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P54845 (NRL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neural retina-specific leucine zipper protein

Short name=NRL
Gene names
Name:NRL
Synonyms:D14S46E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Interacts with FIZ1. This interaction represses transactivation By similarity. Interacts (via the leucine-zipper domain) with CRX. Ref.10

Subcellular location

Nucleus.

Tissue specificity

Neural retina.

Domain

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. Ref.11

Post-translational modification

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.

Involvement in disease

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. Ref.12 Ref.14

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. Ref.13

Sequence similarities

Belongs to the bZIP family.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processSensory transduction
Transcription
Transcription regulation
Vision
   Cellular componentNucleus
   DiseaseDisease mutation
Retinitis pigmentosa
   LigandDNA-binding
   Molecular functionDevelopmental protein
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of rhodopsin gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of rhodopsin gene expression

Traceable author statement PubMed 8939891. Source: ProtInc

response to stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

retinal rod cell development

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement PubMed 8939891. Source: ProtInc

visual perception

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentnucleus

Traceable author statement PubMed 8939891. Source: ProtInc

   Molecular_functionDNA binding

Traceable author statement Ref.1. Source: ProtInc

leucine zipper domain binding

Inferred from physical interaction Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10. Source: IntAct

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CRXQ9XSK05EBI-8843813,EBI-8843794From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 237237Neural retina-specific leucine zipper protein
PRO_0000076633

Regions

Domain159 – 22264bZIP
Region30 – 9364Minimal transactivation domain (MTD)
Region159 – 18527Basic motif By similarity
Region187 – 20822Leucine-zipper By similarity

Amino acid modifications

Cross-link20Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Natural variant501S → T in RP27; increased transactivation activity. Ref.12
VAR_009268
Natural variant1601L → P in RDCP; severely reduced transcriptional activity. Ref.13
VAR_064977
Natural variant1701R → S in RP27. Ref.14
VAR_068364

Sequences

Sequence LengthMass (Da)Tools
P54845 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: CCABEDC1C1123614

FASTA23725,940
        10         20         30         40         50         60 
MALPPSPLAM EYVNDFDLMK FEVKREPSEG RPGPPTASLG STPYSSVPPS PTFSEPGMVG 

        70         80         90        100        110        120 
ATEGTRPGLE ELYWLATLQQ QLGAGEALGL SPEEAMELLQ GQGPVPVDGP HGYYPGSPEE 

       130        140        150        160        170        180 
TGAQHVQLAE RFSDAALVSM SVRELNRQLR GCGRDEALRL KQRRRTLKNR GYAQACRSKR 

       190        200        210        220        230 
LQQRRGLEAE RARLAAQLDA LRAEVARLAR ERDLYKARCD RLTSSGPGSG DPSHLFL 

« Hide

References

« Hide 'large scale' references
[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].
Tissue: Retina.
[2]Jackson A.U., Skolnick C., Swaroop A.
Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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].
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].
[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].
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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].
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]"A mutation in NRL is associated with autosomal dominant retinitis pigmentosa."
Bessant D.A.R., Payne A.M., Mitton K.P., Wang Q.-L., Swain P.K., Plant C., Bird A.C., Zack D.J., Swaroop A., Bhattacharya S.S.
Nat. Genet. 21:355-356(1999) [PubMed] [Europe PMC] [Abstract]
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]"Next-generation genetic testing for retinitis pigmentosa."
Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L., Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J., Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E., den Hollander A.I., Hoischen A., Hoyng C. expand/collapse author list , Klevering B.J., van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H.
Hum. Mutat. 33:963-972(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP27 SER-170.
+Additional computationally mapped references.

Web resources

Mutations of the NRL gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
AB593102 mRNA. Translation: BAJ84042.1.
AB593104 mRNA. Translation: BAJ84044.1.
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.
CCDSCCDS9608.1.
PIRA41796.
RefSeqNP_006168.1. NM_006177.3.
XP_005267765.1. XM_005267708.2.
XP_005267766.1. XM_005267709.2.
XP_005267767.1. XM_005267710.2.
UniGeneHs.652297.

3D structure databases

ProteinModelPortalP54845.
SMRP54845. Positions 131-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110957. 3 interactions.
IntActP54845. 1 interaction.
STRING9606.ENSP00000337023.

PTM databases

PhosphoSiteP54845.

Proteomic databases

PaxDbP54845.
PRIDEP54845.

Protocols and materials databases

DNASU4901.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396997; ENSP00000380193; ENSG00000129535.
ENST00000397002; ENSP00000380197; ENSG00000129535.
ENST00000561028; ENSP00000454062; ENSG00000129535.
GeneID4901.
KEGGhsa:4901.
UCSCuc001wlo.3. human.

Organism-specific databases

CTD4901.
GeneCardsGC14M024549.
GeneReviewsNRL.
HGNCHGNC:8002. NRL.
MIM162080. gene+phenotype.
613750. phenotype.
neXtProtNX_P54845.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA31781.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271139.
HOGENOMHOG000261683.
HOVERGENHBG000313.
InParanoidP54845.
KOK09038.
OMAGDHAHFF.
OrthoDBEOG7BGHMQ.
PhylomeDBP54845.
TreeFamTF325689.

Enzyme and pathway databases

SignaLinkP54845.

Gene expression databases

ArrayExpressP54845.
BgeeP54845.
CleanExHS_NRL.
GenevestigatorP54845.

Family and domain databases

Gene3D1.10.880.10. 1 hit.
InterProIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR028575. Nrl.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
PANTHERPTHR10129. PTHR10129. 1 hit.
PTHR10129:SF5. PTHR10129:SF5. 1 hit.
PfamPF03131. bZIP_Maf. 1 hit.
PF08383. Maf_N. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMSSF47454. SSF47454. 1 hit.
PROSITEPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNRL. human.
GeneWikiNRL_(gene).
GenomeRNAi4901.
NextBio18863.
PROP54845.
SOURCESearch...

Entry information

Entry nameNRL_HUMAN
AccessionPrimary (citable) accession number: P54845
Secondary accession number(s): Q53XD0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM