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 24-JAN-2024, entry version 196. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR RefSeq; XP_005267767.1; XM_005267710.3. DR RefSeq; XP_011535104.1; XM_011536802.1. DR RefSeq; XP_011535106.1; XM_011536804.2. DR RefSeq; XP_011535107.1; XM_011536805.2. [P54845-1] DR AlphaFoldDB; P54845; -. DR SMR; P54845; -. DR BioGRID; 110957; 9. 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; 9606-ENSP00000454062; -. DR PeptideAtlas; P54845; -. DR ProteomicsDB; 2286; -. DR ProteomicsDB; 56738; -. [P54845-1] DR Antibodypedia; 22607; 151 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 AGR; HGNC:8002; -. 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; SGDHAHF; -. DR OrthoDB; 2958941at2759; -. DR PhylomeDB; P54845; -. DR TreeFam; TF325689; -. DR PathwayCommons; P54845; -. DR SignaLink; P54845; -. DR SIGNOR; P54845; -. DR BioGRID-ORCS; 4901; 16 hits in 1168 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 male germ line stem cell (sensu Vertebrata) in testis and 94 other cell types or tissues. DR ExpressionAtlas; P54845; baseline and differential. 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 CDD; cd14718; bZIP_Maf_large; 1. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR004826; bZIP_Maf. DR InterPro; IPR046347; bZIP_sf. DR InterPro; IPR013592; Maf_TF_N. DR InterPro; IPR008917; TF_DNA-bd_sf. DR InterPro; IPR024874; Transcription_factor_Maf_fam. DR PANTHER; PTHR10129:SF24; NEURAL RETINA-SPECIFIC LEUCINE ZIPPER PROTEIN; 1. DR PANTHER; PTHR10129; TRANSCRIPTION FACTOR MAF; 1. DR Pfam; PF03131; bZIP_Maf; 1. DR Pfam; PF08383; Maf_N; 1. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR Genevisible; P54845; HS. 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; uncertain significance; alters FT phosphorylation; no effect on subcellular localization; no FT effect on transcriptional coactivator activity; FT 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; uncertain significance; alters FT phosphorylation; no effect on subcellular localization; no FT effect on transcriptional coactivator activity; FT 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; uncertain FT significance; no effect on phosphorylation; no effect on FT 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 //