NR2E3_HUMAN
ID NR2E3_HUMAN Reviewed; 410 AA.
AC Q9Y5X4; B6ZGU0; Q9UHM4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 202.
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; Synonyms=PNR, RNR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Retinoblastoma;
RX PubMed=10220376; DOI=10.1073/pnas.96.9.4814;
RA Kobayashi M., Takezawa S., Hara K., Yu R.T., Umesono Y., Agata K.,
RA Taniwaki M., Yasuda K., Umesono K.;
RT "Identification of a photoreceptor cell-specific nuclear receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4814-4819(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC TISSUE=Retina;
RX PubMed=10611353; DOI=10.1073/pnas.96.26.15149;
RA Chen F., Figueroa D.J., Marmorstein A.D., Zhang Q., Petrukhin K.,
RA Caskey C.T., Austin C.P.;
RT "Retina-specific nuclear receptor: a potential regulator of cellular
RT retinaldehyde-binding protein expressed in retinal pigment epithelium and
RT Muller glial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15149-15154(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
RA Rendtorf N., Vissing H., Shilahtaroglu A., Tommerup N.;
RT "Assignment of the photoreceptor-specific nuclear receptor (PNR) gene to
RT 15q22.32-q24.1 in the Bardet-Biedl Syndrome (BBS4) region.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kobayashi T., Kodani Y., Sawasaki T., Endo Y.;
RT "Comprehensive DNA-binding analysis of human hormone nuclear receptors by
RT fluorescence correlation spectroscopy based on cell-free system.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH CRX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP FUNCTION.
RX PubMed=15689355; DOI=10.1093/hmg/ddi070;
RA Peng G.H., Ahmad O., Ahmad F., Liu J., Chen S.;
RT "The photoreceptor-specific nuclear receptor Nr2e3 interacts with Crx and
RT exerts opposing effects on the transcription of rod versus cone genes.";
RL Hum. Mol. Genet. 14:747-764(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 217-410, SUBUNIT, MUTAGENESIS OF
RP LEU-372 AND LEU-375, FUNCTION, CHARACTERIZATION OF VARIANT ASSOCIATED WITH
RP ESCS GLY-334, AND CHARACTERIZATION OF VARIANTS ESCS PRO-263; GLY-309;
RP GLN-311; PRO-336; VAL-353 AND LYS-407.
RX PubMed=24069298; DOI=10.1371/journal.pone.0074359;
RA Tan M.H., Zhou X.E., Soon F.F., Li X., Li J., Yong E.L., Melcher K.,
RA Xu H.E.;
RT "The crystal structure of the orphan nuclear receptor NR2E3/PNR ligand
RT binding domain reveals a dimeric auto-repressed conformation.";
RL PLoS ONE 8:E74359-E74359(2013).
RN [8]
RP VARIANT ESCS GLN-311, AND CHARACTERIZATION OF VARIANT ESCS GLN-311.
RX PubMed=11071390; DOI=10.1007/s004390000350;
RA Gerber S., Rozet J.-M., Takezawa S., dos Santos L.C., Lopes L.,
RA Gribouval O., Penet C., Perrault I., Ducroq D., Souied E., Jeanpierre M.,
RA Romana S., Frezal J., Ferraz F., Yu-Umesono R., Munnich A., Kaplan J.;
RT "The photoreceptor cell-specific nuclear receptor gene (PNR) accounts for
RT retinitis pigmentosa in the Crypto-Jews from Portugal (Marranos), survivors
RT from the Spanish Inquisition.";
RL Hum. Genet. 107:276-284(2000).
RN [9]
RP VARIANTS ESCS 67-CYS--GLY-69 DEL; GLN-76; TRP-76; HIS-97; TRP-104; LYS-121;
RP SER-234; GLY-309; GLN-311; PRO-385 AND LYS-407, AND VARIANTS GLY-140;
RP THR-163; ILE-232 AND ILE-302.
RX PubMed=10655056; DOI=10.1038/72777;
RA Haider N.B., Jacobson S.G., Cideciyan A.V., Swiderski R., Streb L.M.,
RA Searby C., Beck G., Hockey R., Hanna D.B., Gorman S., Duhl D., Carmi R.,
RA Bennett J., Weleber R.G., Fishman G.A., Wright A.F., Stone E.M.,
RA Sheffield V.C.;
RT "Mutation of a nuclear receptor gene, NR2E3, causes enhanced S cone
RT syndrome, a disorder of retinal cell fate.";
RL Nat. Genet. 24:127-131(2000).
RN [10]
RP VARIANTS ESCS 67-CYS--GLY-69 DEL; HIS-97; GLU-256 AND GLN-311.
RX PubMed=12963616; DOI=10.1001/archopht.121.9.1316;
RA Sharon D., Sandberg M.A., Caruso R.C., Berson E.L., Dryja T.P.;
RT "Shared mutations in NR2E3 in enhanced S-cone syndrome, Goldmann-Favre
RT syndrome, and many cases of clumped pigmentary retinal degeneration.";
RL Arch. Ophthalmol. 121:1316-1323(2003).
RN [11]
RP VARIANTS ESCS 67-CYS--GLY-69 DEL; VAL-88; HIS-97; TRP-104; SER-234;
RP GLU-256; PRO-263; GLY-309; GLN-311; PRO-336; VAL-353 AND LYS-407.
RX PubMed=15459973; DOI=10.1002/humu.9285;
RA Wright A.F., Reddick A.C., Schwartz S.B., Ferguson J.S., Aleman T.S.,
RA Kellner U., Jurklies B., Schuster A., Zrenner E., Wissinger B., Lennon A.,
RA Shu X., Cideciyan A.V., Stone E.M., Jacobson S.G., Swaroop A.;
RT "Mutation analysis of NR2E3 and NRL genes in enhanced S cone syndrome.";
RL Hum. Mutat. 24:439-439(2004).
RN [12]
RP VARIANTS GLN-104 AND GLY-334, AND ASSOCIATION OF VARIANTS GLN-104 AND
RP GLY-334 WITH ESCS.
RX PubMed=16225923; DOI=10.1016/j.ophtha.2005.07.002;
RA Hayashi T., Gekka T., Goto-Omoto S., Takeuchi T., Kubo A., Kitahara K.;
RT "Novel NR2E3 mutations (R104Q, R334G) associated with a mild form of
RT enhanced S-cone syndrome demonstrate compound heterozygosity.";
RL Ophthalmology 112:2115-2115(2005).
RN [13]
RP VARIANT RP37 ARG-56.
RX PubMed=17564971; DOI=10.1086/518426;
RA Coppieters F., Leroy B.P., Beysen D., Hellemans J., De Bosscher K.,
RA Haegeman G., Robberecht K., Wuyts W., Coucke P.J., De Baere E.;
RT "Recurrent mutation in the first zinc finger of the orphan nuclear receptor
RT NR2E3 causes autosomal dominant retinitis pigmentosa.";
RL Am. J. Hum. Genet. 81:147-157(2007).
RN [14]
RP VARIANT ESCS GLN-311, AND VARIANTS LEU-44; GLY-140; THR-163; SER-287 AND
RP ARG-324.
RX PubMed=18294254; DOI=10.1111/j.1399-0004.2008.00963.x;
RA Bernal S., Solans T., Gamundi M.J., Hernan I., de Jorge L., Carballo M.,
RA Navarro R., Tizzano E., Ayuso C., Baiget M.;
RT "Analysis of the involvement of the NR2E3 gene in autosomal recessive
RT retinal dystrophies.";
RL Clin. Genet. 73:360-366(2008).
RN [15]
RP VARIANT RP37 ARG-56, AND VARIANT ESCS GLN-311.
RX PubMed=19006237; DOI=10.1002/humu.20858;
RA Escher P., Gouras P., Roduit R., Tiab L., Bolay S., Delarive T., Chen S.,
RA Tsai C.C., Hayashi M., Zernant J., Merriam J.E., Mermod N., Allikmets R.,
RA Munier F.L., Schorderet D.F.;
RT "Mutations in NR2E3 can cause dominant or recessive retinal degenerations
RT in the same family.";
RL Hum. Mutat. 30:342-351(2009).
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 {ECO:0000269|PubMed:15689355, ECO:0000269|PubMed:24069298}.
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
CC complex that includes NR2E3, PIAS3, NRL, CRX and/or NR1D1. Binds NR1D1.
CC 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. {ECO:0000250, ECO:0000269|PubMed:15689355,
CC ECO:0000269|PubMed:24069298}.
CC -!- INTERACTION:
CC Q9Y5X4; P61964: WDR5; NbExp=5; IntAct=EBI-7216962, EBI-540834;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:15689355}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9Y5X4-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q9Y5X4-2; Sequence=VSP_003679;
CC -!- TISSUE SPECIFICITY: Eye specific; found solely in the outer nuclear
CC layer of the adult neurosensory retina, where the nuclei of cone and
CC rod photoreceptors reside. {ECO:0000269|PubMed:15689355}.
CC -!- PTM: Di- and tri-sumoylated in developing retina. PIAS3-mediated
CC sumoylation promotes repression of cone-specific gene expression and
CC activation of rod-specific genes. Sumoylation on Lys-185 appears to be
CC the main site (By similarity). {ECO:0000250}.
CC -!- DISEASE: Enhanced S cone syndrome (ESCS) [MIM:268100]: Autosomal
CC recessive retinopathy in which patients have increased sensitivity to
CC blue light; perception of blue light is mediated by what is normally
CC the least populous cone photoreceptor subtype, the S (short wavelength,
CC blue) cones. ESCS is also associated with visual loss, with night
CC blindness occurring from early in life, varying degrees of L (long,
CC red)- and M (middle, green)-cone vision, and retinal degeneration.
CC {ECO:0000269|PubMed:10655056, ECO:0000269|PubMed:11071390,
CC ECO:0000269|PubMed:12963616, ECO:0000269|PubMed:15459973,
CC ECO:0000269|PubMed:16225923, ECO:0000269|PubMed:18294254,
CC ECO:0000269|PubMed:19006237, ECO:0000269|PubMed:24069298}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Retinitis pigmentosa 37 (RP37) [MIM:611131]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:17564971,
CC ECO:0000269|PubMed:19006237}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Mutations of the NR2E3 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/nr2e3mut.htm";
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DR EMBL; AF121129; AAD28301.1; -; mRNA.
DR EMBL; AF148128; AAF22227.1; -; mRNA.
DR EMBL; AJ276674; CAB82769.1; -; Genomic_DNA.
DR EMBL; AB307710; BAH02301.1; -; mRNA.
DR EMBL; CH471082; EAW77876.1; -; Genomic_DNA.
DR CCDS; CCDS73750.1; -. [Q9Y5X4-1]
DR CCDS; CCDS73751.1; -. [Q9Y5X4-2]
DR RefSeq; NP_055064.1; NM_014249.3. [Q9Y5X4-1]
DR RefSeq; NP_057430.1; NM_016346.3. [Q9Y5X4-2]
DR PDB; 4LOG; X-ray; 2.70 A; A/B=217-410.
DR PDBsum; 4LOG; -.
DR AlphaFoldDB; Q9Y5X4; -.
DR SMR; Q9Y5X4; -.
DR BioGRID; 115320; 20.
DR IntAct; Q9Y5X4; 11.
DR STRING; 9606.ENSP00000482504; -.
DR BindingDB; Q9Y5X4; -.
DR ChEMBL; CHEMBL4374; -.
DR iPTMnet; Q9Y5X4; -.
DR PhosphoSitePlus; Q9Y5X4; -.
DR BioMuta; NR2E3; -.
DR DMDM; 8928275; -.
DR MassIVE; Q9Y5X4; -.
DR MaxQB; Q9Y5X4; -.
DR PeptideAtlas; Q9Y5X4; -.
DR PRIDE; Q9Y5X4; -.
DR ProteomicsDB; 86529; -. [Q9Y5X4-1]
DR ProteomicsDB; 86530; -. [Q9Y5X4-2]
DR Antibodypedia; 72976; 431 antibodies from 30 providers.
DR DNASU; 10002; -.
DR Ensembl; ENST00000617575.5; ENSP00000482504.1; ENSG00000278570.5. [Q9Y5X4-1]
DR Ensembl; ENST00000621098.1; ENSP00000479962.1; ENSG00000278570.5. [Q9Y5X4-2]
DR GeneID; 10002; -.
DR KEGG; hsa:10002; -.
DR MANE-Select; ENST00000617575.5; ENSP00000482504.1; NM_014249.4; NP_055064.1.
DR UCSC; uc032cik.2; human. [Q9Y5X4-1]
DR CTD; 10002; -.
DR DisGeNET; 10002; -.
DR GeneCards; NR2E3; -.
DR GeneReviews; NR2E3; -.
DR HGNC; HGNC:7974; NR2E3.
DR HPA; ENSG00000278570; Tissue enriched (retina).
DR MalaCards; NR2E3; -.
DR MIM; 268100; phenotype.
DR MIM; 604485; gene.
DR MIM; 611131; phenotype.
DR neXtProt; NX_Q9Y5X4; -.
DR OpenTargets; ENSG00000278570; -.
DR Orphanet; 53540; Goldmann-Favre syndrome.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA31757; -.
DR VEuPathDB; HostDB:ENSG00000278570; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156926; -.
DR HOGENOM; CLU_007368_20_3_1; -.
DR InParanoid; Q9Y5X4; -.
DR OMA; NEEPHTV; -.
DR OrthoDB; 870262at2759; -.
DR PhylomeDB; Q9Y5X4; -.
DR PathwayCommons; Q9Y5X4; -.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR SignaLink; Q9Y5X4; -.
DR SIGNOR; Q9Y5X4; -.
DR BioGRID-ORCS; 10002; 9 hits in 234 CRISPR screens.
DR GeneWiki; Photoreceptor_cell-specific_nuclear_receptor; -.
DR GenomeRNAi; 10002; -.
DR Pharos; Q9Y5X4; Tchem.
DR PRO; PR:Q9Y5X4; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9Y5X4; protein.
DR Bgee; ENSG00000278570; Expressed in buccal mucosa cell and 124 other tissues.
DR ExpressionAtlas; Q9Y5X4; baseline and differential.
DR Genevisible; Q9Y5X4; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
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:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007602; P:phototransduction; TAS:ProtInc.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
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; IPR000003; Retinoid-X_rcpt/HNF4.
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; PR00545; RETINOIDXR.
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 3D-structure; Alternative splicing; Disease variant; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Receptor; Reference proteome;
KW Repressor; Retinitis pigmentosa; Sensory transduction; Transcription;
KW Transcription regulation; Ubl conjugation; Vision; Zinc; Zinc-finger.
FT CHAIN 1..410
FT /note="Photoreceptor-specific nuclear receptor"
FT /id="PRO_0000053599"
FT DOMAIN 169..410
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 44..120
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 47..67
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 83..108
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 118..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 368..410
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10611353"
FT /id="VSP_003679"
FT VARIANT 44
FT /note="S -> L (associated with autosomal recessive
FT retinitis pigmentosa; dbSNP:rs202098481)"
FT /evidence="ECO:0000269|PubMed:18294254"
FT /id="VAR_062768"
FT VARIANT 56
FT /note="G -> R (in RP37; dbSNP:rs121912631)"
FT /evidence="ECO:0000269|PubMed:17564971,
FT ECO:0000269|PubMed:19006237"
FT /id="VAR_037026"
FT VARIANT 67..69
FT /note="Missing (in ESCS)"
FT /evidence="ECO:0000269|PubMed:10655056,
FT ECO:0000269|PubMed:12963616, ECO:0000269|PubMed:15459973"
FT /id="VAR_009265"
FT VARIANT 76
FT /note="R -> Q (in ESCS; dbSNP:rs104894493)"
FT /evidence="ECO:0000269|PubMed:10655056"
FT /id="VAR_009266"
FT VARIANT 76
FT /note="R -> W (in ESCS; dbSNP:rs104894492)"
FT /evidence="ECO:0000269|PubMed:10655056"
FT /id="VAR_009267"
FT VARIANT 88
FT /note="G -> V (in ESCS; dbSNP:rs1278137915)"
FT /evidence="ECO:0000269|PubMed:15459973"
FT /id="VAR_020839"
FT VARIANT 97
FT /note="R -> H (in ESCS; dbSNP:rs1489149705)"
FT /evidence="ECO:0000269|PubMed:10655056,
FT ECO:0000269|PubMed:12963616, ECO:0000269|PubMed:15459973"
FT /id="VAR_010025"
FT VARIANT 104
FT /note="R -> Q (associated with ESCS; dbSNP:rs766096417)"
FT /evidence="ECO:0000269|PubMed:16225923"
FT /id="VAR_062769"
FT VARIANT 104
FT /note="R -> W (in ESCS; dbSNP:rs990307718)"
FT /evidence="ECO:0000269|PubMed:10655056,
FT ECO:0000269|PubMed:15459973"
FT /id="VAR_010026"
FT VARIANT 121
FT /note="E -> K (in ESCS; dbSNP:rs146403122)"
FT /evidence="ECO:0000269|PubMed:10655056"
FT /id="VAR_010027"
FT VARIANT 140
FT /note="E -> G (in dbSNP:rs1805020)"
FT /evidence="ECO:0000269|PubMed:10655056,
FT ECO:0000269|PubMed:18294254"
FT /id="VAR_010028"
FT VARIANT 163
FT /note="M -> T (in dbSNP:rs1805021)"
FT /evidence="ECO:0000269|PubMed:10655056,
FT ECO:0000269|PubMed:18294254"
FT /id="VAR_010029"
FT VARIANT 232
FT /note="V -> I (in dbSNP:rs1805023)"
FT /evidence="ECO:0000269|PubMed:10655056"
FT /id="VAR_010030"
FT VARIANT 234
FT /note="W -> S (in ESCS)"
FT /evidence="ECO:0000269|PubMed:10655056,
FT ECO:0000269|PubMed:15459973"
FT /id="VAR_010031"
FT VARIANT 256
FT /note="A -> E (in ESCS; dbSNP:rs377257254)"
FT /evidence="ECO:0000269|PubMed:12963616,
FT ECO:0000269|PubMed:15459973"
FT /id="VAR_020840"
FT VARIANT 263
FT /note="L -> P (in ESCS; impairs protein folding)"
FT /evidence="ECO:0000269|PubMed:15459973,
FT ECO:0000269|PubMed:24069298"
FT /id="VAR_020841"
FT VARIANT 287
FT /note="G -> S (associated with autosomal recessive
FT retinitis pigmentosa; dbSNP:rs764901119)"
FT /evidence="ECO:0000269|PubMed:18294254"
FT /id="VAR_062770"
FT VARIANT 302
FT /note="V -> I (in dbSNP:rs1805025)"
FT /evidence="ECO:0000269|PubMed:10655056"
FT /id="VAR_010032"
FT VARIANT 309
FT /note="R -> G (in ESCS; impairs protein folding and
FT stability; dbSNP:rs774102273)"
FT /evidence="ECO:0000269|PubMed:10655056,
FT ECO:0000269|PubMed:15459973, ECO:0000269|PubMed:24069298"
FT /id="VAR_010033"
FT VARIANT 311
FT /note="R -> Q (in ESCS; impairs protein folding and
FT stability and hinders the ability to form stable dimers;
FT dbSNP:rs28937873)"
FT /evidence="ECO:0000269|PubMed:10655056,
FT ECO:0000269|PubMed:11071390, ECO:0000269|PubMed:12963616,
FT ECO:0000269|PubMed:15459973, ECO:0000269|PubMed:18294254,
FT ECO:0000269|PubMed:19006237, ECO:0000269|PubMed:24069298"
FT /id="VAR_010034"
FT VARIANT 324
FT /note="K -> R (associated with autosomal recessive
FT retinitis pigmentosa)"
FT /evidence="ECO:0000269|PubMed:18294254"
FT /id="VAR_062771"
FT VARIANT 334
FT /note="R -> G (associated with ESCS; impairs protein
FT folding and stability)"
FT /evidence="ECO:0000269|PubMed:16225923,
FT ECO:0000269|PubMed:24069298"
FT /id="VAR_062772"
FT VARIANT 336
FT /note="L -> P (in ESCS; impairs protein folding and
FT stability; dbSNP:rs752883545)"
FT /evidence="ECO:0000269|PubMed:15459973,
FT ECO:0000269|PubMed:24069298"
FT /id="VAR_020842"
FT VARIANT 353
FT /note="L -> V (in ESCS; impairs protein folding and
FT stability)"
FT /evidence="ECO:0000269|PubMed:15459973,
FT ECO:0000269|PubMed:24069298"
FT /id="VAR_020843"
FT VARIANT 385
FT /note="R -> P (in ESCS; dbSNP:rs766769900)"
FT /evidence="ECO:0000269|PubMed:10655056"
FT /id="VAR_010035"
FT VARIANT 407
FT /note="M -> K (in ESCS; impairs protein folding and
FT stability; dbSNP:rs1303613101)"
FT /evidence="ECO:0000269|PubMed:10655056,
FT ECO:0000269|PubMed:15459973, ECO:0000269|PubMed:24069298"
FT /id="VAR_010036"
FT MUTAGEN 372
FT /note="L->R: Reduces transcription repressor activity."
FT /evidence="ECO:0000269|PubMed:24069298"
FT MUTAGEN 375
FT /note="L->R: Reduces transcription repressor activity."
FT /evidence="ECO:0000269|PubMed:24069298"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 220..237
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:4LOG"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 295..312
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 339..360
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 367..372
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 383..390
FT /evidence="ECO:0007829|PDB:4LOG"
FT HELIX 399..408
FT /evidence="ECO:0007829|PDB:4LOG"
SQ SEQUENCE 410 AA; 44692 MW; D49525830ED0A000 CRC64;
METRPTALMS STVAAAAPAA GAASRKESPG RWGLGEDPTG VSPSLQCRVC GDSSSGKHYG
IYACNGCSGF FKRSVRRRLI YRCQVGAGMC PVDKAHRNQC QACRLKKCLQ AGMNQDAVQN
ERQPRSTAQV HLDSMESNTE SRPESLVAPP APAGRSPRGP TPMSAARALG HHFMASLITA
ETCAKLEPED ADENIDVTSN DPEFPSSPYS SSSPCGLDSI HETSARLLFM AVKWAKNLPV
FSSLPFRDQV ILLEEAWSEL FLLGAIQWSL PLDSCPLLAP PEASAAGGAQ GRLTLASMET
RVLQETISRF RALAVDPTEF ACMKALVLFK PETRGLKDPE HVEALQDQSQ VMLSQHSKAH
HPSQPVRFGK LLLLLPSLRF ITAERIELLF FRKTIGNTPM EKLLCDMFKN
