Swiss-Prot entry
ID ANDR_MACMU STANDARD; PRT; 895 AA.
AC Q6QT55; O97891;
DT 01-FEB-2005 (Rel. 46, Created)
DT 01-FEB-2005 (Rel. 46, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Androgen receptor (Dihydrotestosterone receptor).
GN Name=AR; Synonyms=NR3C4;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Chen F., Towler D.;
RT "Full length cDNA encoding rhesus monkey androgen receptor.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE OF 767-876.
RC TISSUE=Prostate;
RX MEDLINE=99225357; PubMed=10208992 [NCBI, ExPASy, EBI, Israel, Japan];
RA Abdelgadir S.E., Roselli C.E., Choate J.V., Resko J.A.;
RT "Androgen receptor messenger ribonucleic acid in brains and
RT pituitaries of male rhesus monkeys: studies on distribution, hormonal
RT control, and relationship to luteinizing hormone secretion.";
RL Biol. Reprod. 60:1251-1256(1999).
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. The AR N-terminal poly-Gln
CC region binds Ran resulting in enhancement of AR-mediated
CC transactivation. Ran-binding decreases as the poly-Gln length
CC increases. Interacts with RANBP9. Interacts with HIPK3 in the
CC presence of androgen (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 (By similarity).
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; AY526325; AAS19691.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF092930; AAD16104.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P06401; 1A28. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; Q6QT55; 531-604, 645-894.
DR InterPro; IPR001103; Andrgn_receptor.
DR InterPro; IPR000536; Hrmon_recept_lig.
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; 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; Q6QT55.
DR ProtoNet; Q6QT55.
DR ProtoMap; Q6QT55.
DR PRESAGE; Q6QT55.
DR DIP; Q6QT55.
DR ModBase; Q6QT55.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Receptor; Steroid-binding;
KW Transcription; Transcription regulation; Zinc-finger.
FT DOMAIN 1 533 Modulating (By similarity).
FT DNA_BIND 534 607 Nuclear receptor-type.
FT ZN_FING 535 555 C4-type.
FT ZN_FING 571 595 C4-type.
FT DOMAIN 666 895 Ligand-binding.
FT DOMAIN 55 62 Poly-Gln.
FT DOMAIN 68 74 Poly-Gln.
FT DOMAIN 178 182 Poly-Gln.
FT DOMAIN 357 366 Poly-Pro.
FT DOMAIN 381 387 Poly-Ala.
FT DOMAIN 434 448 Poly-Gly.
SQ SEQUENCE 895 AA; 96537 MW; 40D2A5BA0CA8B598 CRC64;
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAASAAPP GASLQQQQQQ
QQETSPRQQQ QQQQGEDGSP QAHRRGPTGY LVLDEEQQPS QPQSAPECHP ERGCVPEPGA
AVAAGKGLPQ QLPAPPDEDD SAAPSTLSLL GPTFPGLSSC SADLKDILSE ASTMQLLQQQ
QQEAVSEGSS SGRAREASGA PTSSKDNYLE GTSTISDSAK ELCKAVSVSM GLGVEALEHL
SPGEQLRGDC MYAPVLGVPP AVRPTPCAPL AECKGSLLDD SAGKSTEDTA EYSPFKGGYT
KGLEGESLGC SGSAAAGSSG TLELPSTLSL YKSGALDEAA AYQSRDYYNF PLALAGPPPP
PPPPHPHARI KLENPLDYGS AWAAAAAQCR YGDLASLHGA GAAGPGSGSP SAAASSSWHT
LFTAEEGQLY GPCGGGGGGG GGGGGGAGEA GAVAPYGYTR PPQGLAGQEG DFTAPDVWYP
GGMVSRVPYP SPTCVKSEMG PWMDSYSGPY GDMRLETARD HVLPIDYYFP PQKTCLICGD
EASGCHYGAL TCGSCKVFFK RAAEGKQKYL CASRNDCTID KFRRKNCPSC RLRKCYEAGM
TLGARKLKKL GNLKLQEEGE ASSTTSPTEE TAQKLTVSHI EGYECQPIFL NVLEAIEPGV
VCAGHDNNQP DSFAALLSSL NELGERQLVH VVKWAKALPG FRNLHVDDQM AVIQYSWMGL
MVFAMGWRSF TNVNSRMLYF APDLVFNEYR MHKSRMYSQC VRMRHLSQEF GWLQITPQEF
LCMKALLLFS IIPVDGLKNQ KFFDELRMNY IKELDRIIAC KRKNPTSCSR RFYQLTKLLD
SVQPIARELH QFTFDLLIKS HMVSVDFPEM MAEIISVQVP KILSGKVKPI YFHTQ
//