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Androgen receptor (Dihydrotestosterone receptor) (Nuclear receptor subfamily 3 group C member 4)

 ANDR_CANLF              Reviewed;         907 AA.
Q9TT90; Q6WSP7;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-SEP-2018, entry version 137.
RecName: Full=Androgen receptor;
AltName: Full=Dihydrotestosterone receptor;
AltName: Full=Nuclear receptor subfamily 3 group C member 4;
Name=AR; Synonyms=NR3C4;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11768233; DOI=10.1023/A:1012752107129;
Lu B., Smock S.L., Castleberry T.A., Owen T.A.;
"Molecular cloning and functional characterization of the canine
androgen receptor.";
Mol. Cell. Biochem. 226:129-140(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Duan W.R., Kelce W.R., Levin S., Blomme E.A.G.;
"Comparision of rat, dog and human androgen receptors.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Steroid hormone receptors are ligand-activated
transcription factors that regulate eukaryotic gene expression and
affect cellular proliferation and differentiation in target
tissues. Transcription factor activity is modulated by bound
coactivator and corepressor proteins. Transcription activation is
down-regulated by NR0B2. Activated, but not phosphorylated, by
HIPK3 and ZIPK/DAPK3. {ECO:0000250|UniProtKB:P10275,
ECO:0000250|UniProtKB:P15207}.
-!- SUBUNIT: Binds DNA as a homodimer. Part of a ternary complex
containing AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and
NR0B2 in the presence of androgen. The ligand binding domain
interacts with KAT7/HBO1 in the presence of dihydrotestosterone.
Interacts with EFCAB6/DJBP, PELP1, PQBP1, RANBP9, RBAK, SPDEF,
SRA1, TGFB1I1 and RREB1. Interacts with ZMIZ1/ZIMP10 and
ZMIZ2/ZMIP7 which both enhance its transactivation activity.
Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts via the
ligand-binding domain with LXXLL and FXXLF motifs from NCOA1,
NCOA2, NCOA3, NCOA4 and MAGEA11. The AR N-terminal poly-Gln region
binds Ran resulting in enhancement of AR-mediated transactivation.
Ran-binding decreases as the poly-Gln length increases. Interacts
with HIP1 (via coiled coil domain). Interacts (via ligand-binding
domain) with TRIM68. Interacts with TNK2. Interacts with USP26.
Interacts with RNF6. Interacts (regulated by RNF6 probably through
polyubiquitination) with RNF14; regulates AR transcriptional
activity. Interacts with PRMT2 and TRIM24. Interacts with RACK1.
Interacts with RANBP10; this interaction enhances
dihydrotestosterone-induced AR transcriptional activity. Interacts
with PRPF6 in a hormone-independent way; this interaction enhances
dihydrotestosterone-induced AR transcriptional activity. Interacts
with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with LPXN.
Interacts with MAK. Part of a complex containing AR, MAK and
NCOA3. Interacts with CRY1. Interacts with CCAR1 and GATA2.
Interacts with ZNF318. Interacts with BUD31. Interacts with
ARID4A. Interacts with ARID4B. {ECO:0000250|UniProtKB:P10275,
ECO:0000250|UniProtKB:P15207, ECO:0000250|UniProtKB:P19091}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}.
Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the
promoter of target genes. Predominantly cytoplasmic in unligated
form but translocates to the nucleus upon ligand-binding. Can also
translocate to the nucleus in unligated form in the presence of
RACK1. {ECO:0000250|UniProtKB:P10275}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain. In
the presence of bound steroid the ligand-binding domain interacts
with the N-terminal modulating domain, and thereby activates AR
transcription factor activity. Agonist binding is required for
dimerization and binding to target DNA. The transcription factor
activity of the complex formed by ligand-activated AR and DNA is
modulated by interactions with coactivator and corepressor
proteins. Interaction with RANBP9 is mediated by both the N-
terminal domain and the DNA-binding domain. Interaction with
EFCAB6/DJBP is mediated by the DNA-binding domain (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated in prostate cancer cells in response to
several growth factors including EGF. Phosphorylation is induced
by c-Src kinase (CSK). Tyr-522 is one of the major phosphorylation
sites and an increase in phosphorylation and Src kinase activity
is associated with prostate cancer progression (By similarity).
Phosphorylation by TNK2 enhances the DNA-binding and
transcriptional activity. Phosphorylation at Ser-67 by CDK9
regulates AR promoter selectivity and cell growth (By similarity).
{ECO:0000250|UniProtKB:P10275}.
-!- PTM: Sumoylated on Lys-389 (major) and Lys-508 (By similarity).
Ubiquitinated. Deubiquitinated by USP26 (By similarity). 'Lys-6'
and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR
transcriptional activity and specificity (By similarity).
{ECO:0000250|UniProtKB:P10275}.
-!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is
required for plasma membrane targeting and for rapid intracellular
signaling via ERK and AKT kinases and cAMP generation (By
similarity). {ECO:0000250|UniProtKB:P10275}.
-!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors
are thought to be weakly associated with nuclear components;
hormone binding greatly increases receptor affinity. The hormone-
receptor complex appears to recognize discrete DNA sequences
upstream of transcriptional start sites.
-!- MISCELLANEOUS: Transcriptional activity is enhanced by binding to
RANBP9.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF197950; AAF18084.1; -; mRNA.
EMBL; AY271347; AAQ84563.1; -; mRNA.
RefSeq; NP_001003053.1; NM_001003053.1.
UniGene; Cfa.141; -.
ProteinModelPortal; Q9TT90; -.
SMR; Q9TT90; -.
STRING; 9615.ENSCAFP00000024499; -.
PaxDb; Q9TT90; -.
PRIDE; Q9TT90; -.
GeneID; 403588; -.
KEGG; cfa:403588; -.
CTD; 367; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
HOGENOM; HOG000254783; -.
HOVERGEN; HBG007583; -.
InParanoid; Q9TT90; -.
KO; K08557; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005497; F:androgen binding; ISS:UniProtKB.
GO; GO:0004882; F:androgen receptor activity; ISS:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:0004879; F:nuclear receptor activity; ISS:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB.
GO; GO:0030522; P:intracellular receptor signaling pathway; ISS:BHF-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
GO; GO:0045720; P:negative regulation of integrin biosynthetic process; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0042327; P:positive regulation of phosphorylation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR001103; Andrgn_rcpt.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF02166; Androgen_recep; 1.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00521; ANDROGENR.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; DNA-binding; Isopeptide bond;
Lipid-binding; Lipoprotein; Metal-binding; Nucleus; Palmitate;
Phosphoprotein; Receptor; Reference proteome; Steroid-binding;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 907 Androgen receptor.
/FTId=PRO_0000053701.
DOMAIN 656 887 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 546 619 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 547 567 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 583 607 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 574 Interaction with ZNF318.
{ECO:0000250|UniProtKB:P19091}.
REGION 1 545 Modulating. {ECO:0000250}.
REGION 539 906 Interaction with LPXN.
{ECO:0000250|UniProtKB:P10275}.
REGION 559 649 Interaction with HIPK3.
{ECO:0000250|UniProtKB:P15207}.
REGION 579 906 Interaction with CCAR1.
{ECO:0000250|UniProtKB:P10275}.
REGION 612 906 Interaction with KAT7.
{ECO:0000250|UniProtKB:P10275}.
COMPBIAS 55 64 Poly-Gln.
COMPBIAS 70 76 Poly-Gln.
COMPBIAS 131 134 Poly-Gln.
COMPBIAS 180 202 Poly-Gln.
COMPBIAS 329 332 Poly-Ser.
COMPBIAS 375 384 Poly-Pro.
COMPBIAS 399 405 Poly-Ala.
BINDING 693 693 Androgen. {ECO:0000250|UniProtKB:P10275}.
BINDING 740 740 Androgen. {ECO:0000250|UniProtKB:P10275}.
BINDING 865 865 Androgen. {ECO:0000250|UniProtKB:P10275}.
SITE 708 708 Interaction with coactivator LXXL and
FXXFY motifs.
{ECO:0000250|UniProtKB:P10275}.
SITE 885 885 Interaction with coactivator FXXLF and
FXXFY motifs.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 67 67 Phosphoserine; by CDK9.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 228 228 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 272 272 Phosphotyrosine; by CSK and TNK2.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 310 310 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 349 349 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 360 360 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 365 365 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 366 366 Phosphotyrosine; by CSK and TNK2.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 396 396 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 522 522 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 539 539 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 638 638 Phosphoserine; by STK4/MST1.
{ECO:0000250|UniProtKB:P10275}.
MOD_RES 903 903 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P10275}.
CROSSLNK 389 389 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 508 508 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 833 833 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10275}.
CROSSLNK 835 835 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10275}.
CONFLICT 123 123 T -> A (in Ref. 2; AAQ84563).
{ECO:0000305}.
CONFLICT 183 183 R -> Q (in Ref. 2; AAQ84563).
{ECO:0000305}.
CONFLICT 202 202 Q -> QQ (in Ref. 2; AAQ84563).
{ECO:0000305}.
CONFLICT 823 823 I -> V (in Ref. 2; AAQ84563).
{ECO:0000305}.
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


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