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RecName: Full=Nuclear receptor subfamily 2 group C member 1; AltName: Full=Orphan nuclear receptor TR2; AltName: Full=Testicular receptor 2

UniProtKB/Swiss-Prot: Q8VIJ4.1

Identical Proteins FASTA Graphics 

LOCUS       NR2C1_RAT                590 aa            linear   ROD 27-NOV-2024
DEFINITION  RecName: Full=Nuclear receptor subfamily 2 group C member 1;
            AltName: Full=Orphan nuclear receptor TR2; AltName: Full=Testicular
            receptor 2.
ACCESSION   Q8VIJ4
VERSION     Q8VIJ4.1
DBSOURCE    UniProtKB: locus NR2C1_RAT, accession Q8VIJ4;
            class: standard.
            created: Apr 14, 2009.
            sequence updated: Mar 1, 2002.
            annotation updated: Nov 27, 2024.
            xrefs: L26398.1, AAL31316.1, CH473960.2, EDM16889.1, BC061822.1,
            AAH61822.1, NP_665723.1, XP_008763438.1, XP_017450160.1
            xrefs (non-sequence databases): AlphaFoldDB:Q8VIJ4, SMR:Q8VIJ4,
            STRING:10116.ENSRNOP00000071901, BindingDB:Q8VIJ4,
            PhosphoSitePlus:Q8VIJ4, PaxDb:10116-ENSRNOP00000009578,
            Ensembl:ENSRNOT00000009578.5, Ensembl:ENSRNOP00000009578.1,
            Ensembl:ENSRNOG00000006983.8, Ensembl:ENSRNOT00055009689,
            Ensembl:ENSRNOP00055007494, Ensembl:ENSRNOG00055005975,
            Ensembl:ENSRNOT00060008220, Ensembl:ENSRNOP00060006182,
            Ensembl:ENSRNOG00060004922, Ensembl:ENSRNOT00065020082,
            Ensembl:ENSRNOP00065015404, Ensembl:ENSRNOG00065012332,
            GeneID:252924, KEGG:rno:252924, UCSC:RGD:3200, AGR:RGD:3200,
            CTD:7181, RGD:3200, eggNOG:KOG3575, GeneTree:ENSGT00940000158165,
            InParanoid:Q8VIJ4, OMA:QDQGPNK, OrthoDB:5400963at2759,
            PhylomeDB:Q8VIJ4, TreeFam:TF316650, Reactome:R-RNO-383280,
            PRO:PR:Q8VIJ4, Proteomes:UP000002494, Proteomes:UP000234681,
            Bgee:ENSRNOG00000006983, GO:0005634, GO:0016605, GO:0003677,
            GO:0001227, GO:0042826, GO:0004879, GO:0042803, GO:0000978,
            GO:1990837, GO:0008270, GO:0030154, GO:0045892, GO:0000122,
            GO:0048386, CDD:cd06967, CDD:cd06952, FunFam:1.10.565.10:FF:000012,
            FunFam:3.30.50.10:FF:000015, Gene3D:3.30.50.10, Gene3D:1.10.565.10,
            InterPro:IPR035500, InterPro:IPR048245, InterPro:IPR048246,
            InterPro:IPR000536, InterPro:IPR050274, InterPro:IPR001723,
            InterPro:IPR001628, InterPro:IPR013088, PANTHER:PTHR24083,
            PANTHER:PTHR24083:SF49, Pfam:PF00104, Pfam:PF00105, PRINTS:PR00398,
            PRINTS:PR00047, SMART:SM00430, SMART:SM00399, SUPFAM:SSF57716,
            SUPFAM:SSF48508, PROSITE:PS51843, PROSITE:PS00031, PROSITE:PS51030
KEYWORDS    Activator; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
            Phosphoprotein; Receptor; Reference proteome; Repressor;
            Transcription; Transcription regulation; Ubl conjugation; Zinc;
            Zinc-finger.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Ideta,R., Adachi,K., Takeda,H., Chang,C., Yeh,S., Lee,Y. and Su,C.
  TITLE     Gene expression of the androgen repressed rat TR2 orphan receptor:
            a member of steroid receptor superfamily
  JOURNAL   Endocr. J. 3, 277-283 (1995)
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            TISSUE=Testis
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Mural,R.J., Adams,M.D., Myers,E.W., Smith,H.O. and Venter,J.C.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-SEP-2005) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
            STRAIN=Brown Norway
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            TISSUE=Prostate
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
COMMENT     [FUNCTION] Orphan nuclear receptor. Binds the IR7 element in the
            promoter of its own gene in an autoregulatory negative feedback
            mechanism. Primarily repressor of a broad range of genes including
            ESR1 and RARB. Together with NR2C2, forms the core of the DRED
            (direct repeat erythroid-definitive) complex that represses
            embryonic and fetal globin transcription. Binds to hormone response
            elements (HREs) consisting of two 5'-AGGTCA-3' half site direct
            repeat consensus sequences. Also activator of OCT4 gene expression.
            Plays a fundamental role in early embryogenesis and regulates
            embryonic stem cell proliferation and differentiation. Mediator of
            retinoic acid-regulated preadipocyte proliferation (By similarity).
            {ECO:0000250}.
            [SUBUNIT] Homodimer (By similarity). Heterodimer; with NR2C2 which
            is required for chromatin remodeling and for binding to promoter
            regions such as globin DR1 repeats (By similarity). Interacts with
            ESR1; the interaction prevents homodimerization of ESR1 and
            suppresses its transcriptional activity and cell growth. Interacts
            with NRIP1 (via its LXXLL motifs); the interaction provides
            corepressor activity. Interacts with HDAC3 (via the DNA-binding
            domain); the interaction recruits phosphorylated NR2C1 to PML
            bodies for sumoylation. Interacts with HDAC4 (via the DNA-binding
            domain). Interacts with PIAS1; the interaction is required for
            sumoylation of NR2C1. Interacts with UBE2I; the interaction is
            required for sumoylation of NR2C1. Interacts with KAT2B; the
            interaction acts as a corepressor of gene expression (By
            similarity). {ECO:0000250}.
            [SUBCELLULAR LOCATION] Nucleus
            {ECO:0000255|PROSITE-ProRule:PRU00407}. Nucleus, PML body
            {ECO:0000250}. Note=Recruited by HDAC3, after all-trans retinoic
            acid stimulated MAPK1-mediated Thr-210 phosphorylation, to PML
            bodies for subsequent sumoylation. {ECO:0000250}.
            [PTM] Sumoylation requires both PIAS1 and UBE2I. Sumoylation
            appears to dissociate NR2C1 from the PML nuclear bodies. Enhances
            the interaction with NRIP1 but inhibits interaction with KAT2B. In
            proliferating cells, stimulation by all-trans retinoic acid,
            activation of MAPK1-mediated phosphorylation and recruitment to PML
            bodies with subsequent sumoylation, suppresses OCT4 expression (By
            similarity). {ECO:0000250}.
            [PTM] Phosphorylated on several serine and threonine residues.
            Phosphorylation on Thr-210, stimulated by all-trans retinoic acid
            (atRA) mediates PML location and sumoylation in proliferating cells
            which then modulates its association with effector molecules, KAT2B
            and NRIP1. Phosphorylation on Ser-568 by PKC is important for
            protein stability and function as activator of RARB (By
            similarity). {ECO:0000250}.
            [SIMILARITY] Belongs to the nuclear hormone receptor family. NR2
            subfamily. {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
     gene            1..590
                     /gene="Nr2c1"
                     /gene_synonym="Tr2"
     Protein         1..590
                     /product="Nuclear receptor subfamily 2 group C member 1"
                     /note="Orphan nuclear receptor TR2; Testicular receptor 2"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..590
                     /region_name="Mature chain"
                     /note="Nuclear receptor subfamily 2 group C member 1.
                     /id=PRO_0000369405."
     Region          1..166
                     /region_name="Region of interest in the sequence"
                     /note="Required for interaction with KAT2B.
                     /evidence=ECO:0000250."
     Region          96..182
                     /region_name="NR_DBD_TR2_like"
                     /note="DNA-binding domain of the TR2 and TR4 (human
                     testicular receptor 2 and 4) is composed of two C4-type
                     zinc fingers; cd06967"
                     /db_xref="CDD:143525"
     Site            98..173
                     /site_type="DNA binding"
                     /note="Nuclear receptor.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00407."
     Site            order(101,104,118,121,137,143,153,156)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143525"
     Region          101..121
                     /region_name="Zinc finger region"
                     /note="NR C4-type.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00407."
     Site            order(111..113,119..120,122,124,127,130,150..151,154,157,
                     168,171)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143525"
     Region          137..156
                     /region_name="Zinc finger region"
                     /note="NR C4-type.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00407."
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q505F1."
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13056."
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P13056."
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphothreonine; by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q505F1."
     Bond            bond(238)
                     /bond_type="xlink"
                     /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                     G-Cter in SUMO); alternate. /evidence=ECO:0000250."
     Bond            bond(238)
                     /bond_type="xlink"
                     /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                     G-Cter in SUMO2); alternate.
                     /evidence=ECO:0000250|UniProtKB:P13056."
     Region          333..577
                     /region_name="Domain"
                     /note="NR LBD.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01189."
     Region          355..576
                     /region_name="NR_LBD_TR2_like"
                     /note="The ligand binding domain of the orphan nuclear
                     receptors TR4 and TR2; cd06952"
                     /db_xref="CDD:132750"
     Site            order(379..380,384,418,422,425,439,466)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:132750"
     Site            order(389,392,396,401,406..407,409..410,413..414)
                     /site_type="active"
                     /note="putative coactivator recognition site [active]"
                     /db_xref="CDD:132750"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by PKC.
                     /evidence=ECO:0000250|UniProtKB:Q505F1."
     Region          571..590
                     /region_name="Region of interest in the sequence"
                     /note="Required for interaction with NRIP1.
                     /evidence=ECO:0000250."
     Bond            bond(575)
                     /bond_type="xlink"
                     /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                     G-Cter in SUMO2). /evidence=ECO:0000250|UniProtKB:P13056."
ORIGIN      
        1 matieeiahq iidqqmgeiv teqqtgqkiq ivtaldhstq gkqfilanhe gstpgkvflt
       61 tpdaagvnql ffaspdlstp hlqlltensp dqgpnkvfdl cvvcgdkasg rhygaitceg
      121 ckgffkrsir knlvyscrgs kdciinkhhr nrcqycrlqr ciafgmkqds vqcerkpiev
      181 srekssncaa stekiyirkd lrsplaatpt fvtdsetars tglldsgmfv nihpsgikte
      241 pallmtpdka escqgdlgtl asvvtslanl gkakdlshcg gdlpvvqslr ngdtsfgafh
      301 qdiqtngdvs rafdnlakal tpgenpacqs pgesmegsth liagepscme regpllsdsh
      361 vvfrltmpsp mpeylnvhyi gesasrllfl smhwalsips fqalgqensi slvkaywnel
      421 ftlglaqcwq vmnvatilat fvnclhnslq qdkmsperrk llmehifklq efcnsmvklc
      481 idgheyaylk aivlfspdhp glenmeliek fqekayvefq dyitrtypdd tyrlsrlllr
      541 lpalrlmnat iteelffkgl ignvridsvi philkmepad ynsqiighsl
//
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