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Protein

Retinaldehyde-binding protein 1

Gene

Rlbp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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'.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei18011-cis-retinalBy similarity1
Binding sitei20211-cis-retinalBy similarity1

GO - Molecular functioni

  • 11-cis retinal binding Source: MGI
  • retinol binding Source: UniProtKB-KW
  • transporter activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Transport, Vision

Keywords - Ligandi

Retinol-binding

Enzyme and pathway databases

ReactomeiR-MMU-2187335. The retinoid cycle in cones (daylight vision).
R-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:97930. Rlbp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000793312 – 317Retinaldehyde-binding protein 1Add BLAST316

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Z275.
PaxDbiQ9Z275.
PRIDEiQ9Z275.

PTM databases

iPTMnetiQ9Z275.
PhosphoSitePlusiQ9Z275.

Expressioni

Tissue specificityi

Retina and pineal gland.

Gene expression databases

BgeeiENSMUSG00000039194.
CleanExiMM_RLBP1.
ExpressionAtlasiQ9Z275. baseline and differential.
GenevisibleiQ9Z275. MM.

Interactioni

Protein-protein interaction databases

BioGridi202898. 1 interactor.
STRINGi10090.ENSMUSP00000054545.

Structurei

3D structure databases

ProteinModelPortaliQ9Z275.
SMRiQ9Z275.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ9Z275.
KOiK19625.
OMAiFHVGRAY.
OrthoDBiEOG091G0KN0.
PhylomeDBiQ9Z275.

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. 2 hits.
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.

Q9Z275-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDGVGTFRM VPEEEQELRA QLEQLTTKDH GPVFGPCSQL PRHTLQKAKD
60 70 80 90 100
ELNEKEETRE EAVRELQELV QAQAASGEEL ALAVAERVQA RDSAFLLRFI
110 120 130 140 150
RARKFDVGRA YELLKGYVNF RLQYPELFDS LSMEALRCTI EAGYPGVLSS
160 170 180 190 200
RDKYGRVVML FNIENWHCEE VTFDEILQAY CFILEKLLEN EETQINGFCI
210 220 230 240 250
VENFKGFTMQ QAAGLRPSDL KKMVDMLQDS FPARFKAIHF IHQPWYFTTT
260 270 280 290 300
YNVVKPFLKN KLLQRVFVHG DDLDGFFQEI DENILPADFG GTLPKYDGKV
310
VAEQLFGPRA EVENTAL
Length:317
Mass (Da):36,408
Last modified:January 23, 2007 - v3
Checksum:iB337341AAACFAE59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084642
, AF084638, AF084639, AF084640, AF084641 Genomic DNA. Translation: AAC99427.1.
BC016268 mRNA. Translation: AAH16268.1.
CCDSiCCDS39990.1.
RefSeqiNP_001166954.1. NM_001173483.1.
NP_065624.1. NM_020599.2.
XP_006540780.1. XM_006540717.1.
XP_006540781.1. XM_006540718.1.
UniGeneiMm.41653.

Genome annotation databases

EnsembliENSMUST00000053718; ENSMUSP00000054545; ENSMUSG00000039194.
ENSMUST00000179243; ENSMUSP00000137143; ENSMUSG00000039194.
GeneIDi19771.
KEGGimmu:19771.
UCSCiuc009hye.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084642
, AF084638, AF084639, AF084640, AF084641 Genomic DNA. Translation: AAC99427.1.
BC016268 mRNA. Translation: AAH16268.1.
CCDSiCCDS39990.1.
RefSeqiNP_001166954.1. NM_001173483.1.
NP_065624.1. NM_020599.2.
XP_006540780.1. XM_006540717.1.
XP_006540781.1. XM_006540718.1.
UniGeneiMm.41653.

3D structure databases

ProteinModelPortaliQ9Z275.
SMRiQ9Z275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202898. 1 interactor.
STRINGi10090.ENSMUSP00000054545.

PTM databases

iPTMnetiQ9Z275.
PhosphoSitePlusiQ9Z275.

Proteomic databases

MaxQBiQ9Z275.
PaxDbiQ9Z275.
PRIDEiQ9Z275.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053718; ENSMUSP00000054545; ENSMUSG00000039194.
ENSMUST00000179243; ENSMUSP00000137143; ENSMUSG00000039194.
GeneIDi19771.
KEGGimmu:19771.
UCSCiuc009hye.2. mouse.

Organism-specific databases

CTDi6017.
MGIiMGI:97930. Rlbp1.

Phylogenomic databases

eggNOGiKOG1471. Eukaryota.
ENOG410XRSQ. LUCA.
GeneTreeiENSGT00550000074253.
HOGENOMiHOG000059544.
HOVERGENiHBG004720.
InParanoidiQ9Z275.
KOiK19625.
OMAiFHVGRAY.
OrthoDBiEOG091G0KN0.
PhylomeDBiQ9Z275.

Enzyme and pathway databases

ReactomeiR-MMU-2187335. The retinoid cycle in cones (daylight vision).
R-MMU-2453902. The canonical retinoid cycle in rods (twilight vision).

Miscellaneous databases

PROiQ9Z275.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000039194.
CleanExiMM_RLBP1.
ExpressionAtlasiQ9Z275. baseline and differential.
GenevisibleiQ9Z275. MM.

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. 2 hits.
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_MOUSE
AccessioniPrimary (citable) accession number: Q9Z275
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.