRFGDL ASLHGGGATG PGSGSPSAAA ASSWHTLFTA
EEGQLYGPCG GGGGGTSEAG AVTPYGYSRP PQGLAGQEGD FPAPDVWYPS GVVSRVPYPS
PSCVKSEMGP WMESYSGPYG DVRLETARDH VLPIDYYFPP QKTCLICGDE ASGCHYGALT
CGSCKVFFKR AAEGKQKYLC ASRNDCTIDK FRRKNCPSCR LRKCYEAGMT LGARKLKKLG
NLKLQEEGEA SSATSPTEES SQKLTVSHIE GYECQPIFLN VLEAIEPGVV CAGHDNNQPD
SFAALLSSLN ELGERQLVHV VKWAKALPGF RNLHVDDQMA VIQYSWMGLM VFAMGWRSFT
NVNSRMLYFA PDLVFNEYRM HKSRMYSQCV RMRHLSQEFG WLQITPQEFL CMKALLLFSI
IPVDGLKNQK FFDELRMNYI KELDRIIACK RKNPTSCSRR FYQLTKLLDS VQPIARELHQ
FTFDLLIKSH MVSVDFPEMM AEIISVQVPK ILSGKVKPIY FHTQ
//