ID   NR2E3_BOVIN             Reviewed;         411 AA.
AC   Q9TTF0;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Photoreceptor-specific nuclear receptor;
DE   AltName: Full=Nuclear receptor subfamily 2 group E member 3;
DE   AltName: Full=Retina-specific nuclear receptor;
GN   Name=NR2E3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=11725181; DOI=10.1097/00041327-200109000-00003;
RA   Eichen J.G., Dalmau J., Demopoulos A., Wade D., Posner J.B.,
RA   Rosenfeld M.R.;
RT   "The photoreceptor cell-specific nuclear receptor is an autoantigen of
RT   paraneoplastic retinopathy.";
RL   J. Neuroophthalmol. 21:168-172(2001).
RN   [2]
RP   INTERACTION WITH NR1D1, AND IDENTIFICATION IN ROD PHOTORECEPTOR COMPLEX.
RX   PubMed=15190009; DOI=10.1093/hmg/ddh173;
RA   Cheng H., Khanna H., Oh E.C., Hicks D., Mitton K.P., Swaroop A.;
RT   "Photoreceptor-specific nuclear receptor NR2E3 functions as a
RT   transcriptional activator in rod photoreceptors.";
RL   Hum. Mol. Genet. 13:1563-1575(2004).
CC   -!- FUNCTION: Orphan nuclear receptor of retinal photoreceptor cells.
CC       Transcriptional factor that is an activator of rod development and
CC       repressor of cone development. Binds the promoter region of a number of
CC       rod- and cone-specific genes, including rhodopsin, M- and S-opsin and
CC       rod-specific phosphodiesterase beta subunit. Enhances rhodopsin
CC       expression. Represses M- and S-cone opsin expression.
CC   -!- SUBUNIT: Homodimer. Interacts with PIAS3; the interaction sumoylates
CC       NR2E3 and promotes repression of cone-specific gene transcription and
CC       activation of rod-specific genes (By similarity). Component of a rod
CC       photoreceptor complex that includes NR2E3, PIAS3, NRL, CRX and/or
CC       NR1D1. Binds directly in the complex with CRX, PIAS3 and NR1D1 (By
CC       similarity). Interacts (via the DNA-binding domain) with CRX (via its
CC       DNA binding domain); the interaction represses S- and M-cone opsin
CC       expression (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- PTM: Di- and tri-sumoylated in developing retina. PIAS3-mediated
CC       sumoylation is required for repression of cone-specific gene expression
CC       and rod photoreceptor development. Sumoylation on Lys-186 appears to be
CC       the main site.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF15392.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF107729; AAF15392.2; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q9TTF0; -.
DR   SMR; Q9TTF0; -.
DR   STRING; 9913.ENSBTAP00000018926; -.
DR   PaxDb; Q9TTF0; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   InParanoid; Q9TTF0; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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   1: Evidence at protein level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Receptor;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..411
FT                   /note="Photoreceptor-specific nuclear receptor"
FT                   /id="PRO_0000387611"
FT   DOMAIN          170..411
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        36..112
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         39..59
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         75..95
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          108..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        186
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        331
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        338
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  44878 MW;  1CDD3A497C187FF7 CRC64;
     MSSNVAAAVP AAVSASRKES PGRWGLGEEP TGVGPSLQCR VCGDSSSGKH YGIYACNGCS
     GFFKRSVRRR LIYRCQVGAG MCPVDKAHRN QCQACRLKKC LQAGMNQDAV QNERQPRSTA
     QVRMDSVESE TEPRLQPLAT PPALAGPSSR GPTPVSAARA LGPQALMPPG HHHFMASLIT
     AETCTKLEPE DADENIDVTS NDPEFPSSPY SSSSPCALDS IHETSARLLF MAVKWAKNLP
     VFSNLPFRDQ VILLEEAWSE LFLLGAIQWS LPLDNCPLLA LPEASAGGSS QGRLVLASAE
     TRILQETISR FRALAVDPTE FACMKALVLF KPETRGLKDP EHVEALQDQS QVMLSQHSKA
     HHPSQLVRFG KLLLLLPSLR FISSERVELL FFRKTIGNTP MEKLLCDMFK N