ANDR_LITCT
ID ANDR_LITCT Reviewed; 777 AA.
AC Q7T1K4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Androgen receptor;
DE Short=bfAR;
DE AltName: Full=Dihydrotestosterone receptor;
DE AltName: Full=Nuclear receptor subfamily 3 group C member 4;
GN Name=ar; Synonyms=nr3c4;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400 {ECO:0000312|EMBL:AAP85538.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis {ECO:0000269|PubMed:13129498};
RX PubMed=13129498; DOI=10.1016/s0016-6480(03)00215-6;
RA Chattopadhyay S., Park J.H., Seong J.Y., Kwon H.B., Lee K.;
RT "Cloning and characterization of androgen receptor from bullfrog, Rana
RT catesbeiana.";
RL Gen. Comp. Endocrinol. 134:10-17(2003).
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. {ECO:0000250|UniProtKB:P10275, ECO:0000250|UniProtKB:P15207}.
CC -!- SUBUNIT: Binds DNA as a homodimer. Interacts via the ligand-binding
CC domain with LXXLL and FXXLF motifs from coactivator proteins (By
CC similarity). Interacts (via ligand-binding domain) with TRIM68 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm
CC {ECO:0000250|UniProtKB:P10275}.
CC -!- TISSUE SPECIFICITY: Detected in somatic Leydig and Sertoli cells in
CC testis with high level expression. Also detected at lower expression
CC levels in forebrain and heart. {ECO:0000269|PubMed:13129498}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; AY324231; AAP85538.1; -; mRNA.
DR AlphaFoldDB; Q7T1K4; -.
DR SMR; Q7T1K4; -.
DR PRIDE; Q7T1K4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005497; F:androgen binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
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; 2.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
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 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Lipid-binding; Metal-binding; Nucleus; Receptor;
KW Steroid-binding; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..777
FT /note="Androgen receptor"
FT /id="PRO_0000053713"
FT DOMAIN 526..757
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 417..489
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 417..434
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 453..472
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..416
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 53..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 563
FT /ligand="17beta-hydroxy-5alpha-androstan-3-one"
FT /ligand_id="ChEBI:CHEBI:16330"
FT /evidence="ECO:0000250"
FT BINDING 610
FT /ligand="17beta-hydroxy-5alpha-androstan-3-one"
FT /ligand_id="ChEBI:CHEBI:16330"
FT /evidence="ECO:0000250"
FT BINDING 735
FT /ligand="17beta-hydroxy-5alpha-androstan-3-one"
FT /ligand_id="ChEBI:CHEBI:16330"
FT /evidence="ECO:0000250"
FT SITE 578
FT /note="Interaction with coactivator LXXL motif"
FT /evidence="ECO:0000250"
FT SITE 755
FT /note="Interaction with coactivator FXXLF motif"
FT /evidence="ECO:0000250"
SQ SEQUENCE 777 AA; 86436 MW; 33344FD7553D4641 CRC64;
MEVHIGLGGV YKQPPGKMIR GAFENLFLSV REALQGERRS AASLDTSSPI SACVHPHPTW
NEPSTWTEVR GTPWREPQGA QPDPPPCSPR SQAPQFTLSS CTTELKEILG EQGGMPEEGN
SESASKEGYP ESISDSAKEI CKAVSVSLGL SMEALEHLSA AGEWQRGDCM FAGPPHHTMG
AQTCQVAEED KSDTSFSQYR EGAFRRAGQS TYSAGKAPED GSSLPTEDKE QPCTDMALSE
PGSLRSRGME VMPSLTLYKP TAFMEDASAY PGRDYYSFQM ALAPHGRIKV ESPIEFAGSA
WGGPSRYSEF PGFSHCGPSA NWHSLFEEGQ ATASYTDSSL YSYPRSHVPA GPDGEFSAEA
WYPATAMLGR VHMAVPMRPR MTHGWTATLG IRRRLGWTGV ESTFYPIDYY FPPQKPCLSC
EDEASGCHYE ALTCGSCKVF FKRAAEGNQK YLCASRNDCT IDKFRRKNCP SCRLRKCYEA
GMTLGARKLK KLGNLKAQEE LEGSPGQSEG REMPPNMSIP QLEGYSCQPI FLNVLEAIEP
MVVCSGHDNN QPDSFALLLS SLNELGERQL VHVVKWAKAL PGFRNLHVND QMTVIQYSWM
GLMIFAMGWR SFKNVNSRML YFAPDLVFNE YRMHKSRMYS QCVRMRHLSQ EFGWLQVTPE
EFLCDEGPSA LSIIPVEGLK DQKCFDELRM NYIKELDRVI SCKRNNPASS SPRFFNLPKL
LGSVQPIDVN LVQFTFGLFG KAQMVSVDFP EMMSEIISVQ VPKILSGRVK PLYFHSS
