ANDR_RAT
ID ANDR_RAT Reviewed; 902 AA.
AC P15207; Q63049;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Androgen receptor;
DE AltName: Full=Dihydrotestosterone receptor;
DE AltName: Full=Nuclear receptor subfamily 3 group C member 4;
GN Name=Ar; Synonyms=Nr3c4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3216867; DOI=10.1210/mend-2-12-1276;
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 [MRNA].
RC TISSUE=Prostate;
RX PubMed=3174628; DOI=10.1073/pnas.85.19.7211;
RA Chang C., Kokontis J., Liao S.;
RT "Structural analysis of complementary DNA and amino acid sequences of human
RT and rat androgen receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7211-7215(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TFM GLN-735.
RX PubMed=2341409; DOI=10.1016/s0021-9258(19)38972-0;
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 PubMed=9725910; DOI=10.1091/mbc.9.9.2527;
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).
RN [5]
RP INTERACTION WITH SRA1.
RX PubMed=12350225; DOI=10.1042/bj20020743;
RA Kawashima H., Takano H., Sugita S., Takahara Y., Sugimura K., Nakatani T.;
RT "A novel steroid receptor co-activator protein (SRAP) as an alternative
RT form of steroid receptor RNA-activator gene: expression in prostate cancer
RT cells and enhancement of androgen receptor activity.";
RL Biochem. J. 369:163-171(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-633, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 647-902 OF MUTANT ALA-860 IN
RP COMPLEX WITH DIHYDROTESTOSTERONE.
RX PubMed=11320241; DOI=10.1073/pnas.081565498;
RA Sack J.S., Kish K.F., Wang C., Attar R.M., Kiefer S.E., An Y., Wu G.Y.,
RA Scheffler J.E., Salvati M.E., Krystek S.R. Jr., Weinmann R., Einspahr H.M.;
RT "Crystallographic structures of the ligand-binding domains of the androgen
RT receptor and its T877A mutant complexed with the natural agonist
RT dihydrotestosterone.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4904-4909(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 533-637 IN COMPLEX WITH DNA AND
RP ZINC IONS, AND SUBUNIT.
RX PubMed=15037741; DOI=10.1073/pnas.0401123101;
RA Shaffer P.L., Jivan A., Dollins D.E., Claessens F., Gewirth D.T.;
RT "Structural basis of androgen receptor binding to selective androgen
RT response elements.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4758-4763(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 647-902 OF MUTANT ALA-860 IN
RP COMPLEX WITH SYNTHETIC ANTAGONIST.
RX PubMed=15603938; DOI=10.1016/j.bmcl.2004.10.085;
RA Salvati M.E., Balog A., Shan W., Wei D.D., Pickering D., Attar R.M.,
RA Geng J., Rizzo C.A., Gottardis M.M., Weinmann R., Krystek S.R., Sack J.,
RA An Y., Kish K.;
RT "Structure based approach to the design of bicyclic-1H-isoindole-1,3(2H)-
RT dione based androgen receptor antagonists.";
RL Bioorg. Med. Chem. Lett. 15:271-276(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 647-902 IN COMPLEX WITH SYNTHETIC
RP ANDROGEN ANTAGONIST, AND FUNCTION.
RX PubMed=17181141; DOI=10.1021/jm061101w;
RA Sun C., Robl J.A., Wang T.C., Huang Y., Kuhns J.E., Lupisella J.A.,
RA Beehler B.C., Golla R., Sleph P.G., Seethala R., Fura A., Krystek S.R. Jr.,
RA An Y., Malley M.F., Sack J.S., Salvati M.E., Grover G.J., Ostrowski J.,
RA Hamann L.G.;
RT "Discovery of potent, orally-active, and muscle-selective androgen receptor
RT modulators based on an N-aryl-hydroxybicyclohydantoin scaffold.";
RL J. Med. Chem. 49:7596-7599(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 647-902 IN COMPLEX WITH THE
RP SYNTHETIC AGONIST MBS-564929, AND FUNCTION.
RX PubMed=17008401; DOI=10.1210/en.2006-0843;
RA Ostrowski J., Kuhns J.E., Lupisella J.A., Manfredi M.C., Beehler B.C.,
RA Krystek S.R. Jr., Bi Y., Sun C., Seethala R., Golla R., Sleph P.G.,
RA Fura A., An Y., Kish K.F., Sack J.S., Mookhtiar K.A., Grover G.J.,
RA Hamann L.G.;
RT "Pharmacological and X-ray structural characterization of a novel selective
RT androgen receptor modulator: potent hyperanabolic stimulation of skeletal
RT muscle with hypostimulation of prostate in rats.";
RL Endocrinology 148:4-12(2007).
CC -!- FUNCTION: Steroid hormone receptors are ligand-activated transcription
CC factors that regulate eukaryotic gene expression and affect cellular
CC proliferation and differentiation in target tissues. Transcription
CC factor activity is modulated by bound coactivator and corepressor
CC proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen
CC response elements/ARE on target genes, negatively regulating androgen
CC receptor signaling and androgen-induced cell proliferation.
CC Transcription activation is also down-regulated by NR0B2. Activated,
CC but not phosphorylated, by HIPK3 and ZIPK/DAPK3 (By similarity).
CC {ECO:0000250|UniProtKB:P10275, ECO:0000269|PubMed:17008401,
CC ECO:0000269|PubMed:17181141}.
CC -!- SUBUNIT: Binds DNA as a homodimer. Part of a ternary complex containing
CC AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and NR0B2 in the
CC presence of androgen. The ligand binding domain interacts with
CC KAT7/HBO1 in the presence of dihydrotestosterone. Interacts with
CC EFCAB6/DJBP, PQBP1, RANBP9, RBAK, SPDEF, SRA1, TGFB1I1, ZNF318 and
CC RREB1. Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance
CC its transactivation activity. Interacts with SLC30A9 and RAD54L2/ARIP4.
CC Interacts with MACROD1 (via macro domain) (By similarity). Interacts
CC via the ligand-binding domain with LXXLL and FXXLF motifs from NCOA1,
CC NCOA2, NCOA3, NCOA4 and MAGEA11. The AR N-terminal poly-Gln region
CC binds Ran resulting in enhancement of AR-mediated transactivation. Ran-
CC binding decreases as the poly-Gln length increases. Interacts with HIP1
CC (via coiled coil domain). Interacts (via ligand-binding domain) with
CC TRIM68. Interacts with TNK2. Interacts with USP26. Interacts with RNF6.
CC Interacts (regulated by RNF6 probably through polyubiquitination) with
CC RNF14; regulates AR transcriptional activity. Interacts with PRMT2 and
CC TRIM24. Interacts with RACK1. Interacts with RANBP10; this interaction
CC enhances dihydrotestosterone-induced AR transcriptional activity.
CC Interacts with PRPF6 in a hormone-independent way; this interaction
CC enhances dihydrotestosterone-induced AR transcriptional activity.
CC Interacts with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with
CC LPXN. Interacts with MAK. Part of a complex containing AR, MAK and
CC NCOA3. Interacts with CRY1. Interacts with CCAR1 and GATA2 (By
CC similarity). Interacts with BUD31 (By similarity). Interacts with
CC ARID4A (By similarity). Interacts with ARID4B (By similarity).
CC Interacts (via NR LBD domain) with ZBTB7A; the interaction is direct
CC and androgen-dependent (By similarity). Interacts with NCOR1 (By
CC similarity). Interacts with NCOR2 (By similarity). Interacts with CRY2
CC in a ligand-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P10275, ECO:0000250|UniProtKB:P19091,
CC ECO:0000269|PubMed:11320241, ECO:0000269|PubMed:12350225,
CC ECO:0000269|PubMed:15037741, ECO:0000269|PubMed:15603938,
CC ECO:0000269|PubMed:17008401, ECO:0000269|PubMed:17181141,
CC ECO:0000269|PubMed:9725910}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9725910}. Cytoplasm
CC {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target
CC genes. Predominantly cytoplasmic in unligated form but translocates to
CC the nucleus upon ligand-binding. Can also translocate to the nucleus in
CC unligated form in the presence of RACK1.
CC {ECO:0000250|UniProtKB:P10275}.
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, a
CC DNA-binding domain and a C-terminal ligand-binding domain. In the
CC presence of bound steroid the ligand-binding domain interacts with the
CC N-terminal modulating domain, and thereby activates AR transcription
CC factor activity. Agonist binding is required for dimerization and
CC binding to target DNA. The transcription factor activity of the complex
CC formed by ligand-activated AR and DNA is modulated by interactions with
CC coactivator and corepressor proteins. Interaction with RANBP9 is
CC mediated by both the N-terminal domain and the DNA-binding domain.
CC Interaction with EFCAB6/DJBP is mediated by the DNA-binding domain (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated in prostate cancer cells in response to several
CC growth factors including EGF. Phosphorylation is induced by c-Src
CC kinase (CSK). Tyr-517 is one of the major phosphorylation sites and an
CC increase in phosphorylation and Src kinase activity is associated with
CC prostate cancer progression (By similarity). Phosphorylation by TNK2
CC enhances the DNA-binding and transcriptional activity. Phosphorylation
CC at Ser-61 by CDK9 regulates AR promoter selectivity and cell growth.
CC Phosphorylation by PAK6 leads to AR-mediated transcription inhibition
CC (By similarity). {ECO:0000250|UniProtKB:P10275}.
CC -!- PTM: Sumoylated on Lys-384 (major) and Lys-503 (By similarity).
CC Ubiquitinated. Deubiquitinated by USP26 (By similarity). 'Lys-6' and
CC 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional
CC activity and specificity (By similarity).
CC {ECO:0000250|UniProtKB:P10275}.
CC -!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required
CC for plasma membrane targeting and for rapid intracellular signaling via
CC ERK and AKT kinases and cAMP generation (By similarity).
CC {ECO:0000250|UniProtKB:P10275}.
CC -!- DISEASE: Note=Defects in Ar are a cause of androgen insensitivity. Rats
CC with this syndrome are called testicular feminized (TFM).
CC {ECO:0000269|PubMed:2341409}.
CC -!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors are
CC thought to be weakly associated with nuclear components; hormone
CC binding greatly increases receptor affinity. The hormone-receptor
CC complex appears to recognize discrete DNA sequences upstream of
CC 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. {ECO:0000305}.
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DR EMBL; M20133; AAA40733.1; -; mRNA.
DR EMBL; M23264; AAA40759.1; -; mRNA.
DR EMBL; J05454; AAA40734.1; -; Genomic_DNA.
DR PIR; B40494; B40494.
DR RefSeq; NP_036634.1; NM_012502.1.
DR PDB; 1I37; X-ray; 2.00 A; A=647-902.
DR PDB; 1I38; X-ray; 2.00 A; A=647-902.
DR PDB; 1R4I; X-ray; 3.10 A; A/B=533-637.
DR PDB; 1XNN; X-ray; 2.20 A; A=647-902.
DR PDB; 2IHQ; X-ray; 2.00 A; A=647-902.
DR PDB; 2NW4; X-ray; 3.00 A; A=647-902.
DR PDB; 3G0W; X-ray; 1.95 A; A=647-902.
DR PDBsum; 1I37; -.
DR PDBsum; 1I38; -.
DR PDBsum; 1R4I; -.
DR PDBsum; 1XNN; -.
DR PDBsum; 2IHQ; -.
DR PDBsum; 2NW4; -.
DR PDBsum; 3G0W; -.
DR AlphaFoldDB; P15207; -.
DR SMR; P15207; -.
DR BioGRID; 246396; 3.
DR DIP; DIP-5963N; -.
DR IntAct; P15207; 1.
DR STRING; 10116.ENSRNOP00000009129; -.
DR BindingDB; P15207; -.
DR ChEMBL; CHEMBL3072; -.
DR DrugCentral; P15207; -.
DR GuidetoPHARMACOLOGY; 628; -.
DR iPTMnet; P15207; -.
DR PhosphoSitePlus; P15207; -.
DR PaxDb; P15207; -.
DR PRIDE; P15207; -.
DR GeneID; 24208; -.
DR KEGG; rno:24208; -.
DR CTD; 367; -.
DR RGD; 2147; Ar.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; P15207; -.
DR OrthoDB; 615449at2759; -.
DR PhylomeDB; P15207; -.
DR TreeFam; TF350286; -.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-RNO-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-RNO-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR EvolutionaryTrace; P15207; -.
DR PRO; PR:P15207; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0016607; C:nuclear speck; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005497; F:androgen binding; IMP:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; TAS:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:RGD.
DR GO; GO:0070974; F:POU domain binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0032553; F:ribonucleotide binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060520; P:activation of prostate induction by androgen receptor signaling pathway; ISO:RGD.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IMP:RGD.
DR GO; GO:0048645; P:animal organ formation; ISO:RGD.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; ISO:RGD.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:RGD.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; IEP:RGD.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; ISO:RGD.
DR GO; GO:0007620; P:copulation; IMP:RGD.
DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; ISO:RGD.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISO:RGD.
DR GO; GO:0009566; P:fertilization; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISO:RGD.
DR GO; GO:0030522; P:intracellular receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060599; P:lateral sprouting involved in mammary gland duct morphogenesis; ISO:RGD.
DR GO; GO:0033327; P:Leydig cell differentiation; ISO:RGD.
DR GO; GO:0008049; P:male courtship behavior; IMP:RGD.
DR GO; GO:0048808; P:male genitalia morphogenesis; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0046661; P:male sex differentiation; IMP:RGD.
DR GO; GO:0019102; P:male somatic sex determination; ISO:RGD.
DR GO; GO:0060749; P:mammary gland alveolus development; ISO:RGD.
DR GO; GO:0060571; P:morphogenesis of an epithelial fold; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0045720; P:negative regulation of integrin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISO:RGD.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0060406; P:positive regulation of penile erection; IMP:RGD.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; ISO:RGD.
DR GO; GO:0060736; P:prostate gland growth; IEP:RGD.
DR GO; GO:0048638; P:regulation of developmental growth; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0060685; P:regulation of prostatic bud formation; ISO:RGD.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0019098; P:reproductive behavior; IDA:RGD.
DR GO; GO:0048608; P:reproductive structure development; ISO:RGD.
DR GO; GO:0061458; P:reproductive system development; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:0072520; P:seminiferous tubule development; ISO:RGD.
DR GO; GO:0007338; P:single fertilization; ISO:RGD.
DR GO; GO:0014734; P:skeletal muscle hypertrophy; IMP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IMP:RGD.
DR GO; GO:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; ISO:RGD.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR001103; Andrgn_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF02166; Androgen_recep; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00521; ANDROGENR.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; DNA-binding; Isopeptide bond;
KW Lipid-binding; Lipoprotein; Metal-binding; Nucleus; Palmitate;
KW Phosphoprotein; Receptor; Reference proteome; Steroid-binding;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..902
FT /note="Androgen receptor"
FT /id="PRO_0000053712"
FT DOMAIN 651..882
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 541..614
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 542..562
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 578..602
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..569
FT /note="Interaction with ZNF318"
FT /evidence="ECO:0000250|UniProtKB:P19091"
FT REGION 1..540
FT /note="Modulating"
FT REGION 35..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..901
FT /note="Interaction with LPXN"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT REGION 554..644
FT /note="Interaction with HIPK3"
FT /evidence="ECO:0000269|PubMed:9725910"
FT REGION 574..901
FT /note="Interaction with CCAR1"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT REGION 607..901
FT /note="Interaction with KAT7"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT COMPBIAS 59..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 688
FT /ligand="17beta-hydroxy-5alpha-androstan-3-one"
FT /ligand_id="ChEBI:CHEBI:16330"
FT /evidence="ECO:0000269|PubMed:11320241,
FT ECO:0007744|PDB:1I37"
FT BINDING 735
FT /ligand="17beta-hydroxy-5alpha-androstan-3-one"
FT /ligand_id="ChEBI:CHEBI:16330"
FT /evidence="ECO:0000269|PubMed:11320241,
FT ECO:0007744|PDB:1I37"
FT BINDING 860
FT /ligand="17beta-hydroxy-5alpha-androstan-3-one"
FT /ligand_id="ChEBI:CHEBI:16330"
FT /evidence="ECO:0000269|PubMed:11320241,
FT ECO:0007744|PDB:1I37"
FT SITE 703
FT /note="Interaction with coactivator LXXL and FXXFY motifs"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT SITE 880
FT /note="Interaction with coactivator FXXLF and FXXFY motifs"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 61
FT /note="Phosphoserine; by CDK9"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 221
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 265
FT /note="Phosphotyrosine; by CSK and TNK2"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 305
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 344
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 355
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 360
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 361
FT /note="Phosphotyrosine; by CSK and TNK2"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 391
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 517
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 534
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 898
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 503
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 828
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT CROSSLNK 830
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT VARIANT 735
FT /note="R -> Q (in TFM; has only 10-15% of the androgen-
FT binding capacity of wild-type AR)"
FT /evidence="ECO:0000269|PubMed:2341409"
FT CONFLICT 195
FT /note="Missing (in Ref. 3; AAA40734)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="S -> L (in Ref. 2; AAA40759)"
FT /evidence="ECO:0000305"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:1R4I"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:1R4I"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:1R4I"
FT HELIX 560..570
FT /evidence="ECO:0007829|PDB:1R4I"
FT STRAND 579..582
FT /evidence="ECO:0007829|PDB:1R4I"
FT TURN 588..593
FT /evidence="ECO:0007829|PDB:1R4I"
FT HELIX 595..605
FT /evidence="ECO:0007829|PDB:1R4I"
FT HELIX 655..663
FT /evidence="ECO:0007829|PDB:3G0W"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:1I37"
FT HELIX 680..703
FT /evidence="ECO:0007829|PDB:3G0W"
FT HELIX 708..710
FT /evidence="ECO:0007829|PDB:3G0W"
FT HELIX 713..740
FT /evidence="ECO:0007829|PDB:3G0W"
FT STRAND 743..748
FT /evidence="ECO:0007829|PDB:3G0W"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:3G0W"
FT HELIX 755..760
FT /evidence="ECO:0007829|PDB:3G0W"
FT HELIX 764..779
FT /evidence="ECO:0007829|PDB:3G0W"
FT HELIX 784..795
FT /evidence="ECO:0007829|PDB:3G0W"
FT STRAND 797..800
FT /evidence="ECO:0007829|PDB:3G0W"
FT HELIX 807..826
FT /evidence="ECO:0007829|PDB:3G0W"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:2IHQ"
FT HELIX 833..866
FT /evidence="ECO:0007829|PDB:3G0W"
FT HELIX 867..869
FT /evidence="ECO:0007829|PDB:3G0W"
FT HELIX 876..884
FT /evidence="ECO:0007829|PDB:3G0W"
FT HELIX 886..890
FT /evidence="ECO:0007829|PDB:3G0W"
FT STRAND 893..896
FT /evidence="ECO:0007829|PDB:3G0W"
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
