Swiss-Prot entry
ID ANDR_RAT STANDARD; PRT; 902 AA.
AC P15207; Q63049;
DT 01-APR-1990 (Rel. 14, Created)
DT 01-APR-1990 (Rel. 14, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Androgen receptor (Dihydrotestosterone receptor).
GN Name=Ar; Synonyms=Nr3c4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=89112209; PubMed=3216867 [NCBI, ExPASy, EBI, Israel, Japan];
RA Tan J., Joseph D.R., Quarmby V.E., Lubahn D.B., Sar M., French F.S.,
RA Wilson E.M.;
RT "The rat androgen receptor: primary structure, autoregulation of its
RT messenger ribonucleic acid, and immunocytochemical localization of the
RT receptor protein.";
RL Mol. Endocrinol. 2:1276-1285(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Prostate;
RX MEDLINE=89017168; PubMed=3174628 [NCBI, ExPASy, EBI, Israel, Japan];
RA Chang C., Kokontis J., Liao S.;
RT "Structural analysis of complementary DNA and amino acid sequences of
RT human and rat androgen receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7211-7215(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE, AND VARIANT TFM GLN-735.
RX MEDLINE=90256822; PubMed=2341409 [NCBI, ExPASy, EBI, Israel, Japan];
RA Yarbrough W.G., Quarmby V.E., Simental J.A., Joseph D.R., Sar M.,
RA Lubahn D.B., Olsen K.L., French F.S., Wilson E.M.;
RT "A single base mutation in the androgen receptor gene causes androgen
RT insensitivity in the testicular feminized rat.";
RL J. Biol. Chem. 265:8893-8900(1990).
RN [4]
RP INTERACTION WITH HIPK3, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX MEDLINE=98395052; PubMed=9725910 [NCBI, ExPASy, EBI, Israel, Japan];
RA Moilanen A.-M., Karvonen U., Poukka H., Jaenne O.A., Palvimo J.J.;
RT "Activation of androgen receptor function by a novel nuclear protein
RT kinase.";
RL Mol. Biol. Cell 9:2527-2543(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. 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 (By similarity). Interacts with
CC HIPK3 in the presence of androgen.
CC -!- SUBCELLULAR LOCATION: Nuclear.
CC -!- TISSUE SPECIFICITY: Highest levels in the seminal vesicle, ventral
CC prostate and coagulating gland with lower levels in the kidney and
CC levator ani muscle.
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 -!- DISEASE: Defects in Ar are a cause of androgen insensitivity. Rats
CC with this syndrome are called testicular feminized (TFM).
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; M20133; AAA40733.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M23264; AAA40759.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; J05454; AAA40734.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; B40494; B40494.
DR PDB; 1I37; X-ray; A=643-902. [ExPASy / RCSB]
DR PDB; 1I38; X-ray; A=643-902. [ExPASy / RCSB]
DR TRANSFAC; T00042; -.
DR Ensembl; ENSRNOG00000005639; Rattus_norvegicus
DR RGD; 2147; Ar.
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 CMR; P15207.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P15207.
DR ProtoNet; P15207.
DR ProtoMap; P15207.
DR PRESAGE; P15207.
DR DIP; P15207.
DR ModBase; P15207.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW 3D-structure; Disease mutation; DNA-binding; Nuclear protein;
KW Receptor; Steroid-binding; Transcription; Transcription regulation;
KW Zinc-finger.
FT DOMAIN 1 540 Modulating.
FT DNA_BIND 541 614 Nuclear receptor-type.
FT ZN_FING 542 562 C4-type.
FT DOMAIN 554 644 Interaction with HIPK3.
FT ZN_FING 578 602 C4-type.
FT DOMAIN 673 902 Ligand-binding.
FT DOMAIN 63 67 Poly-Arg.
FT DOMAIN 174 195 Poly-Gln.
FT DOMAIN 370 376 Poly-Pro.
FT DOMAIN 394 400 Poly-Ala.
FT DOMAIN 444 450 Poly-Gly.
FT VARIANT 735 735 R -> Q (in TFM; has only 10-15% of the
FT androgen-binding capacity of wild-type
FT AR).
FT CONFLICT 195 195 Missing (in Ref. 3).
FT CONFLICT 389 389 S -> L (in Ref. 2).
FT HELIX 656 663
FT HELIX 680 703
FT TURN 704 704
FT TURN 706 707
FT HELIX 708 710
FT HELIX 713 738
FT TURN 739 742
FT STRAND 745 748
FT TURN 749 750
FT STRAND 751 753
FT HELIX 755 759
FT TURN 760 762
FT TURN 764 765
FT HELIX 766 779
FT TURN 780 781
FT HELIX 784 794
FT TURN 795 796
FT STRAND 798 800
FT TURN 801 802
FT TURN 805 806
FT HELIX 807 823
FT TURN 824 825
FT TURN 832 833
FT HELIX 834 865
FT TURN 866 866
FT HELIX 867 870
FT TURN 871 871
FT HELIX 876 890
FT TURN 891 892
FT STRAND 894 896
SQ SEQUENCE 902 AA; 98218 MW; 43F4064759FDCBED CRC64;
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REAIQNPGPR HPEAASIAPP GACLQQRQET
SPRRRRRQQH PEDGSPQAHI RGTTGYLALE EEQQPSQQQS ASEGHPESGC LPEPGAATAP
GKGLPQQPPA PPDQDDSAAP STLSLLGPTF PGLSSCSADI KDILSEAGTM QLLQQQQQQQ
QQQQQQQQQQ QQQQQEVISE GSSSVRAREA TGAPSSSKDS YLGGNSTISD SAKELCKAVS
VSMGLGVEAL EHLSPGEQLR GDCMYASLLG GPPAVRPTPC APLAECKGLS LDEGPGKGTE
ETAEYSSFKG GYAKGLEGES LGCSGSSEAG SSGTLEIPSS LSLYKSGAVD EAAAYQNRDY
YNFPLALSGP PHPPPPTHPH ARIKLENPSD YGSAWAAAAA QCRYGDLASL HGGSVAGPST
GSPPATASSS WHTLFTAEEG QLYGPGGGGG SSSPSDAGPV APYGYTRPPQ GLASQEGDFS
ASEVWYPGGV VNRVPYPSPS CVKSEMGPWM ENYSGPYGDM RLDSTRDHVL PIDYYFPPQK
TCLICGDEAS GCHYGALTCG SCKVFFKRAA EGKQKYLCAS RNDCTIDKFR RKNCPSCRLR
KCYEAGMTLG ARKLKKLGNL KLQEEGENSS AGSPTEDPSQ KMTVSHIEGY ECQPIFLNVL
EAIEPGVVCA GHDNNQPDSF AALLSSLNEL GERQLVHVVK WAKALPGFRN LHVDDQMAVI
QYSWMGLMVF AMGWRSFTNV NSRMLYFAPD LVFNEYRMHK SRMYSQCVRM RHLSQEFGWL
QITPQEFLCM KALLLFSIIP VDGLKNQKFF DELRMNYIKE LDRIIACKRK NPTSCSRRFY
QLTKLLDSVQ PIARELHQFT FDLLIKSHMV SVDFPEMMAE IISVQVPKIL SGKVKPIYFH
TQ
//