NRL_MOUSE
ID NRL_MOUSE Reviewed; 237 AA.
AC P54846;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Neural retina-specific leucine zipper protein;
DE Short=NRL;
GN Name=Nrl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Retina;
RX PubMed=8288222; DOI=10.1006/geno.1993.1458;
RA Farjo Q., Jackson A.U., Xu J., Gryzenia M., Skolnick C., Agarwal N.,
RA Swaroop A.;
RT "Molecular characterization of the murine neural retina leucine zipper
RT gene, Nrl.";
RL Genomics 18:216-222(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=11477108; DOI=10.1074/jbc.m105855200;
RA Swain P.K., Hicks D., Mears A.J., Apel I.J., Smith J.E., John S.K.,
RA Hendrickson A., Milam A.H., Swaroop A.;
RT "Multiple phosphorylated isoforms of NRL are expressed in rod
RT photoreceptors.";
RL J. Biol. Chem. 276:36824-36830(2001).
RN [4]
RP DISRUPTION PHENOTYPE, AND SUMOYLATION AT LYS-20 AND LYS-24.
RX PubMed=20551322; DOI=10.1074/jbc.m110.142810;
RA Roger J.E., Nellissery J., Kim D.S., Swaroop A.;
RT "Sumoylation of bZIP transcription factor NRL modulates target gene
RT expression during photoreceptor differentiation.";
RL J. Biol. Chem. 285:25637-25644(2010).
CC -!- FUNCTION: Acts as a transcriptional activator which regulates the
CC expression of several rod-specific genes, including RHO and PDE6B.
CC Functions also as a transcriptional coactivator, stimulating
CC transcription mediated by the transcription factor CRX and NR2E3. Binds
CC in a sequence-specific manner to the rhodopsin promoter.
CC {ECO:0000250|UniProtKB:P54845}.
CC -!- SUBUNIT: Interacts with FIZ1; this interaction represses
CC transactivation. Interacts (via the leucine-zipper domain) with CRX.
CC {ECO:0000250|UniProtKB:P54845}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54845}. Nucleus
CC {ECO:0000250|UniProtKB:P54845}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level)
CC (PubMed:11477108). {ECO:0000269|PubMed:11477108}.
CC -!- DOMAIN: The minimal transactivation domain (MTD) is conserved across
CC the MAF family, it may activate transcription by recruiting TBP and
CC associated factors at the promoters of target genes.
CC {ECO:0000250|UniProtKB:P54845}.
CC -!- PTM: Disumoylated at Lys-20. Sumoylation modulates the transcriptional
CC activity of NRL on RHO and NR2E3 promoters, and is required for normal
CC rod differentiation. {ECO:0000269|PubMed:20551322}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:P54845}.
CC -!- DISRUPTION PHENOTYPE: Photoreceptor precursors in retina produce only
CC cones that primarily express S-opsin. {ECO:0000269|PubMed:20551322}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; L14935; AAA16843.1; -; mRNA.
DR EMBL; BC031440; AAH31440.1; -; mRNA.
DR CCDS; CCDS27113.1; -.
DR PIR; A48912; A48912.
DR RefSeq; NP_001129546.1; NM_001136074.2.
DR RefSeq; NP_001258845.1; NM_001271916.1.
DR RefSeq; NP_001258846.1; NM_001271917.1.
DR RefSeq; NP_032762.1; NM_008736.3.
DR AlphaFoldDB; P54846; -.
DR SMR; P54846; -.
DR STRING; 10090.ENSMUSP00000107035; -.
DR iPTMnet; P54846; -.
DR PhosphoSitePlus; P54846; -.
DR PaxDb; P54846; -.
DR PRIDE; P54846; -.
DR ProteomicsDB; 293972; -.
DR Antibodypedia; 22607; 125 antibodies from 26 providers.
DR DNASU; 18185; -.
DR Ensembl; ENSMUST00000062232; ENSMUSP00000054457; ENSMUSG00000040632.
DR Ensembl; ENSMUST00000111404; ENSMUSP00000107035; ENSMUSG00000040632.
DR Ensembl; ENSMUST00000178694; ENSMUSP00000136445; ENSMUSG00000040632.
DR GeneID; 18185; -.
DR KEGG; mmu:18185; -.
DR UCSC; uc007tyu.3; mouse.
DR CTD; 4901; -.
DR MGI; MGI:102567; Nrl.
DR VEuPathDB; HostDB:ENSMUSG00000040632; -.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000161862; -.
DR HOGENOM; CLU_063062_0_0_1; -.
DR InParanoid; P54846; -.
DR OMA; SEPGMMG; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; P54846; -.
DR TreeFam; TF325689; -.
DR BioGRID-ORCS; 18185; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Nrl; mouse.
DR PRO; PR:P54846; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P54846; protein.
DR Bgee; ENSMUSG00000040632; Expressed in retinal neural layer and 19 other tissues.
DR ExpressionAtlas; P54846; baseline and differential.
DR Genevisible; P54846; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0043522; F:leucine zipper domain binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0046548; P:retinal rod cell development; IMP:MGI.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR013592; Maf_TF_N.
DR InterPro; IPR028575; Nrl.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR InterPro; IPR024874; Transcription_factor_Maf_fam.
DR PANTHER; PTHR10129; PTHR10129; 1.
DR PANTHER; PTHR10129:SF24; PTHR10129:SF24; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR Pfam; PF08383; Maf_N; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Developmental protein; DNA-binding; Isopeptide bond;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..237
FT /note="Neural retina-specific leucine zipper protein"
FT /id="PRO_0000076634"
FT DOMAIN 159..222
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 26..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..93
FT /note="Minimal transactivation domain (MTD)"
FT /evidence="ECO:0000250|UniProtKB:P54845"
FT REGION 159..185
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 187..208
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 34..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:20551322"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:20551322"
SQ SEQUENCE 237 AA; 26083 MW; AF1A2B3772C95EC8 CRC64;
MAFPPSPLAM EYVNDFDLMK FEIKREPSEG RSGVPTASLG STPYSSVPPS PTFSEPGMVG
GGEAPRPGLE ELYWLATLQQ QLGSDEVLGL SPDEAVELLQ NQGPVSMEGP LGYYSGSPGE
TGAQHVQLPE RFSDAALVSM SVRELNRQLR GCGRDEALRL KQRRRTLKNR GYAQACRSKR
LQQRRGLEAE RARLAAQLDA LRAEVARLAR ERDLYKARCD RLTSGGPGSD DHTHLFL
