Swiss-Prot entry

ID   ANDR_MOUSE     STANDARD;      PRT;   899 AA.
AC   P19091;
DT   01-NOV-1990 (Rel. 16, Created)
DT   01-NOV-1990 (Rel. 16, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Androgen receptor (Dihydrotestosterone receptor).
GN   Name=Ar; Synonyms=Nr3c4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; 
OC   Muridae; Murinae; Mus. 
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c;
RX   MEDLINE=90386642; PubMed=2403358 [NCBI, ExPASy, EBI, Israel, Japan];
RA   He W.W., Fischer L.M., Sun S., Bilhartz D.L., Zhu X., Young C.Y.F.,
RA   Kelley D.B., Tindall D.J.;
RT   "Molecular cloning of androgen receptors from divergent species with a
RT   polymerase chain reaction technique: complete cDNA sequence of the
RT   mouse androgen receptor and isolation of androgen receptor cDNA probes
RT   from dog, guinea pig and clawed frog.";
RL   Biochem. Biophys. Res. Commun. 171:697-704(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=91133433; PubMed=2178222 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Gaspar M.L., Meo T., Tosi M.;
RT   "Structure and size distribution of the androgen receptor mRNA in
RT   wild-type and Tfm/Y mutant mice.";
RL   Mol. Endocrinol. 4:1600-1610(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=91354214; PubMed=1883336 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Faber P.W., King A., van Rooij H.C.J., Brinkmann A.O., de Both N.J.,
RA   Trapman J.;
RT   "The mouse androgen receptor. Functional analysis of the protein and
RT   characterization of the gene.";
RL   Biochem. J. 278:269-278(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=92017874; PubMed=1681426 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Charest N.J., Zhou Z., Lubahn D.B., Olsen K.L., Wilson E.M.,
RA   French F.S.;
RT   "A frameshift mutation destabilizes androgen receptor messenger RNA in
RT   the Tfm mouse.";
RL   Mol. Endocrinol. 5:573-581(1991).
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; S56585; AAB19916.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; X53779; CAA37795.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; M37890; AAA37234.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; X59592; CAA42160.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; A35895; A35895.
DR   HSSP; P10275; 1E3G. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; P19091; 535-608, 649-898.
DR   TRANSFAC; T00041; -.
DR   Ensembl; ENSMUSG00000046532; Mus_musculus
DR   MGD; MGI:88064; Ar.
DR   GeneLynx; Ar..
DR   SOURCE; Ar..
DR   GO; GO:0005737; C:cytoplasm; IDA.
DR   GO; GO:0005634; C:nucleus; IDA.
DR   GO; GO:0005515; F:protein binding; IPI.
DR   GO; GO:0003700; F:transcription factor activity; IDA.
DR   GO; GO:0008151; P:cell growth and/or maintenance; IDA.
DR   GO; GO:0001701; P:embryonic development (sensu Mammalia); IMP.
DR   GO; GO:0008584; P:male gonad development; IMP.
DR   GO; GO:0045449; P:regulation of transcription; IDA.
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; P19091.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; P19091.
DR   ProtoNet; P19091.
DR   ProtoMap; P19091.
DR   PRESAGE; P19091.
DR   DIP; P19091.
DR   ModBase; P19091.
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    537       Modulating (By similarity).
FT   DNA_BIND    538    611       Nuclear receptor-type.
FT   ZN_FING     539    559       C4-type.
FT   DOMAIN      551    641       Interaction with HIPK3 (By similarity).
FT   ZN_FING     575    599       C4-type.
FT   DOMAIN      670    899       Ligand-binding.
FT   DOMAIN       63     67       Poly-Arg.
FT   DOMAIN      174    193       Poly-Gln.
FT   DOMAIN      367    373       Poly-Pro.
FT   DOMAIN      391    397       Poly-Ala.
FT   DOMAIN      441    447       Poly-Gly.
SQ   SEQUENCE   899 AA;  98194 MW;  FD9EE07C07F7A568 CRC64;
     MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REAIQNPGPR HPEAANIAPP GACLQQRQET
     SPRRRRRQQH TEDGSPQAHI RGPTGYLALE EEQQPSQQQA ASEGHPESSC LPEPGAATAP
     GKGLPQQPPA PPDQDDSAAP STLSLLGPTF PGLSSCSADI KDILNEAGTM QLLQQQQQQQ
     QHQQQHQQHQ QQQEVISEGS SARAREATGA PSSSKDSYLG GNSTISDSAK ELCKAVSVSM
     GLGVEALEHL SPGEQLRGDC MYASLLGGPP AVRPTPCAPL PECKGLPLDE GPGKSTEETA
     EYSSFKGGYA KGLEGESLGC SGSSEAGSSG TLEIPSSLSL YKSGALDEAA AYQNRDYYNF
     PLALSGPPHP PPPTHPHARI KLENPLDYGS AWAAAAAQCR YGDLGSLHGG SVAGPSTGSP
     PATTSSSWHT LFTAEEGQLY GPGGGGGSSS PSDAGPVAPY GYTRPPQGLT SQESDYSASE
     VWYPGGVVNR VPYPSPNCVK SEMGPWMENY SGPYGDMRLD STRDHVLPID YYFPPQKTCL
     ICGDEASGCH YGALTCGSCK VFFKRAAEGK QKYLCASRND CTIDKFRRKN CPSCRLRKCY
     EAGMTLGARK LKKLGNLKLQ EEGENSNAGS PTEDPSQKMT VSHIEGYECQ PIFLNVLEAI
     EPGVVCAGHD NNQPDSFAAL LSSLNELGER QLVHVVKWAK ALPGFRNLHV DDQMAVIQYS
     WMGLMVFAMG WRSFTNVNSR MLYFAPDLVF NEYRMHKSRM YSQCVRMRHL SQEFGWLQIT
     PQEFLCMKAL LLFSIIPVDG LKNQKFFDEL RMNYIKELDR IIACKRKNPT SCSRRFYQLT
     KLLDSVQPIA RELHQFTFDL LIKSHMVSVD FPEMMAEIIS VQVPKILSGK VKPIYFHTQ
//