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Protein

Retinol-binding protein 4

Gene

Rbp4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD
  • retinal binding Source: UniProtKB-KW
  • retinol binding Source: RGD
  • retinol transporter activity Source: RGD
  • transporter activity Source: RGD

GO - Biological processi

  • eye development Source: Ensembl
  • gluconeogenesis Source: Ensembl
  • glucose homeostasis Source: Ensembl
  • maintenance of gastrointestinal epithelium Source: Ensembl
  • positive regulation of insulin secretion Source: Ensembl
  • response to ethanol Source: RGD
  • response to retinoic acid Source: Ensembl
  • retinol metabolic process Source: RGD
  • retinol transport Source: RGD
  • transport Source: RGD
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

ReactomeiR-RNO-2453902. The canonical retinoid cycle in rods (twilight vision).
R-RNO-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
Gene namesi
Name:Rbp4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3546. Rbp4.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 201183Retinol-binding protein 4PRO_0000017970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi22 ↔ 178By similarity
Disulfide bondi88 ↔ 192By similarity
Disulfide bondi138 ↔ 147By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP04916.
PRIDEiP04916.

Expressioni

Gene expression databases

BgeeiENSRNOG00000015518.
ExpressionAtlasiP04916. baseline and differential.
GenevisibleiP04916. RN.

Interactioni

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021055.

Structurei

3D structure databases

ProteinModelPortaliP04916.
SMRiP04916. Positions 19-192.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJHC. Eukaryota.
ENOG4111K1Y. LUCA.
GeneTreeiENSGT00510000047107.
HOGENOMiHOG000293156.
HOVERGENiHBG004493.
InParanoidiP04916.
KOiK18271.
OMAiGHMSATA.
OrthoDBiEOG091G0KIM.
PhylomeDBiP04916.
TreeFamiTF331445.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002449. Retinol-bd/Purpurin.
[Graphical view]
PANTHERiPTHR11873. PTHR11873. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFiPIRSF036893. Lipocalin_ApoD. 1 hit.
PIRSF500204. RBP_purpurin. 1 hit.
PRINTSiPR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P04916-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEWVWALVLL AALGGGSAER DCRVSSFRVK ENFDKARFSG LWYAIAKKDP
60 70 80 90 100
EGLFLQDNII AEFSVDEKGH MSATAKGRVR LLSNWEVCAD MVGTFTDTED
110 120 130 140 150
PAKFKMKYWG VASFLQRGND DHWIIDTDYD TFALQYSCRL QNLDGTCADS
160 170 180 190 200
YSFVFSRDPN GLTPETRRLV RQRQEELCLE RQYRWIEHNG YCQSRPSRNS

L
Length:201
Mass (Da):23,220
Last modified:August 13, 1987 - v1
Checksum:iE6737E293B37A30A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03046, M10610 Genomic DNA. Translation: AAA42018.1.
M10934 mRNA. Translation: AAA42020.1.
PIRiA92493. VART.
RefSeqiNP_037294.1. NM_013162.1.
UniGeneiRn.108214.

Genome annotation databases

EnsembliENSRNOT00000021055; ENSRNOP00000021055; ENSRNOG00000015518.
GeneIDi25703.
KEGGirno:25703.
UCSCiRGD:3546. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03046, M10610 Genomic DNA. Translation: AAA42018.1.
M10934 mRNA. Translation: AAA42020.1.
PIRiA92493. VART.
RefSeqiNP_037294.1. NM_013162.1.
UniGeneiRn.108214.

3D structure databases

ProteinModelPortaliP04916.
SMRiP04916. Positions 19-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021055.

Proteomic databases

PaxDbiP04916.
PRIDEiP04916.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021055; ENSRNOP00000021055; ENSRNOG00000015518.
GeneIDi25703.
KEGGirno:25703.
UCSCiRGD:3546. rat.

Organism-specific databases

CTDi5950.
RGDi3546. Rbp4.

Phylogenomic databases

eggNOGiENOG410IJHC. Eukaryota.
ENOG4111K1Y. LUCA.
GeneTreeiENSGT00510000047107.
HOGENOMiHOG000293156.
HOVERGENiHBG004493.
InParanoidiP04916.
KOiK18271.
OMAiGHMSATA.
OrthoDBiEOG091G0KIM.
PhylomeDBiP04916.
TreeFamiTF331445.

Enzyme and pathway databases

ReactomeiR-RNO-2453902. The canonical retinoid cycle in rods (twilight vision).
R-RNO-975634. Retinoid metabolism and transport.

Miscellaneous databases

PROiP04916.

Gene expression databases

BgeeiENSRNOG00000015518.
ExpressionAtlasiP04916. baseline and differential.
GenevisibleiP04916. RN.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002449. Retinol-bd/Purpurin.
[Graphical view]
PANTHERiPTHR11873. PTHR11873. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFiPIRSF036893. Lipocalin_ApoD. 1 hit.
PIRSF500204. RBP_purpurin. 1 hit.
PRINTSiPR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRET4_RAT
AccessioniPrimary (citable) accession number: P04916
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: September 7, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.