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Q9TT90

- ANDR_CANFA

UniProt

Q9TT90 - ANDR_CANFA

Protein

Androgen receptor

Gene

AR

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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.By similarity

    Sites

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi546 – 61974Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri547 – 56721NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri583 – 60725NR C4-typePROSITE-ProRule annotationAdd
    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

    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 PROSITE-ProRule annotation. 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.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nuclear chromatin Source: UniProtKB
    3. nucleus Source: UniProtKB

    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 CDK9By similarity
    Modified residuei81 – 811PhosphoserineBy similarity
    Modified residuei228 – 2281Phosphotyrosine; by CSKBy similarity
    Modified residuei272 – 2721Phosphotyrosine; by CSK and TNK2By similarity
    Modified residuei310 – 3101Phosphotyrosine; by CSKBy similarity
    Modified residuei349 – 3491Phosphotyrosine; by CSKBy similarity
    Modified residuei360 – 3601Phosphotyrosine; by CSKBy similarity
    Modified residuei365 – 3651Phosphotyrosine; by CSKBy similarity
    Modified residuei366 – 3661Phosphotyrosine; by CSK and TNK2By similarity
    Cross-linki389 – 389Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei396 – 3961Phosphotyrosine; by CSKBy similarity
    Cross-linki508 – 508Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei522 – 5221Phosphotyrosine; by CSKBy similarity
    Modified residuei539 – 5391Phosphotyrosine; by CSKBy similarity
    Modified residuei638 – 6381Phosphoserine; by STK4/MST1By 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 CSKBy 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.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.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.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.By similarity

    Structurei

    3D structure databases

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

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 545545ModulatingBy similarityAdd
    BLAST
    Regioni539 – 907369Interaction with LPXNBy similarityAdd
    BLAST
    Regioni559 – 64991Interaction with HIPK3By similarityAdd
    BLAST
    Regioni612 – 907296Interaction with KAT7By 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.By similarity

    Sequence similaritiesi

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

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

    « Hide

    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

    Experimental Info

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

    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: October 1, 2014
    This is version 114 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