Swiss-Prot entry
ID ANDR_CANFA STANDARD; PRT; 907 AA.
AC Q9TT90; Q6WSP7;
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 Canis familiaris (Dog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Fissipedia; Canidae;
OC Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=21618348; PubMed=11768233 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1023/A:1012752107129;
RA Lu B., Smock S.L., Castleberry T.A., Owen T.A.;
RT "Molecular cloning and functional characterization of the canine
RT androgen receptor.";
RL Mol. Cell. Biochem. 226:129-140(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Duan W.R., Kelce W.R., Levin S., Blomme E.A.G.;
RT "Comparision of rat, dog and human androgen receptors.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 (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; AF197950; AAF18084.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY271347; AAQ84563.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P10275; 1E3G. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; Q9TT90; 543-616, 657-906.
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; Q9TT90.
DR ProtoNet; Q9TT90.
DR ProtoMap; Q9TT90.
DR PRESAGE; Q9TT90.
DR DIP; Q9TT90.
DR ModBase; Q9TT90.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Receptor; Steroid-binding;
KW Transcription; Transcription regulation; Zinc-finger.
FT DOMAIN 1 545 Modulating (By similarity).
FT DNA_BIND 546 619 Nuclear receptor-type.
FT ZN_FING 547 567 C4-type.
FT DOMAIN 559 649 Interaction with HIPK3 (By similarity).
FT ZN_FING 583 607 C4-type.
FT DOMAIN 678 907 Ligand-binding.
FT DOMAIN 55 64 Poly-Gln.
FT DOMAIN 70 76 Poly-Gln.
FT DOMAIN 131 134 Poly-Gln.
FT DOMAIN 180 202 Poly-Gln.
FT DOMAIN 329 332 Poly-Ser.
FT DOMAIN 375 384 Poly-Pro.
FT DOMAIN 399 405 Poly-Ala.
FT CONFLICT 123 123 T -> A (in Ref. 2).
FT CONFLICT 183 183 R -> Q (in Ref. 2).
FT CONFLICT 202 202 Q -> QQ (in Ref. 2).
FT CONFLICT 823 823 I -> V (in Ref. 2).
SQ SEQUENCE 907 AA; 98727 MW; C8619F78DD2338AF CRC64;
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAVSAAPP GAHLQQQQQQ
QQQQETSPRQ QQQQQQGDDG SPQAQSRGPT GYLALDEEQQ PSQQRSASKG HPESACVPEP
GVTSATGKGL QQQQPAPPDE NDSAAPSTLS LLGPTFPGLS SCSTDLKDIL SEAGTMQLLQ
QQRQQQQQQQ QQQQQQQQQQ QQEVVSEGSS SGRAREAAGA STSSKDSYLG GSSTISDSAK
ELCKAVSVSM GLGVEALEHL SPGEQLRGDC MYAPLLGGPP AVRPCAPLAE CKGSLLDDGP
GKGTEETAEY SPFKAGYAKG LDGDSLGCSS SSEAGGSGTL EMPSTLSLYK SGALDEAAAY
QSRDYYNFPL SLGGPPPHPP PPHPHTRIKL ENPLDYGSAW AAAAAQCRYG DLASLHGAGA
AGPSSGSPSA TTSSSWHTLF TAEEGQLYGP CGGSGGGSAG DGGSVAPYGY TRPPQGLAGQ
EGDFPPPDVW YPGGVVSRVP FPSPSCVKSE MGSWMESYSG PYGDMRLETA RDHVLPIDYY
FPPQKTCLIC GDEASGCHYG ALTCGSCKVF FKRAAEGKQK YLCASRNDCT IDKFRRKNCP
SCRLRKCYEA GMTLGARKLK KLGNLKLQEE GEASNVTSPT EEPTQKLTVS HIEGYECQPI
FLNVLEAIEP GVVCAGHDNN QPDSFAALLS SLNELGERQL VHVVKWAKAL PGFRNLHVDD
QMAVIQYSWM GLMVFAMGWR SFTNVNSRML YFAPDLVFNE YRMHKSRMYS QCVRMRHLSQ
EFGWLQITPQ EFLCMKALLL FSIIPVDGLK NQKFFDELRM NYIKELDRII ACKRKNPTSC
SRRFYQLTKL LDSVQPIARE LHQFTFDLLI KSHMVSVDFP EMMAEIISVQ VPKILSGKVK
PIYFHTQ
//