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P54845

- NRL_HUMAN

UniProt

P54845 - NRL_HUMAN

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Protein
Neural retina-specific leucine zipper protein
Gene
NRL, D14S46E
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcription factor which regulates the expression of several rod-specific genes, in cluding RHO and PDE6B By similarity.

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. leucine zipper domain binding Source: UniProtKB
  3. protein binding Source: IntAct
  4. sequence-specific DNA binding Source: InterPro
  5. sequence-specific DNA binding transcription factor activity Source: Ensembl

GO - Biological processi

  1. positive regulation of rhodopsin gene expression Source: Ensembl
  2. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. regulation of rhodopsin gene expression Source: ProtInc
  4. response to stimulus Source: UniProtKB-KW
  5. retinal rod cell development Source: Ensembl
  6. transcription from RNA polymerase II promoter Source: ProtInc
  7. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Sensory transduction, Transcription, Transcription regulation, Vision

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiP54845.

Names & Taxonomyi

Protein namesi
Recommended name:
Neural retina-specific leucine zipper protein
Short name:
NRL
Gene namesi
Name:NRL
Synonyms:D14S46E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:8002. NRL.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 27 (RP27) [MIM:613750]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501S → T in RP27; increased transactivation activity. 1 Publication
VAR_009268
Natural varianti170 – 1701R → S in RP27. 1 Publication
VAR_068364
Retinal degeneration autosomal recessive clumped pigment type (RDCP) [MIM:162080]: A retinopathy characterized by night blindness since early childhood, consistent with a severe reduction in rod function. Color vision is normal although there is a relatively enhanced function of short-wavelength-sensitive cones in the macula. Signs of retinal degeneration and clusters of clumped pigment deposits in the peripheral fundus at the level of the retinal pigment epithelium are present.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti160 – 1601L → P in RDCP; severely reduced transcriptional activity. 1 Publication
VAR_064977

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

MIMi162080. gene+phenotype.
613750. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA31781.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 237237Neural retina-specific leucine zipper protein
PRO_0000076633Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki20 – 20Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-linki24 – 24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Post-translational modificationi

Disumoylated at Lys-20. Sumoylation modulates the transcriptional activity of NRL on RHO and NR2E3 promoters, and is required for normal rod differentiation By similarity.

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP54845.
PRIDEiP54845.

PTM databases

PhosphoSiteiP54845.

Expressioni

Tissue specificityi

Neural retina.

Gene expression databases

ArrayExpressiP54845.
BgeeiP54845.
CleanExiHS_NRL.
GenevestigatoriP54845.

Interactioni

Subunit structurei

Interacts with FIZ1. This interaction represses transactivation By similarity. Interacts (via the leucine-zipper domain) with CRX.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CRXQ9XSK05EBI-8843813,EBI-8843794From a different organism.

Protein-protein interaction databases

BioGridi110957. 3 interactions.
IntActiP54845. 1 interaction.
STRINGi9606.ENSP00000337023.

Structurei

3D structure databases

ProteinModelPortaliP54845.
SMRiP54845. Positions 131-222.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini159 – 22264bZIP
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 9364Minimal transactivation domain (MTD)
Add
BLAST
Regioni159 – 18527Basic motif By similarity
Add
BLAST
Regioni187 – 20822Leucine-zipper By similarity
Add
BLAST

Domaini

The minimal transactivation domain (MTD) is conserved across the MAF family, it may activate trancription by recruiting TBP and associated factors at the promoters of target genes.1 Publication

Sequence similaritiesi

Belongs to the bZIP family.

Phylogenomic databases

eggNOGiNOG271139.
HOGENOMiHOG000261683.
HOVERGENiHBG000313.
InParanoidiP54845.
KOiK09038.
OMAiGDHAHFF.
OrthoDBiEOG7BGHMQ.
PhylomeDBiP54845.
TreeFamiTF325689.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR028575. Nrl.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
PANTHERiPTHR10129. PTHR10129. 1 hit.
PTHR10129:SF5. PTHR10129:SF5. 1 hit.
PfamiPF03131. bZIP_Maf. 1 hit.
PF08383. Maf_N. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMiSSF47454. SSF47454. 1 hit.
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P54845-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MALPPSPLAM EYVNDFDLMK FEVKREPSEG RPGPPTASLG STPYSSVPPS    50
PTFSEPGMVG ATEGTRPGLE ELYWLATLQQ QLGAGEALGL SPEEAMELLQ 100
GQGPVPVDGP HGYYPGSPEE TGAQHVQLAE RFSDAALVSM SVRELNRQLR 150
GCGRDEALRL KQRRRTLKNR GYAQACRSKR LQQRRGLEAE RARLAAQLDA 200
LRAEVARLAR ERDLYKARCD RLTSSGPGSG DPSHLFL 237
Length:237
Mass (Da):25,940
Last modified:October 1, 1996 - v1
Checksum:iCCABEDC1C1123614
GO
Isoform 2 (identifier: P54845-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.

Note: No experimental confirmation available.

Show »
Length:98
Mass (Da):11,276
Checksum:i1553BA64DAED254C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501S → T in RP27; increased transactivation activity. 1 Publication
VAR_009268
Natural varianti160 – 1601L → P in RDCP; severely reduced transcriptional activity. 1 Publication
VAR_064977
Natural varianti170 – 1701R → S in RP27. 1 Publication
VAR_068364

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 139139Missing in isoform 2.
VSP_055567Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M95925 mRNA. Translation: AAA96828.1.
M81840 mRNA. Translation: AAA59948.1.
U95012 Genomic DNA. Translation: AAB82768.1.
BX161381 mRNA. Translation: CAD61873.1.
BX161522 mRNA. Translation: CAD61954.1.
AB593101 mRNA. Translation: BAJ84041.1.
AB593102 mRNA. Translation: BAJ84042.1.
AB593103 mRNA. Translation: BAJ84043.1.
AB593104 mRNA. Translation: BAJ84044.1.
AB593105 mRNA. Translation: BAJ84045.1.
AB593106 mRNA. Translation: BAJ84046.1.
BT006942 mRNA. Translation: AAP35588.1.
AL136295 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66116.1.
BC012395 mRNA. Translation: AAH12395.1.
CCDSiCCDS9608.1.
PIRiA41796.
RefSeqiNP_006168.1. NM_006177.3.
XP_005267765.1. XM_005267708.2.
XP_005267766.1. XM_005267709.2.
XP_005267767.1. XM_005267710.2.
UniGeneiHs.652297.

Genome annotation databases

EnsembliENST00000396995; ENSP00000380191; ENSG00000129535.
ENST00000396997; ENSP00000380193; ENSG00000129535.
ENST00000397002; ENSP00000380197; ENSG00000129535.
ENST00000561028; ENSP00000454062; ENSG00000129535.
GeneIDi4901.
KEGGihsa:4901.
UCSCiuc001wlo.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Mutations of the NRL gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M95925 mRNA. Translation: AAA96828.1 .
M81840 mRNA. Translation: AAA59948.1 .
U95012 Genomic DNA. Translation: AAB82768.1 .
BX161381 mRNA. Translation: CAD61873.1 .
BX161522 mRNA. Translation: CAD61954.1 .
AB593101 mRNA. Translation: BAJ84041.1 .
AB593102 mRNA. Translation: BAJ84042.1 .
AB593103 mRNA. Translation: BAJ84043.1 .
AB593104 mRNA. Translation: BAJ84044.1 .
AB593105 mRNA. Translation: BAJ84045.1 .
AB593106 mRNA. Translation: BAJ84046.1 .
BT006942 mRNA. Translation: AAP35588.1 .
AL136295 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66116.1 .
BC012395 mRNA. Translation: AAH12395.1 .
CCDSi CCDS9608.1.
PIRi A41796.
RefSeqi NP_006168.1. NM_006177.3.
XP_005267765.1. XM_005267708.2.
XP_005267766.1. XM_005267709.2.
XP_005267767.1. XM_005267710.2.
UniGenei Hs.652297.

3D structure databases

ProteinModelPortali P54845.
SMRi P54845. Positions 131-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110957. 3 interactions.
IntActi P54845. 1 interaction.
STRINGi 9606.ENSP00000337023.

PTM databases

PhosphoSitei P54845.

Proteomic databases

PaxDbi P54845.
PRIDEi P54845.

Protocols and materials databases

DNASUi 4901.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000396995 ; ENSP00000380191 ; ENSG00000129535 .
ENST00000396997 ; ENSP00000380193 ; ENSG00000129535 .
ENST00000397002 ; ENSP00000380197 ; ENSG00000129535 .
ENST00000561028 ; ENSP00000454062 ; ENSG00000129535 .
GeneIDi 4901.
KEGGi hsa:4901.
UCSCi uc001wlo.3. human.

Organism-specific databases

CTDi 4901.
GeneCardsi GC14M024549.
GeneReviewsi NRL.
HGNCi HGNC:8002. NRL.
MIMi 162080. gene+phenotype.
613750. phenotype.
neXtProti NX_P54845.
Orphaneti 791. Retinitis pigmentosa.
PharmGKBi PA31781.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271139.
HOGENOMi HOG000261683.
HOVERGENi HBG000313.
InParanoidi P54845.
KOi K09038.
OMAi GDHAHFF.
OrthoDBi EOG7BGHMQ.
PhylomeDBi P54845.
TreeFami TF325689.

Enzyme and pathway databases

SignaLinki P54845.

Miscellaneous databases

ChiTaRSi NRL. human.
GeneWikii NRL_(gene).
GenomeRNAii 4901.
NextBioi 18863.
PROi P54845.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54845.
Bgeei P54845.
CleanExi HS_NRL.
Genevestigatori P54845.

Family and domain databases

Gene3Di 1.10.880.10. 1 hit.
InterProi IPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR028575. Nrl.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view ]
PANTHERi PTHR10129. PTHR10129. 1 hit.
PTHR10129:SF5. PTHR10129:SF5. 1 hit.
Pfami PF03131. bZIP_Maf. 1 hit.
PF08383. Maf_N. 1 hit.
[Graphical view ]
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47454. SSF47454. 1 hit.
PROSITEi PS50217. BZIP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A conserved retina-specific gene encodes a basic motif/leucine zipper domain."
    Swaroop A., Xu J.Z., Pawar H., Jackson A.U., Skolnick C., Agarwal N.
    Proc. Natl. Acad. Sci. U.S.A. 89:266-270(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retina.
  2. Jackson A.U., Skolnick C., Swaroop A.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retina.
  3. "Human bZIP transcription factor gene NRL: structure, genomic sequence, and fine linkage mapping at 14q11.2 and negative mutation analysis in patients with retinal degeneration."
    Farjo Q., Jackson A.U., Pieke-Dahl S., Scott K., Kimberling W.J., Sieving P.A., Richards J.E., Swaroop A.
    Genomics 45:395-401(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: B-cell and Neuroblastoma.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
    Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
    Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Retinoblastoma.
  7. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye.
  10. "The leucine zipper of NRL interacts with the CRX homeodomain. A possible mechanism of transcriptional synergy in rhodopsin regulation."
    Mitton K.P., Swain P.K., Chen S., Xu S., Zack D.J., Swaroop A.
    J. Biol. Chem. 275:29794-29799(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRX.
  11. "The minimal transactivation domain of the basic motif-leucine zipper transcription factor NRL interacts with TATA-binding protein."
    Friedman J.S., Khanna H., Swain P.K., Denicola R., Cheng H., Mitton K.P., Weber C.H., Hicks D., Swaroop A.
    J. Biol. Chem. 279:47233-47241(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN MINIMAL TRANSACTIVATION DOMAIN.
  12. Cited for: VARIANT RP27 THR-50.
  13. "Recessive NRL mutations in patients with clumped pigmentary retinal degeneration and relative preservation of blue cone function."
    Nishiguchi K.M., Friedman J.S., Sandberg M.A., Swaroop A., Berson E.L., Dryja T.P.
    Proc. Natl. Acad. Sci. U.S.A. 101:17819-17824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RDCP PRO-160, CHARACTERIZATION OF VARIANT RDCP PRO-160.
  14. Cited for: VARIANT RP27 SER-170.

Entry informationi

Entry nameiNRL_HUMAN
AccessioniPrimary (citable) accession number: P54845
Secondary accession number(s): A8MX14, Q53XD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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