NR2C1_MACFA
ID NR2C1_MACFA Reviewed; 603 AA.
AC Q95K90;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Nuclear receptor subfamily 2 group C member 1;
GN Name=NR2C1; ORFNames=QmoA-12557;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Medulla oblongata;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Orphan nuclear receptor. Binds the IR7 element in the
CC promoter of its own gene in an autoregulatory negative feedback
CC mechanism. Primarily repressor of a broad range of genes. Binds to
CC hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half
CC site direct repeat consensus sequences. Together with NR2C2, forms the
CC core of the DRED (direct repeat erythroid-definitive) complex that
CC represses embryonic and fetal globin transcription. Also activator of
CC OCT4 gene expression. May be involved in stem cell proliferation and
CC differentiation. Mediator of retinoic acid-regulated preadipocyte
CC proliferation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer; binds DNA as a
CC heterodimer with NR2C2 required for chromatin remodeling and for
CC binding to promoter regions such as globin DR1 repeats (By similarity).
CC Interacts with ESR1; the interaction prevents homodimerization of ESR1
CC and suppresses its transcriptional activity and cell growth. Interacts
CC with NRIP1 (via its LXXLL motifs); the interaction provides corepressor
CC activity. Interacts with HDAC3 (via the DNA-binding domain). Interacts
CC with HDAC4 (via the DNA-binding domain). Interacts with PIAS1; the
CC interaction is required for sumoylation of NR2C1. Interacts with UBE2I;
CC the interaction is required for sumoylation of NR2C1. Interacts with
CC KAT2B; the interaction acts as a corepressor of gene expression (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC Nucleus, PML body {ECO:0000250}. Note=Recruited by HDAC3, after all-
CC trans retinoic acid stimulated MAPK1-mediated Thr-220 phosphorylation,
CC to PML bodies for subsequent sumoylation. {ECO:0000250}.
CC -!- PTM: Sumoylation requires both PIAS1 and UBE2I. Sumoylation appears to
CC dissociate NR2C1 from the PML nuclear bodies. Enhances the interaction
CC with NRIP1 but inhibits interaction with KAT2B. In proliferating cells,
CC stimulation by all-trans retinoic acid, activation of MAPK1-mediated
CC phosphorylation and recruitment to PML bodies with subsequent
CC sumoylation, suppresses OCT4 expression (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on several serine and threonine residues.
CC Phosphorylation on Thr-220, stimulated by all-trans retinoic acid
CC (atRA) mediates PML location and sumoylation in proliferating cells
CC which then modulates its association with effector molecules, KAT2B and
CC NRIP1. Phosphorylation on Ser-581 by PKC is important for protein
CC stability and function as activator of RARB (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; AB063066; BAB60786.1; -; mRNA.
DR RefSeq; NP_001274567.1; NM_001287638.1.
DR RefSeq; XP_005571940.1; XM_005571883.2.
DR RefSeq; XP_005571941.1; XM_005571884.2.
DR RefSeq; XP_005571942.1; XM_005571885.2.
DR AlphaFoldDB; Q95K90; -.
DR STRING; 9541.XP_005571940.1; -.
DR Ensembl; ENSMFAT00000036133; ENSMFAP00000009708; ENSMFAG00000035305.
DR GeneID; 102136205; -.
DR KEGG; mcf:102136205; -.
DR CTD; 7181; -.
DR VEuPathDB; HostDB:ENSMFAG00000035305; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000158165; -.
DR OMA; RKPIEMS; -.
DR OrthoDB; 278171at2759; -.
DR Proteomes; UP000233100; Chromosome 11.
DR Bgee; ENSMFAG00000035305; Expressed in cerebellum and 13 other tissues.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048386; P:positive regulation of retinoic acid receptor signaling pathway; IEA:Ensembl.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
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 Activator; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..603
FT /note="Nuclear receptor subfamily 2 group C member 1"
FT /id="PRO_0000369403"
FT DOMAIN 348..590
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 110..185
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 113..133
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 149..168
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..178
FT /note="Required for interaction with KAT2B"
FT /evidence="ECO:0000250"
FT REGION 584..603
FT /note="Required for interaction with NRIP1"
FT /evidence="ECO:0000250"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q505F1"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13056"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13056"
FT MOD_RES 222
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q505F1"
FT MOD_RES 581
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q505F1"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P13056"
FT CROSSLNK 588
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P13056"
SQ SEQUENCE 603 AA; 67256 MW; D3D506CB45A2CCA6 CRC64;
MATIEEIAHQ IIEQQMGEIV TEQQTGQKIQ IVTALDHNTQ GKQFILTNHD GSTPSKVILA
RQDSTPGKVF LTPDAAGVNQ LFFTTPDLSA QHLQLLTDNS SPDQGPNKVF DLCVVCGDKA
SGRHYGAVTC EGCKGFFKRS IRKNLVYSCR GSKDCIINKH HRNRCQYCRL QRCIAFGMKQ
DSVQCERKPI EVSREKSSNC AASTEKIYIR KDLRSPLTAT PTFVTDSETT RSTGLLDSGM
FVNIHPSGVK TESTVLMTSD KAESCQGDLS TLASVVTSLA NLGKTKDLSQ NSNEMSMIES
LSNDDTSLCE FQEMQTNGDV SRAFDTLAKA LNPGESTACQ SSVAGMEGSV HLITGDSSIN
YTEKEGPLLS DSHVAFRLTM PSPMPEYLNV HYIGESASRL LFLSMHWALS IPSFQALGQE
NSISLVKAYW NELFTLGLAQ CWQVMNVATI LATFVNCLHN SLQQDKMSTE RRKLLMEHIF
KLQEFCNSMV KLCIDGYEYA YLKAIVLFSP DHPGLENMEQ IEKFQEKAYV EFQDYITKTY
PDDTYRLSRL LLRLPALRLM NATITEELFF KGLIGNIRID SVIPHILKME PADYNSQIIG
HSI
