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Protein

Retinol-binding protein 4

Gene

RBP4

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 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

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

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_0000017969Add
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

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000009070.

Structurei

3D structure databases

ProteinModelPortaliP06912.
SMRiP06912. Positions 19-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJHC. Eukaryota.
ENOG4111K1Y. LUCA.
HOGENOMiHOG000293156.
HOVERGENiHBG004493.
InParanoidiP06912.
KOiK18271.

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.

P06912-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEWVWALVLL AALGSGRGER DCRVSSFRVK ENFDKARFAG TWYAMAKKDP
60 70 80 90 100
EGLFLQDNIV AEFSVDENGH MSATAKGRVR LLNNWDVCAD MVGTFTDTED
110 120 130 140 150
PAKFKMKYWG VASFLQRGND DHWIIDTDYD TFAVQYSCRL LNFDGTCADS
160 170 180 190 200
YSFVFSRDPH GLPPDVQKLV RQRQEELCLS RQYRLIVHNG YCDDKSVRNL

L
Length:201
Mass (Da):23,102
Last modified:October 1, 1996 - v2
Checksum:i4153FCF050184136
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S45958 mRNA. Translation: AAB23582.1.
PIRiA49178. VARB.
RefSeqiNP_001075790.1. NM_001082321.1.
UniGeneiOcu.3311.

Genome annotation databases

GeneIDi100009161.
KEGGiocu:100009161.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S45958 mRNA. Translation: AAB23582.1.
PIRiA49178. VARB.
RefSeqiNP_001075790.1. NM_001082321.1.
UniGeneiOcu.3311.

3D structure databases

ProteinModelPortaliP06912.
SMRiP06912. Positions 19-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000009070.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009161.
KEGGiocu:100009161.

Organism-specific databases

CTDi5950.

Phylogenomic databases

eggNOGiENOG410IJHC. Eukaryota.
ENOG4111K1Y. LUCA.
HOGENOMiHOG000293156.
HOVERGENiHBG004493.
InParanoidiP06912.
KOiK18271.

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...

Publicationsi

  1. "The lacrimal gland synthesizes retinol-binding protein."
    Lee S.Y., Ubels J.L., Soprano D.R.
    Exp. Eye Res. 55:163-171(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Amino acid sequence homologies between rabbit, rat, and human serum retinol-binding proteins."
    Sundelin J., Laurent B.C., Anundi H., Traegaardh L., Larhammar D., Bjoerck L., Eriksson U., Aakerstroem B., Jones A., Newcomer M., Peterson P.A., Rask L.
    J. Biol. Chem. 260:6472-6480(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-201.

Entry informationi

Entry nameiRET4_RABIT
AccessioniPrimary (citable) accession number: P06912
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 1, 1996
Last modified: November 11, 2015
This is version 102 of the entry and version 2 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.