P12271 · RLBP1_HUMAN

  • Protein
    Retinaldehyde-binding protein 1
  • Gene
    RLBP1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Soluble retinoid carrier essential the proper function of both rod and cone photoreceptors. Participates in the regeneration of active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-trans products of the rhodopsin photocycle and in the de novo synthesis of these retinoids from 11-trans metabolic precursors. The cycling of retinoids between photoreceptor and adjacent pigment epithelium cells is known as the 'visual cycle'.

Features

Showing features for binding site.

131720406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site18011-cis-retinal (UniProtKB | ChEBI)
Binding site20211-cis-retinal (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell body
Cellular Componentcentrosome
Cellular Componentcytosol
Cellular Componentnucleoplasm
Molecular Function11-cis retinal binding
Molecular Functionphosphatidylinositol bisphosphate binding
Molecular Functionretinol binding
Biological Processvisual perception
Biological Processvitamin A metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Retinaldehyde-binding protein 1
  • Alternative names
    • Cellular retinaldehyde-binding protein

Gene names

    • Name
      RLBP1
    • Synonyms
      CRALBP

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P12271
  • Secondary accessions
    • B2R667

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Involvement in disease

Bothnia retinal dystrophy (BRD)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A type of retinitis punctata albescens. Affected individuals show night blindness from early childhood with features consistent with retinitis punctata albescens and macular degeneration.
  • See also
    MIM:607475
Natural variants in BRD
Variant IDPosition(s)ChangeDescription
VAR_015172234R>Win BRD; dbSNP:rs28933990

Rod-cone dystrophy Newfoundland (NFRCD)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A rod-cone dystrophy reminiscent of retinitis punctata albescens but with a substantially lower age at onset and more-rapid and distinctive progression. Rod-cone dystrophies results from initial loss of rod photoreceptors, later followed by cone photoreceptors loss.
  • See also
    MIM:607476

Retinitis punctata albescens (RPA)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A form of fleck retina disease characterized by aggregation of white flecks posteriorly in the retina, causing night blindness and delayed dark adaptation. It differs from fundus albipunctatus in being progressive and evolving to generalized atrophy of the retina.
  • See also
    MIM:136880
Natural variants in RPA
Variant IDPosition(s)ChangeDescription
VAR_005140151R>Qin RPA; loss of ability to bind 11-cis-retinaldehyde; dbSNP:rs137853290
VAR_037317226M>Kin RPA; dbSNP:rs137853291

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_005140151in RPA; loss of ability to bind 11-cis-retinaldehyde; dbSNP:rs137853290
Natural variantVAR_037317226in RPA; dbSNP:rs137853291
Natural variantVAR_015172234in BRD; dbSNP:rs28933990

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 410 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00000793302-317Retinaldehyde-binding protein 1

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Retina and pineal gland. Not present in photoreceptor cells but is expressed abundantly in the adjacent retinal pigment epithelium (RPE) and in the Mueller glial cells of the retina.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with DEGS1; the interaction increases synthesis of chromophore-precursors by DEGS1.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P12271KLHL8 Q9P2G9-23EBI-11959637, EBI-11959635

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain136-297CRAL-TRIO

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    317
  • Mass (Da)
    36,474
  • Last updated
    2007-01-23 v2
  • Checksum
    80A3B0AE65FDA6EB
MSEGVGTFRMVPEEEQELRAQLEQLTTKDHGPVFGPCSQLPRHTLQKAKDELNEREETREEAVRELQEMVQAQAASGEELAVAVAERVQEKDSGFFLRFIRARKFNVGRAYELLRGYVNFRLQYPELFDSLSPEAVRCTIEAGYPGVLSSRDKYGRVVMLFNIENWQSQEITFDEILQAYCFILEKLLENEETQINGFCIIENFKGFTMQQAASLRTSDLRKMVDMLQDSFPARFKAIHFIHQPWYFTTTYNVVKPFLKSKLLERVFVHGDDLSGFYQEIDENILPSDFGGTLPKYDGKAVAEQLFGPQAQAENTAF

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H3BTN3H3BTN3_HUMANRLBP171
H3BN92H3BN92_HUMANRLBP1108

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
J04213
EMBL· GenBank· DDBJ
AAA60251.1
EMBL· GenBank· DDBJ
mRNA
L34219
EMBL· GenBank· DDBJ
AAA65123.1
EMBL· GenBank· DDBJ
Genomic DNA
AK312457
EMBL· GenBank· DDBJ
BAG35364.1
EMBL· GenBank· DDBJ
mRNA
CH471101
EMBL· GenBank· DDBJ
EAX02038.1
EMBL· GenBank· DDBJ
Genomic DNA
BC004199
EMBL· GenBank· DDBJ
AAH04199.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp