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Q9TT90

- ANDR_CANFA

UniProt

Q9TT90 - ANDR_CANFA

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Protein

Androgen receptor

Gene
AR, NR3C4
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei693 – 6931Androgen By similarity
Sitei708 – 7081Interaction with coactivator LXXL motif By similarity
Binding sitei740 – 7401Androgen By similarity
Binding sitei865 – 8651Androgen By similarity
Sitei885 – 8851Interaction with coactivator FXXLF motif By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi546 – 61974Nuclear receptorAdd
BLAST
Zinc fingeri547 – 56721NR C4-typeAdd
BLAST
Zinc fingeri583 – 60725NR C4-typeAdd
BLAST

GO - Molecular functioni

  1. androgen receptor activity Source: UniProtKB
  2. beta-catenin binding Source: UniProtKB
  3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
  4. sequence-specific DNA binding Source: InterPro
  5. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  6. steroid binding Source: UniProtKB-KW
  7. transcription regulatory region DNA binding Source: UniProtKB
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. androgen receptor signaling pathway Source: UniProtKB
  2. intracellular receptor signaling pathway Source: BHF-UCL
  3. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  4. negative regulation of integrin biosynthetic process Source: UniProtKB
  5. positive regulation of cell proliferation Source: UniProtKB
  6. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  7. positive regulation of phosphorylation Source: UniProtKB
  8. positive regulation of transcription, DNA-templated Source: UniProtKB
  9. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  10. regulation of establishment of protein localization to plasma membrane Source: UniProtKB
  11. transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Androgen receptor
Alternative name(s):
Dihydrotestosterone receptor
Nuclear receptor subfamily 3 group C member 4
Gene namesi
Name:AR
Synonyms:NR3C4
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity
Note: 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 GNB2L1 By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nuclear chromatin Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 907907Androgen receptorPRO_0000053701Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671Phosphoserine; by CDK9 By similarity
Modified residuei81 – 811Phosphoserine By similarity
Modified residuei228 – 2281Phosphotyrosine; by CSK By similarity
Modified residuei272 – 2721Phosphotyrosine; by CSK and TNK2 By similarity
Modified residuei310 – 3101Phosphotyrosine; by CSK By similarity
Modified residuei349 – 3491Phosphotyrosine; by CSK By similarity
Modified residuei360 – 3601Phosphotyrosine; by CSK By similarity
Modified residuei365 – 3651Phosphotyrosine; by CSK By similarity
Modified residuei366 – 3661Phosphotyrosine; by CSK and TNK2 By similarity
Cross-linki389 – 389Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei396 – 3961Phosphotyrosine; by CSK By similarity
Cross-linki508 – 508Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei522 – 5221Phosphotyrosine; by CSK By similarity
Modified residuei539 – 5391Phosphotyrosine; by CSK By similarity
Modified residuei638 – 6381Phosphoserine; by STK4/MST1 By similarity
Cross-linki833 – 833Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki835 – 835Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei903 – 9031Phosphotyrosine; by CSK By similarity

Post-translational modificationi

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.
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.
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.

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

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, ZNF318 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 GNB2L1/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 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9TT90.
SMRiQ9TT90. Positions 543-616, 651-906.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 545545Modulating By similarityAdd
BLAST
Regioni539 – 907369Interaction with LPXN By similarityAdd
BLAST
Regioni559 – 64991Interaction with HIPK3 By similarityAdd
BLAST
Regioni612 – 907296Interaction with KAT7 By similarityAdd
BLAST
Regioni678 – 907230Ligand-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 6410Poly-Gln
Compositional biasi70 – 767Poly-Gln
Compositional biasi131 – 1344Poly-Gln
Compositional biasi180 – 20223Poly-GlnAdd
BLAST
Compositional biasi329 – 3324Poly-Ser
Compositional biasi375 – 38410Poly-Pro
Compositional biasi399 – 4057Poly-Ala

Domaini

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.

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri547 – 56721NR C4-typeAdd
BLAST
Zinc fingeri583 – 60725NR C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG245477.
HOGENOMiHOG000254783.
HOVERGENiHBG007583.
InParanoidiQ9TT90.
KOiK08557.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR001103. Andrgn_rcpt.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF02166. Androgen_recep. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00521. ANDROGENR.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9TT90-1 [UniParc]FASTAAdd to Basket

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MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAVSAAPP    50
GAHLQQQQQQ QQQQETSPRQ QQQQQQGDDG SPQAQSRGPT GYLALDEEQQ 100
PSQQRSASKG HPESACVPEP GVTSATGKGL QQQQPAPPDE NDSAAPSTLS 150
LLGPTFPGLS SCSTDLKDIL SEAGTMQLLQ QQRQQQQQQQ QQQQQQQQQQ 200
QQEVVSEGSS SGRAREAAGA STSSKDSYLG GSSTISDSAK ELCKAVSVSM 250
GLGVEALEHL SPGEQLRGDC MYAPLLGGPP AVRPCAPLAE CKGSLLDDGP 300
GKGTEETAEY SPFKAGYAKG LDGDSLGCSS SSEAGGSGTL EMPSTLSLYK 350
SGALDEAAAY QSRDYYNFPL SLGGPPPHPP PPHPHTRIKL ENPLDYGSAW 400
AAAAAQCRYG DLASLHGAGA AGPSSGSPSA TTSSSWHTLF TAEEGQLYGP 450
CGGSGGGSAG DGGSVAPYGY TRPPQGLAGQ EGDFPPPDVW YPGGVVSRVP 500
FPSPSCVKSE MGSWMESYSG PYGDMRLETA RDHVLPIDYY FPPQKTCLIC 550
GDEASGCHYG ALTCGSCKVF FKRAAEGKQK YLCASRNDCT IDKFRRKNCP 600
SCRLRKCYEA GMTLGARKLK KLGNLKLQEE GEASNVTSPT EEPTQKLTVS 650
HIEGYECQPI FLNVLEAIEP GVVCAGHDNN QPDSFAALLS SLNELGERQL 700
VHVVKWAKAL PGFRNLHVDD QMAVIQYSWM GLMVFAMGWR SFTNVNSRML 750
YFAPDLVFNE YRMHKSRMYS QCVRMRHLSQ EFGWLQITPQ EFLCMKALLL 800
FSIIPVDGLK NQKFFDELRM NYIKELDRII ACKRKNPTSC SRRFYQLTKL 850
LDSVQPIARE LHQFTFDLLI KSHMVSVDFP EMMAEIISVQ VPKILSGKVK 900
PIYFHTQ 907
Length:907
Mass (Da):98,727
Last modified:May 1, 2000 - v1
Checksum:iC8619F78DD2338AF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1231T → A in AAQ84563. 1 Publication
Sequence conflicti183 – 1831R → Q in AAQ84563. 1 Publication
Sequence conflicti202 – 2021Q → QQ in AAQ84563. 1 Publication
Sequence conflicti823 – 8231I → V in AAQ84563. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF197950 mRNA. Translation: AAF18084.1.
AY271347 mRNA. Translation: AAQ84563.1.
RefSeqiNP_001003053.1. NM_001003053.1.
UniGeneiCfa.141.

Genome annotation databases

GeneIDi403588.
KEGGicfa:403588.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF197950 mRNA. Translation: AAF18084.1 .
AY271347 mRNA. Translation: AAQ84563.1 .
RefSeqi NP_001003053.1. NM_001003053.1.
UniGenei Cfa.141.

3D structure databases

ProteinModelPortali Q9TT90.
SMRi Q9TT90. Positions 543-616, 651-906.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 403588.
KEGGi cfa:403588.

Organism-specific databases

CTDi 367.

Phylogenomic databases

eggNOGi NOG245477.
HOGENOMi HOG000254783.
HOVERGENi HBG007583.
InParanoidi Q9TT90.
KOi K08557.

Miscellaneous databases

NextBioi 20817094.

Family and domain databases

Gene3Di 1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProi IPR001103. Andrgn_rcpt.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view ]
Pfami PF02166. Androgen_recep. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR00521. ANDROGENR.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and functional characterization of the canine androgen receptor."
    Lu B., Smock S.L., Castleberry T.A., Owen T.A.
    Mol. Cell. Biochem. 226:129-140(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Comparision of rat, dog and human androgen receptors."
    Duan W.R., Kelce W.R., Levin S., Blomme E.A.G.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiANDR_CANFA
AccessioniPrimary (citable) accession number: Q9TT90
Secondary accession number(s): Q6WSP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.
Transcriptional activity is enhanced by binding to RANBP9.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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