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Protein

Retinol-binding protein 4

Gene

RBP4

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

Functioni

Retinol-binding protein that mediates retinol transport in blood plasma (PubMed:5541771). Delivers retinol from the liver stores to the peripheral tissues (Probable). Transfers the bound all-trans retinol to STRA6, that then facilitates retinol transport across the cell membrane (PubMed:22665496).Curated1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei116SubstrateBy similarity1

GO - Molecular functioni

  • protein heterodimerization activity Source: Ensembl
  • retinal binding Source: UniProtKB-KW
  • retinol binding Source: BHF-UCL
  • retinol transmembrane transporter activity Source: BHF-UCL

GO - Biological processi

Keywordsi

Biological processSensory transduction, Transport, Vision
LigandRetinol-binding, Vitamin A

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000138207-MONOMER
ReactomeiR-HSA-2453864 Retinoid cycle disease events
R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)
R-HSA-6809583 Retinoid metabolism disease events
R-HSA-975634 Retinoid metabolism and transport

Names & Taxonomyi

Protein namesi
Recommended name:
Retinol-binding protein 4
Alternative name(s):
Plasma retinol-binding protein
Short name:
PRBP
Short name:
RBP
Cleaved into the following 4 chains:
Gene namesi
Name:RBP4
ORF Names:PRO2222
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000138207.12
HGNCiHGNC:9922 RBP4
MIMi180250 gene
neXtProtiNX_P02753

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Retinal dystrophy, iris coloboma, and comedogenic acne syndrome (RDCCAS)3 Publications
The disease is caused by mutations affecting the gene represented in this entry. Loss of functional RBP4 protein results in serum retinol deficiency. Lack of normal levels of retinol impairs the visual cycle leading to night blindness at early stages; prolonged deficiency may lead to retinal degeneration. Additionally, retinol deficiency may result in dry skin, increased susceptibility to infection and acne (PubMed:23189188).1 Publication
Disease descriptionA disease characterized by retinal degeneration, ocular colobomas involving both the anterior and posterior segment, impaired night vision and loss of visual acuity. Additional characteristic features include developmental abnormalities and severe acne.
See also OMIM:615147
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00927659I → N in RDCCAS. 2 PublicationsCorresponds to variant dbSNP:rs121918584EnsemblClinVar.1
Natural variantiVAR_00927793G → D in RDCCAS. 2 PublicationsCorresponds to variant dbSNP:rs121918585EnsemblClinVar.1
Microphthalmia, isolated, with coloboma, 10 (MCOPCB10)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present. Ocular colobomas are a set of malformations resulting from abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure).
See also OMIM:616428
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07385673A → T in MCOPCB10; dramatic reduction in retinol binding; has greater affinity for the STRA6 receptor. 1 PublicationCorresponds to variant dbSNP:rs794726862EnsemblClinVar.1
Natural variantiVAR_07385775A → T in MCOPCB10; dramatic reduction in retinol binding; has greater affinity for the STRA6 receptor. 1 PublicationCorresponds to variant dbSNP:rs794726861EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Microphthalmia

Organism-specific databases

DisGeNETi5950
MalaCardsiRBP4
MIMi615147 phenotype
616428 phenotype
OpenTargetsiENSG00000138207
Orphaneti352718 Progressive retinal dystrophy due to retinol transport defect
PharmGKBiPA34289

Chemistry databases

ChEMBLiCHEMBL3100
DrugBankiDB06985 2-[({4-[2-(trifluoromethyl)phenyl]piperidin-1-yl}carbonyl)amino]benzoic acid
DB05076 Fenretinide
DB03917 N-Ethyl Retinamide
DB00162 Vitamin A
GuidetoPHARMACOLOGYi2549

Polymorphism and mutation databases

BioMutaiRBP4
DMDMi62298174

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 183 PublicationsAdd BLAST18
ChainiPRO_000001796119 – 201Retinol-binding protein 4Add BLAST183
ChainiPRO_000001796219 – 200Plasma retinol-binding protein(1-182)Add BLAST182
ChainiPRO_000001796319 – 199Plasma retinol-binding protein(1-181)Add BLAST181
ChainiPRO_000001796419 – 197Plasma retinol-binding protein(1-179)Add BLAST179
ChainiPRO_000001796519 – 194Plasma retinol-binding protein(1-176)Add BLAST176

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi22 ↔ 1781 Publication
Disulfide bondi88 ↔ 1921 Publication
Disulfide bondi138 ↔ 1471 Publication
Modified residuei139Omega-N-methylarginineBy similarity1

Keywords - PTMi

Disulfide bond, Methylation

Proteomic databases

MaxQBiP02753
PaxDbiP02753
PeptideAtlasiP02753
PRIDEiP02753
ProteomicsDBi12699
51582

2D gel databases

SWISS-2DPAGEiP02753

PTM databases

iPTMnetiP02753
PhosphoSitePlusiP02753

Expressioni

Tissue specificityi

Detected in blood plasma and in urine (at protein level).2 Publications

Gene expression databases

BgeeiENSG00000138207 Expressed in 178 organ(s), highest expression level in liver
CleanExiHS_RBP4
ExpressionAtlasiP02753 baseline and differential
GenevisibleiP02753 HS

Organism-specific databases

HPAiCAB004555
HPA001641

Interactioni

Subunit structurei

Interacts with TTR (PubMed:5541771, PubMed:7754382, PubMed:10052934, PubMed:19021760). Interaction with TTR prevents its loss by filtration through the kidney glomeruli (Probable). Interacts with STRA6 (PubMed:22665496, PubMed:25910211).Curated6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TTRO552452EBI-2116134,EBI-7038226From Crocodylus porosus.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111884, 13 interactors
CORUMiP02753
IntActiP02753, 4 interactors
MINTiP02753
STRINGi9606.ENSP00000360519

Chemistry databases

BindingDBiP02753

Structurei

Secondary structure

1201
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP02753
SMRiP02753
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02753

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJHC Eukaryota
ENOG4111K1Y LUCA
GeneTreeiENSGT00510000047107
HOVERGENiHBG004493
InParanoidiP02753
KOiK18271
OMAiGHMSATA
OrthoDBiEOG091G0KIM
PhylomeDBiP02753
TreeFamiTF331445

Family and domain databases

Gene3Di2.40.128.20, 1 hit
InterProiView protein in InterPro
IPR012674 Calycin
IPR022271 Lipocalin_ApoD
IPR022272 Lipocalin_CS
IPR000566 Lipocln_cytosolic_FA-bd_dom
IPR002449 Retinol-bd/Purpurin
PANTHERiPTHR11873 PTHR11873, 1 hit
PfamiView protein in Pfam
PF00061 Lipocalin, 1 hit
PIRSFiPIRSF036893 Lipocalin_ApoD, 1 hit
PIRSF500204 RBP_purpurin, 1 hit
PRINTSiPR01174 RETINOLBNDNG
SUPFAMiSSF50814 SSF50814, 1 hit
PROSITEiView protein in PROSITE
PS00213 LIPOCALIN, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.iShow all

P02753-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKWVWALLLL AALGSGRAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP
60 70 80 90 100
EGLFLQDNIV AEFSVDETGQ MSATAKGRVR LLNNWDVCAD MVGTFTDTED
110 120 130 140 150
PAKFKMKYWG VASFLQKGND DHWIVDTDYD TYAVQYSCRL LNLDGTCADS
160 170 180 190 200
YSFVFSRDPN GLPPEAQKIV RQRQEELCLA RQYRLIVHNG YCDGRSERNL

L
Length:201
Mass (Da):23,010
Last modified:March 29, 2005 - v3
Checksum:i660C6DD8CC9B811A
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5VY30Q5VY30_HUMAN
Retinol-binding protein
RBP4 hCG_37964
199Annotation score:

Sequence cautioni

The sequence AAF69622 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8L → F in AAH20633 (PubMed:15489334).Curated1
Sequence conflicti13 – 17LGSGR → WAA in CAA24959 (PubMed:6316270).Curated5
Sequence conflicti13 – 17LGSGR → WAA in CAA26553 (PubMed:2998779).Curated5

Mass spectrometryi

Molecular mass is 21063.46±1.88 Da from positions 17 - 199. Determined by ESI. 1 Publication
Molecular mass is 20534 Da from positions 19 - 197. Determined by MALDI. 1 Publication
Molecular mass is 20162 Da from positions 19 - 194. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00927659I → N in RDCCAS. 2 PublicationsCorresponds to variant dbSNP:rs121918584EnsemblClinVar.1
Natural variantiVAR_07385673A → T in MCOPCB10; dramatic reduction in retinol binding; has greater affinity for the STRA6 receptor. 1 PublicationCorresponds to variant dbSNP:rs794726862EnsemblClinVar.1
Natural variantiVAR_07385775A → T in MCOPCB10; dramatic reduction in retinol binding; has greater affinity for the STRA6 receptor. 1 PublicationCorresponds to variant dbSNP:rs794726861EnsemblClinVar.1
Natural variantiVAR_00927793G → D in RDCCAS. 2 PublicationsCorresponds to variant dbSNP:rs121918585EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00129 mRNA Translation: CAA24959.1
AL356214 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW50065.1
CH471066 Genomic DNA Translation: EAW50066.1
CH471066 Genomic DNA Translation: EAW50067.1
BC020633 mRNA Translation: AAH20633.1
X02775 Genomic DNA Translation: CAA26553.1
X02824 Genomic DNA Translation: CAB46489.1
AF119868 mRNA Translation: AAF69622.1 Different initiation.
AF025334 Genomic DNA Translation: AAC02945.1
AF025335 Genomic DNA Translation: AAC02946.1
CCDSiCCDS31249.1
PIRiA93494 VAHU
RefSeqiNP_001310446.1, NM_001323517.1
NP_001310447.1, NM_001323518.1
NP_006735.2, NM_006744.3
UniGeneiHs.50223

Genome annotation databases

EnsembliENST00000371464; ENSP00000360519; ENSG00000138207
ENST00000371467; ENSP00000360522; ENSG00000138207
GeneIDi5950
KEGGihsa:5950
UCSCiuc001kit.4 human

Similar proteinsi

Cross-referencesi

Web resourcesi

Mutations of the RBP4 gene

Retina International's Scientific Newsletter

Wikipedia

Retinol-binding protein 4 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00129 mRNA Translation: CAA24959.1
AL356214 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW50065.1
CH471066 Genomic DNA Translation: EAW50066.1
CH471066 Genomic DNA Translation: EAW50067.1
BC020633 mRNA Translation: AAH20633.1
X02775 Genomic DNA Translation: CAA26553.1
X02824 Genomic DNA Translation: CAB46489.1
AF119868 mRNA Translation: AAF69622.1 Different initiation.
AF025334 Genomic DNA Translation: AAC02945.1
AF025335 Genomic DNA Translation: AAC02946.1
CCDSiCCDS31249.1
PIRiA93494 VAHU
RefSeqiNP_001310446.1, NM_001323517.1
NP_001310447.1, NM_001323518.1
NP_006735.2, NM_006744.3
UniGeneiHs.50223

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BRPX-ray2.50A19-200[»]
1BRQX-ray2.50A19-200[»]
1JYDX-ray1.70A19-200[»]
1JYJX-ray2.00A19-200[»]
1QABX-ray3.20E/F22-201[»]
1RBPX-ray2.00A19-200[»]
1RLBX-ray3.10E/F19-192[»]
2WQ9X-ray1.65A19-192[»]
2WQAX-ray2.85E/F19-194[»]
2WR6X-ray1.80A19-192[»]
3BSZX-ray3.38E/F19-194[»]
3FMZX-ray2.90A/B19-201[»]
4O9SX-ray2.30A/B19-201[»]
4PSQX-ray2.40A/B19-201[»]
5NTYX-ray2.00A19-200[»]
5NU2X-ray1.50A19-200[»]
5NU6X-ray1.68A19-200[»]
5NU7X-ray1.50A19-200[»]
5NU8X-ray1.59A19-200[»]
5NU9X-ray1.50A19-200[»]
5NUAX-ray1.60A19-200[»]
5NUBX-ray1.60A19-200[»]
ProteinModelPortaliP02753
SMRiP02753
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111884, 13 interactors
CORUMiP02753
IntActiP02753, 4 interactors
MINTiP02753
STRINGi9606.ENSP00000360519

Chemistry databases

BindingDBiP02753
ChEMBLiCHEMBL3100
DrugBankiDB06985 2-[({4-[2-(trifluoromethyl)phenyl]piperidin-1-yl}carbonyl)amino]benzoic acid
DB05076 Fenretinide
DB03917 N-Ethyl Retinamide
DB00162 Vitamin A
GuidetoPHARMACOLOGYi2549

PTM databases

iPTMnetiP02753
PhosphoSitePlusiP02753

Polymorphism and mutation databases

BioMutaiRBP4
DMDMi62298174

2D gel databases

SWISS-2DPAGEiP02753

Proteomic databases

MaxQBiP02753
PaxDbiP02753
PeptideAtlasiP02753
PRIDEiP02753
ProteomicsDBi12699
51582

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371464; ENSP00000360519; ENSG00000138207
ENST00000371467; ENSP00000360522; ENSG00000138207
GeneIDi5950
KEGGihsa:5950
UCSCiuc001kit.4 human

Organism-specific databases

CTDi5950
DisGeNETi5950
EuPathDBiHostDB:ENSG00000138207.12
GeneCardsiRBP4
H-InvDBiHIX0009047
HGNCiHGNC:9922 RBP4
HPAiCAB004555
HPA001641
MalaCardsiRBP4
MIMi180250 gene
615147 phenotype
616428 phenotype
neXtProtiNX_P02753
OpenTargetsiENSG00000138207
Orphaneti352718 Progressive retinal dystrophy due to retinol transport defect
PharmGKBiPA34289
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJHC Eukaryota
ENOG4111K1Y LUCA
GeneTreeiENSGT00510000047107
HOVERGENiHBG004493
InParanoidiP02753
KOiK18271
OMAiGHMSATA
OrthoDBiEOG091G0KIM
PhylomeDBiP02753
TreeFamiTF331445

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000138207-MONOMER
ReactomeiR-HSA-2453864 Retinoid cycle disease events
R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)
R-HSA-6809583 Retinoid metabolism disease events
R-HSA-975634 Retinoid metabolism and transport

Miscellaneous databases

ChiTaRSiRBP4 human
EvolutionaryTraceiP02753
GeneWikiiRetinol_binding_protein_4
GenomeRNAii5950
PROiPR:P02753
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138207 Expressed in 178 organ(s), highest expression level in liver
CleanExiHS_RBP4
ExpressionAtlasiP02753 baseline and differential
GenevisibleiP02753 HS

Family and domain databases

Gene3Di2.40.128.20, 1 hit
InterProiView protein in InterPro
IPR012674 Calycin
IPR022271 Lipocalin_ApoD
IPR022272 Lipocalin_CS
IPR000566 Lipocln_cytosolic_FA-bd_dom
IPR002449 Retinol-bd/Purpurin
PANTHERiPTHR11873 PTHR11873, 1 hit
PfamiView protein in Pfam
PF00061 Lipocalin, 1 hit
PIRSFiPIRSF036893 Lipocalin_ApoD, 1 hit
PIRSF500204 RBP_purpurin, 1 hit
PRINTSiPR01174 RETINOLBNDNG
SUPFAMiSSF50814 SSF50814, 1 hit
PROSITEiView protein in PROSITE
PS00213 LIPOCALIN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRET4_HUMAN
AccessioniPrimary (citable) accession number: P02753
Secondary accession number(s): D3DR38
, O43478, O43479, Q5VY24, Q8WWA3, Q9P178
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 29, 2005
Last modified: September 12, 2018
This is version 210 of the entry and version 3 of the sequence. See 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, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health

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