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Protein

Retinaldehyde-binding protein 1

Gene

RLBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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'.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei18011-cis-retinal1 Publication1
Binding sitei20211-cis-retinal1 Publication1

GO - Molecular functioni

GO - Biological processi

  • response to stimulus Source: UniProtKB-KW
  • retinoid metabolic process Source: Reactome
  • visual perception Source: ProtInc
  • vitamin A metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Transport, Vision

Keywords - Ligandi

Retinol-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000140522-MONOMER.
ZFISH:ENSG00000140522-MONOMER.
ReactomeiR-HSA-2187335. The retinoid cycle in cones (daylight vision).
R-HSA-2453864. Retinoid cycle disease events.
R-HSA-2453902. The canonical retinoid cycle in rods (twilight vision).

Names & Taxonomyi

Protein namesi
Recommended name:
Retinaldehyde-binding protein 1
Alternative name(s):
Cellular retinaldehyde-binding protein
Gene namesi
Name:RLBP1
Synonyms:CRALBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:10024. RLBP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Bothnia retinal dystrophy (BRD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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 OMIM:607475
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015172234R → W in BRD. 1 PublicationCorresponds to variant rs28933990dbSNPEnsembl.1
Rod-cone dystrophy Newfoundland (NFRCD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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 OMIM:607476
Retinitis punctata albescens (RPA)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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 OMIM:136880
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005140151R → Q in RPA; loss of ability to bind 11-cis-retinaldehyde. 2 PublicationsCorresponds to variant rs28933989dbSNPEnsembl.1
Natural variantiVAR_037317226M → K in RPA. 1 PublicationCorresponds to variant rs137853291dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi6017.
MalaCardsiRLBP1.
MIMi136880. phenotype.
607475. phenotype.
607476. phenotype.
OpenTargetsiENSG00000140522.
Orphaneti85128. Bothnia retinal dystrophy.
227796. Fundus albipunctatus.
791. Retinitis pigmentosa.
52427. Retinitis punctata albescens.
PharmGKBiPA34397.

Chemistry databases

DrugBankiDB00162. Vitamin A.

Polymorphism and mutation databases

BioMutaiRLBP1.
DMDMi117391.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000793302 – 317Retinaldehyde-binding protein 1Add BLAST316

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP12271.
PeptideAtlasiP12271.
PRIDEiP12271.

PTM databases

iPTMnetiP12271.
PhosphoSitePlusiP12271.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiENSG00000140522.
CleanExiHS_RLBP1.
ExpressionAtlasiP12271. baseline and differential.
GenevisibleiP12271. HS.

Interactioni

Protein-protein interaction databases

BioGridi111949. 2 interactors.
IntActiP12271. 1 interactor.
STRINGi9606.ENSP00000268125.

Structurei

Secondary structure

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 29Combined sources3
Beta strandi33 – 35Combined sources3
Turni41 – 43Combined sources3
Helixi44 – 49Combined sources6
Turni50 – 52Combined sources3
Turni55 – 57Combined sources3
Helixi58 – 74Combined sources17
Turni75 – 77Combined sources3
Helixi79 – 87Combined sources9
Turni88 – 90Combined sources3
Helixi93 – 102Combined sources10
Turni103 – 105Combined sources3
Helixi107 – 123Combined sources17
Helixi125 – 127Combined sources3
Turni128 – 130Combined sources3
Helixi133 – 141Combined sources9
Beta strandi144 – 147Combined sources4
Beta strandi157 – 162Combined sources6
Turni168 – 170Combined sources3
Helixi173 – 187Combined sources15
Helixi191 – 196Combined sources6
Beta strandi198 – 203Combined sources6
Helixi209 – 214Combined sources6
Helixi217 – 228Combined sources12
Turni232 – 234Combined sources3
Beta strandi235 – 242Combined sources8
Helixi247 – 254Combined sources8
Helixi255 – 257Combined sources3
Helixi260 – 263Combined sources4
Beta strandi266 – 270Combined sources5
Helixi274 – 279Combined sources6
Helixi282 – 284Combined sources3
Helixi287 – 289Combined sources3
Beta strandi291 – 293Combined sources3
Helixi299 – 305Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XGGmodel-A67-295[»]
1XGHmodel-A67-295[»]
3HX3X-ray1.69A2-317[»]
3HY5X-ray3.04A2-317[»]
4CIZX-ray3.40A1-317[»]
4CJ6X-ray1.90A1-317[»]
ProteinModelPortaliP12271.
SMRiP12271.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12271.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini136 – 297CRAL-TRIOPROSITE-ProRule annotationAdd BLAST162

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1471. Eukaryota.
ENOG410XRSQ. LUCA.
GeneTreeiENSGT00550000074253.
HOGENOMiHOG000059544.
HOVERGENiHBG004720.
InParanoidiP12271.
KOiK19625.
OMAiFHVGRAY.
OrthoDBiEOG091G0KN0.
PhylomeDBiP12271.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
InterProiIPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
IPR032941. RLBP1.
[Graphical view]
PANTHERiPTHR10174:SF126. PTHR10174:SF126. 1 hit.
PfamiPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
PRINTSiPR00180. CRETINALDHBP.
SMARTiSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12271-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEGVGTFRM VPEEEQELRA QLEQLTTKDH GPVFGPCSQL PRHTLQKAKD
60 70 80 90 100
ELNEREETRE EAVRELQEMV QAQAASGEEL AVAVAERVQE KDSGFFLRFI
110 120 130 140 150
RARKFNVGRA YELLRGYVNF RLQYPELFDS LSPEAVRCTI EAGYPGVLSS
160 170 180 190 200
RDKYGRVVML FNIENWQSQE ITFDEILQAY CFILEKLLEN EETQINGFCI
210 220 230 240 250
IENFKGFTMQ QAASLRTSDL RKMVDMLQDS FPARFKAIHF IHQPWYFTTT
260 270 280 290 300
YNVVKPFLKS KLLERVFVHG DDLSGFYQEI DENILPSDFG GTLPKYDGKA
310
VAEQLFGPQA QAENTAF
Length:317
Mass (Da):36,474
Last modified:January 23, 2007 - v2
Checksum:i80A3B0AE65FDA6EB
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005140151R → Q in RPA; loss of ability to bind 11-cis-retinaldehyde. 2 PublicationsCorresponds to variant rs28933989dbSNPEnsembl.1
Natural variantiVAR_037317226M → K in RPA. 1 PublicationCorresponds to variant rs137853291dbSNPEnsembl.1
Natural variantiVAR_015172234R → W in BRD. 1 PublicationCorresponds to variant rs28933990dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04213 mRNA. Translation: AAA60251.1.
L34219 Genomic DNA. Translation: AAA65123.1.
AK312457 mRNA. Translation: BAG35364.1.
CH471101 Genomic DNA. Translation: EAX02038.1.
BC004199 mRNA. Translation: AAH04199.1.
CCDSiCCDS32324.1.
PIRiB31955.
RefSeqiNP_000317.1. NM_000326.4.
XP_011520172.1. XM_011521870.2.
UniGeneiHs.1933.

Genome annotation databases

EnsembliENST00000268125; ENSP00000268125; ENSG00000140522.
GeneIDi6017.
KEGGihsa:6017.
UCSCiuc002bnl.4. human.

Cross-referencesi

Web resourcesi

Mutations of the RLBP1 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04213 mRNA. Translation: AAA60251.1.
L34219 Genomic DNA. Translation: AAA65123.1.
AK312457 mRNA. Translation: BAG35364.1.
CH471101 Genomic DNA. Translation: EAX02038.1.
BC004199 mRNA. Translation: AAH04199.1.
CCDSiCCDS32324.1.
PIRiB31955.
RefSeqiNP_000317.1. NM_000326.4.
XP_011520172.1. XM_011521870.2.
UniGeneiHs.1933.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XGGmodel-A67-295[»]
1XGHmodel-A67-295[»]
3HX3X-ray1.69A2-317[»]
3HY5X-ray3.04A2-317[»]
4CIZX-ray3.40A1-317[»]
4CJ6X-ray1.90A1-317[»]
ProteinModelPortaliP12271.
SMRiP12271.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111949. 2 interactors.
IntActiP12271. 1 interactor.
STRINGi9606.ENSP00000268125.

Chemistry databases

DrugBankiDB00162. Vitamin A.

PTM databases

iPTMnetiP12271.
PhosphoSitePlusiP12271.

Polymorphism and mutation databases

BioMutaiRLBP1.
DMDMi117391.

Proteomic databases

PaxDbiP12271.
PeptideAtlasiP12271.
PRIDEiP12271.

Protocols and materials databases

DNASUi6017.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268125; ENSP00000268125; ENSG00000140522.
GeneIDi6017.
KEGGihsa:6017.
UCSCiuc002bnl.4. human.

Organism-specific databases

CTDi6017.
DisGeNETi6017.
GeneCardsiRLBP1.
GeneReviewsiRLBP1.
HGNCiHGNC:10024. RLBP1.
MalaCardsiRLBP1.
MIMi136880. phenotype.
180090. gene.
607475. phenotype.
607476. phenotype.
neXtProtiNX_P12271.
OpenTargetsiENSG00000140522.
Orphaneti85128. Bothnia retinal dystrophy.
227796. Fundus albipunctatus.
791. Retinitis pigmentosa.
52427. Retinitis punctata albescens.
PharmGKBiPA34397.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1471. Eukaryota.
ENOG410XRSQ. LUCA.
GeneTreeiENSGT00550000074253.
HOGENOMiHOG000059544.
HOVERGENiHBG004720.
InParanoidiP12271.
KOiK19625.
OMAiFHVGRAY.
OrthoDBiEOG091G0KN0.
PhylomeDBiP12271.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000140522-MONOMER.
ZFISH:ENSG00000140522-MONOMER.
ReactomeiR-HSA-2187335. The retinoid cycle in cones (daylight vision).
R-HSA-2453864. Retinoid cycle disease events.
R-HSA-2453902. The canonical retinoid cycle in rods (twilight vision).

Miscellaneous databases

ChiTaRSiRLBP1. human.
EvolutionaryTraceiP12271.
GeneWikiiRetinaldehyde-binding_protein_1.
GenomeRNAii6017.
PROiP12271.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000140522.
CleanExiHS_RLBP1.
ExpressionAtlasiP12271. baseline and differential.
GenevisibleiP12271. HS.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
InterProiIPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
IPR032941. RLBP1.
[Graphical view]
PANTHERiPTHR10174:SF126. PTHR10174:SF126. 1 hit.
PfamiPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
PRINTSiPR00180. CRETINALDHBP.
SMARTiSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRLBP1_HUMAN
AccessioniPrimary (citable) accession number: P12271
Secondary accession number(s): B2R667
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 161 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.