NRL_HUMAN
ID NRL_HUMAN Reviewed; 237 AA.
AC P54845; A8MX14; Q53XD0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Neural retina-specific leucine zipper protein;
DE Short=NRL;
GN Name=NRL; Synonyms=D14S46E;
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 1).
RC TISSUE=Retina;
RX PubMed=1729696; DOI=10.1073/pnas.89.1.266;
RA Swaroop A., Xu J.Z., Pawar H., Jackson A.U., Skolnick C., Agarwal N.;
RT "A conserved retina-specific gene encodes a basic motif/leucine zipper
RT domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:266-270(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RA Jackson A.U., Skolnick C., Swaroop A.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9344665; DOI=10.1006/geno.1997.4964;
RA Farjo Q., Jackson A.U., Pieke-Dahl S., Scott K., Kimberling W.J.,
RA Sieving P.A., Richards J.E., Swaroop A.;
RT "Human bZIP transcription factor gene NRL: structure, genomic sequence, and
RT fine linkage mapping at 14q11.2 and negative mutation analysis in patients
RT with retinal degeneration.";
RL Genomics 45:395-401(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, and Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Retinoblastoma;
RX PubMed=21697133; DOI=10.1167/iovs.11-7479;
RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S.,
RA Usami R., Ohtoko K., Kato S.;
RT "Full-length transcriptome analysis of human retina-derived cell lines
RT ARPE-19 and Y79 using the vector-capping method.";
RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [10]
RP INTERACTION WITH CRX.
RX PubMed=10887186; DOI=10.1074/jbc.m003658200;
RA Mitton K.P., Swain P.K., Chen S., Xu S., Zack D.J., Swaroop A.;
RT "The leucine zipper of NRL interacts with the CRX homeodomain. A possible
RT mechanism of transcriptional synergy in rhodopsin regulation.";
RL J. Biol. Chem. 275:29794-29799(2000).
RN [11]
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND 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 [12]
RP DOMAIN MINIMAL TRANSACTIVATION DOMAIN.
RX PubMed=15328344; DOI=10.1074/jbc.m408298200;
RA Friedman J.S., Khanna H., Swain P.K., Denicola R., Cheng H., Mitton K.P.,
RA Weber C.H., Hicks D., Swaroop A.;
RT "The minimal transactivation domain of the basic motif-leucine zipper
RT transcription factor NRL interacts with TATA-binding protein.";
RL J. Biol. Chem. 279:47233-47241(2004).
RN [13]
RP VARIANT RP27 THR-50.
RX PubMed=10192380; DOI=10.1038/7678;
RA Bessant D.A.R., Payne A.M., Mitton K.P., Wang Q.-L., Swain P.K., Plant C.,
RA Bird A.C., Zack D.J., Swaroop A., Bhattacharya S.S.;
RT "A mutation in NRL is associated with autosomal dominant retinitis
RT pigmentosa.";
RL Nat. Genet. 21:355-356(1999).
RN [14]
RP VARIANTS RP27 LEU-51 AND GLU-122, AND INVOLVEMENT IN RP27.
RX PubMed=11385710; DOI=10.1002/humu.1135;
RA Martinez-Gimeno M., Maseras M., Baiget M., Beneito M., Antinolo G.,
RA Ayuso C., Carballo M.;
RT "Mutations P51U and G122E in retinal transcription factor NRL associated
RT with autosomal dominant and sporadic retinitis pigmentosa.";
RL Hum. Mutat. 17:520-520(2001).
RN [15]
RP VARIANTS RP27 LEU-50; PRO-50 AND THR-51.
RX PubMed=11879142; DOI=10.1001/archopht.120.3.369;
RA DeAngelis M.M., Grimsby J.L., Sandberg M.A., Berson E.L., Dryja T.P.;
RT "Novel mutations in the NRL gene and associated clinical findings in
RT patients with dominant retinitis pigmentosa.";
RL Arch. Ophthalmol. 120:369-375(2002).
RN [16]
RP VARIANTS RDCP VAL-76 AND PRO-160, CHARACTERIZATION OF VARIANT RDCP PRO-160,
RP VARIANT RP27 SER-51, AND VARIANT GLN-125.
RX PubMed=15591106; DOI=10.1073/pnas.0408183101;
RA Nishiguchi K.M., Friedman J.S., Sandberg M.A., Swaroop A., Berson E.L.,
RA Dryja T.P.;
RT "Recessive NRL mutations in patients with clumped pigmentary retinal
RT degeneration and relative preservation of blue cone function.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17819-17824(2004).
RN [17]
RP VARIANT RP27 LEU-51, AND VARIANT SER-67.
RX PubMed=15994872; DOI=10.1136/jmg.2005.031682;
RA Ziviello C., Simonelli F., Testa F., Anastasi M., Marzoli S.B., Falsini B.,
RA Ghiglione D., Macaluso C., Manitto M.P., Garre C., Ciccodicola A.,
RA Rinaldi E., Banfi S.;
RT "Molecular genetics of autosomal dominant retinitis pigmentosa (ADRP): a
RT comprehensive study of 43 Italian families.";
RL J. Med. Genet. 42:E47-E47(2005).
RN [18]
RP VARIANT RP27 SER-170.
RX PubMed=22334370; DOI=10.1002/humu.22045;
RA Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L.,
RA Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J.,
RA Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E.,
RA den Hollander A.I., Hoischen A., Hoyng C., Klevering B.J.,
RA van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H.;
RT "Next-generation genetic testing for retinitis pigmentosa.";
RL Hum. Mutat. 33:963-972(2012).
RN [19]
RP CHARACTERIZATION OF VARIANTS RP27 LEU-50; PRO-50; THR-50; LEU-51; SER-51;
RP THR-51; SER-67 AND GLU-122, CHARACTERIZATION OF VARIANTS RDCP VAL-76 AND
RP PRO-160, CHARACTERIZATION OF VARIANT GLN-125, FUNCTION, DNA-BINDING,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=17335001; DOI=10.1002/humu.20488;
RA Kanda A., Friedman J.S., Nishiguchi K.M., Swaroop A.;
RT "Retinopathy mutations in the bZIP protein NRL alter phosphorylation and
RT transcriptional activity.";
RL Hum. Mutat. 28:589-598(2007).
RN [20]
RP VARIANT RP27 THR-96, CHARACTERIZATION OF VARIANTS RP27 THR-50; LEU-51 AND
RP THR-96, AND FUNCTION.
RX PubMed=21981118; DOI=10.1111/j.1399-0004.2011.01796.x;
RA Hernan I., Gamundi M.J., Borras E., Maseras M., Garcia-Sandoval B.,
RA Blanco-Kelly F., Ayuso C., Carballo M.;
RT "Novel p.M96T variant of NRL and shRNA-based suppression and replacement of
RT NRL mutants associated with autosomal dominant retinitis pigmentosa.";
RL Clin. Genet. 82:446-452(2012).
CC -!- FUNCTION: Acts as a transcriptional activator which regulates the
CC expression of several rod-specific genes, including RHO and PDE6B
CC (PubMed:21981118). Functions also as a transcriptional coactivator,
CC stimulating transcription mediated by the transcription factor CRX and
CC NR2E3 (PubMed:17335001). Binds in a sequence-specific manner to the
CC rhodopsin promoter (PubMed:17335001). {ECO:0000269|PubMed:17335001,
CC ECO:0000269|PubMed:21981118}.
CC -!- SUBUNIT: Interacts with FIZ1; this interaction represses
CC transactivation (By similarity). Interacts (via the leucine-zipper
CC domain) with CRX (PubMed:10887186). {ECO:0000250,
CC ECO:0000269|PubMed:10887186}.
CC -!- INTERACTION:
CC P54845; Q9XSK0: CRX; Xeno; NbExp=6; IntAct=EBI-8843813, EBI-8843794;
CC P54845-1; Q96CV9: OPTN; NbExp=6; IntAct=EBI-9819090, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11477108}. Nucleus
CC {ECO:0000269|PubMed:11477108, ECO:0000269|PubMed:17335001}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P54845-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54845-2; Sequence=VSP_055567;
CC -!- TISSUE SPECIFICITY: Expressed in the brain and the retina
CC (PubMed:11477108). Expressed strongly in rod and cone cells (at protein
CC level) (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:0000269|PubMed:15328344}.
CC -!- PTM: Phosphorylated (PubMed:11477108, PubMed:17335001).
CC {ECO:0000269|PubMed:11477108, ECO:0000269|PubMed:17335001}.
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 (By similarity). {ECO:0000250|UniProtKB:P54846}.
CC -!- DISEASE: Retinitis pigmentosa 27 (RP27) [MIM:613750]: 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:10192380,
CC ECO:0000269|PubMed:11385710, ECO:0000269|PubMed:11879142,
CC ECO:0000269|PubMed:15591106, ECO:0000269|PubMed:15994872,
CC ECO:0000269|PubMed:17335001, ECO:0000269|PubMed:21981118,
CC ECO:0000269|PubMed:22334370}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Retinal degeneration autosomal recessive clumped pigment type
CC (RDCP) [MIM:613750]: A retinopathy characterized by night blindness
CC since early childhood, consistent with a severe reduction in rod
CC function. Color vision is normal although there is a relatively
CC enhanced function of short-wavelength-sensitive cones in the macula.
CC Signs of retinal degeneration and clusters of clumped pigment deposits
CC in the peripheral fundus at the level of the retinal pigment epithelium
CC are present. {ECO:0000269|PubMed:15591106,
CC ECO:0000269|PubMed:17335001}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Mutations of the NRL gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/nrlmut.htm";
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DR EMBL; M95925; AAA96828.1; -; mRNA.
DR EMBL; M81840; AAA59948.1; -; mRNA.
DR EMBL; U95012; AAB82768.1; -; Genomic_DNA.
DR EMBL; BX161381; CAD61873.1; -; mRNA.
DR EMBL; BX161522; CAD61954.1; -; mRNA.
DR EMBL; AB593101; BAJ84041.1; -; mRNA.
DR EMBL; AB593102; BAJ84042.1; -; mRNA.
DR EMBL; AB593103; BAJ84043.1; -; mRNA.
DR EMBL; AB593104; BAJ84044.1; -; mRNA.
DR EMBL; AB593105; BAJ84045.1; -; mRNA.
DR EMBL; AB593106; BAJ84046.1; -; mRNA.
DR EMBL; BT006942; AAP35588.1; -; mRNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66116.1; -; Genomic_DNA.
DR EMBL; BC012395; AAH12395.1; -; mRNA.
DR CCDS; CCDS9608.1; -. [P54845-1]
DR PIR; A41796; A41796.
DR RefSeq; NP_006168.1; NM_006177.3. [P54845-1]
DR RefSeq; XP_005267765.1; XM_005267708.4.
DR RefSeq; XP_005267766.1; XM_005267709.3. [P54845-1]
DR RefSeq; XP_005267767.1; XM_005267710.3.
DR RefSeq; XP_011535104.1; XM_011536802.1. [P54845-1]
DR RefSeq; XP_011535106.1; XM_011536804.2. [P54845-1]
DR RefSeq; XP_011535107.1; XM_011536805.2. [P54845-1]
DR AlphaFoldDB; P54845; -.
DR SMR; P54845; -.
DR BioGRID; 110957; 8.
DR ELM; P54845; -.
DR IntAct; P54845; 3.
DR STRING; 9606.ENSP00000454062; -.
DR iPTMnet; P54845; -.
DR PhosphoSitePlus; P54845; -.
DR BioMuta; NRL; -.
DR MassIVE; P54845; -.
DR PaxDb; P54845; -.
DR PeptideAtlas; P54845; -.
DR PRIDE; P54845; -.
DR ProteomicsDB; 2286; -.
DR ProteomicsDB; 56738; -. [P54845-1]
DR Antibodypedia; 22607; 125 antibodies from 26 providers.
DR DNASU; 4901; -.
DR Ensembl; ENST00000396995.1; ENSP00000380191.1; ENSG00000129535.13. [P54845-2]
DR Ensembl; ENST00000396997.1; ENSP00000380193.1; ENSG00000129535.13. [P54845-1]
DR Ensembl; ENST00000397002.6; ENSP00000380197.2; ENSG00000129535.13. [P54845-1]
DR Ensembl; ENST00000560550.1; ENSP00000452966.1; ENSG00000129535.13. [P54845-2]
DR Ensembl; ENST00000561028.6; ENSP00000454062.2; ENSG00000129535.13. [P54845-1]
DR Ensembl; ENST00000642485.1; ENSP00000494928.1; ENSG00000285493.3. [P54845-2]
DR Ensembl; ENST00000643394.1; ENSP00000495627.1; ENSG00000285493.3. [P54845-1]
DR Ensembl; ENST00000645740.1; ENSP00000495155.1; ENSG00000285493.3. [P54845-2]
DR Ensembl; ENST00000646526.3; ENSP00000496316.1; ENSG00000285493.3. [P54845-1]
DR Ensembl; ENST00000647376.1; ENSP00000496275.1; ENSG00000285493.3. [P54845-1]
DR GeneID; 4901; -.
DR KEGG; hsa:4901; -.
DR MANE-Select; ENST00000561028.6; ENSP00000454062.2; NM_001354768.3; NP_001341697.1.
DR UCSC; uc001wlo.4; human. [P54845-1]
DR CTD; 4901; -.
DR DisGeNET; 4901; -.
DR GeneCards; NRL; -.
DR GeneReviews; NRL; -.
DR HGNC; HGNC:8002; NRL.
DR HPA; ENSG00000129535; Tissue enriched (retina).
DR MalaCards; NRL; -.
DR MIM; 162080; gene.
DR MIM; 613750; phenotype.
DR neXtProt; NX_P54845; -.
DR OpenTargets; ENSG00000129535; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA31781; -.
DR VEuPathDB; HostDB:ENSG00000129535; -.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000161862; -.
DR HOGENOM; CLU_063062_0_0_1; -.
DR InParanoid; P54845; -.
DR OMA; SEPGMMG; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; P54845; -.
DR TreeFam; TF325689; -.
DR PathwayCommons; P54845; -.
DR SignaLink; P54845; -.
DR SIGNOR; P54845; -.
DR BioGRID-ORCS; 4901; 8 hits in 1090 CRISPR screens.
DR ChiTaRS; NRL; human.
DR GeneWiki; NRL_(gene); -.
DR GenomeRNAi; 4901; -.
DR Pharos; P54845; Tbio.
DR PRO; PR:P54845; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P54845; protein.
DR Bgee; ENSG00000129535; Expressed in hindlimb stylopod muscle and 92 other tissues.
DR ExpressionAtlas; P54845; baseline and differential.
DR Genevisible; P54845; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0043522; F:leucine zipper domain binding; IPI:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
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:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0046548; P:retinal rod cell development; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
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; Alternative splicing; Cytoplasm; Developmental protein;
KW Disease variant; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW Retinitis pigmentosa; Sensory transduction; Transcription;
KW Transcription regulation; Ubl conjugation; Vision.
FT CHAIN 1..237
FT /note="Neural retina-specific leucine zipper protein"
FT /id="PRO_0000076633"
FT DOMAIN 159..222
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 23..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..93
FT /note="Minimal transactivation domain (MTD)"
FT /evidence="ECO:0000269|PubMed:15328344"
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 38..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:0000250"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..139
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:21697133"
FT /id="VSP_055567"
FT VARIANT 50
FT /note="S -> L (in RP27; decreases phosphorylation; no
FT effect on subcellular localization; increased
FT transcriptional coactivator activity)"
FT /evidence="ECO:0000269|PubMed:11879142,
FT ECO:0000269|PubMed:17335001"
FT /id="VAR_079382"
FT VARIANT 50
FT /note="S -> P (in RP27; decreases phosphorylation; no
FT effect on subcellular localization; increased
FT transcriptional coactivator activity)"
FT /evidence="ECO:0000269|PubMed:11879142,
FT ECO:0000269|PubMed:17335001"
FT /id="VAR_079383"
FT VARIANT 50
FT /note="S -> T (in RP27; decreases phosphorylation; no
FT effect on subcellular localization; increased
FT transactivational activity; increased transcriptional
FT coactivator activity; dbSNP:rs104894459)"
FT /evidence="ECO:0000269|PubMed:10192380,
FT ECO:0000269|PubMed:17335001, ECO:0000269|PubMed:21981118"
FT /id="VAR_009268"
FT VARIANT 51
FT /note="P -> L (in RP27; decreases phosphorylation; no
FT effect on subcellular localization; increased
FT transcriptional coactivator activity)"
FT /evidence="ECO:0000269|PubMed:11385710,
FT ECO:0000269|PubMed:15994872, ECO:0000269|PubMed:17335001,
FT ECO:0000269|PubMed:21981118"
FT /id="VAR_079384"
FT VARIANT 51
FT /note="P -> S (in RP27; decreases phosphorylation; no
FT effect on subcellular localization; increased
FT transcriptional coactivator activity; dbSNP:rs794727281)"
FT /evidence="ECO:0000269|PubMed:15591106,
FT ECO:0000269|PubMed:17335001"
FT /id="VAR_079385"
FT VARIANT 51
FT /note="P -> T (in RP27; autosomal dominant; decreases
FT phosphorylation; no effect on subcellular localization;
FT increased transcriptional coactivator activity)"
FT /evidence="ECO:0000269|PubMed:11879142,
FT ECO:0000269|PubMed:17335001"
FT /id="VAR_079386"
FT VARIANT 67
FT /note="P -> S (in RP27; no effect on phosphorylation; no
FT effect on subcellular localization; no effect on
FT transcriptional coactivator activity; dbSNP:rs199691910)"
FT /evidence="ECO:0000269|PubMed:15994872,
FT ECO:0000269|PubMed:17335001"
FT /id="VAR_079387"
FT VARIANT 76
FT /note="A -> V (in RDCP; unknown pathological significance;
FT alters phosphorylation; no effect on subcellular
FT localization; no effect on transcriptional coactivator
FT activity; dbSNP:rs149921817)"
FT /evidence="ECO:0000269|PubMed:15591106,
FT ECO:0000269|PubMed:17335001"
FT /id="VAR_079388"
FT VARIANT 96
FT /note="M -> T (in RP27; increased transactivational
FT activity; dbSNP:rs397514516)"
FT /evidence="ECO:0000269|PubMed:21981118"
FT /id="VAR_079389"
FT VARIANT 122
FT /note="G -> E (in RP27; unknown pathological significance;
FT alters phosphorylation; no effect on subcellular
FT localization; no effect on transcriptional coactivator
FT activity; dbSNP:rs757038765)"
FT /evidence="ECO:0000269|PubMed:11385710,
FT ECO:0000269|PubMed:17335001"
FT /id="VAR_079390"
FT VARIANT 125
FT /note="H -> Q (found in a patient with atypical retinitis
FT pigmentosa and a patient with cone dysfunction; unknown
FT pathological significance; no effect on phosphorylation; no
FT effect on subcellular localization; dbSNP:rs201970559)"
FT /evidence="ECO:0000269|PubMed:15591106,
FT ECO:0000269|PubMed:17335001"
FT /id="VAR_079391"
FT VARIANT 160
FT /note="L -> P (in RDCP; alters phosphorylation; no effect
FT on subcellular localization; loss of transcriptional
FT coactivator activity; dbSNP:rs104894463)"
FT /evidence="ECO:0000269|PubMed:15591106,
FT ECO:0000269|PubMed:17335001"
FT /id="VAR_064977"
FT VARIANT 170
FT /note="R -> S (in RP27; dbSNP:rs1173385399)"
FT /evidence="ECO:0000269|PubMed:22334370"
FT /id="VAR_068364"
SQ SEQUENCE 237 AA; 25940 MW; CCABEDC1C1123614 CRC64;
MALPPSPLAM EYVNDFDLMK FEVKREPSEG RPGPPTASLG STPYSSVPPS PTFSEPGMVG
ATEGTRPGLE ELYWLATLQQ QLGAGEALGL SPEEAMELLQ GQGPVPVDGP HGYYPGSPEE
TGAQHVQLAE RFSDAALVSM SVRELNRQLR GCGRDEALRL KQRRRTLKNR GYAQACRSKR
LQQRRGLEAE RARLAAQLDA LRAEVARLAR ERDLYKARCD RLTSSGPGSG DPSHLFL
