[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. PubMed=4044565 [NCBI, ExPASy, EBI, Israel, Japan] Laurent B.C., Nilsson M.H.L., Bavik C.O., Jones T.A., Sundelin J., Peterson P.A.; "Characterization of the rat retinol-binding protein gene and its comparison to the three-dimensional structure of the protein."; J. Biol. Chem. 260:11476-11480(1985).
[2]	PROTEIN SEQUENCE OF 19-59, AND NUCLEOTIDE SEQUENCE OF 30-201. PubMed=3838985 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Amino acid sequence homologies between rabbit, rat, and human serum retinol-binding proteins."; J. Biol. Chem. 260:6472-6480(1985).

Comments

FUNCTION: 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.
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

K03046; AAA42018.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M10610; AAA42018.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M10934; AAA42020.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A92493; VART.

NP_037294.1; -.

3D structure databases

HSSP

P02753; 1RBP. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

SMR

P04916; 19-192.

ModBase

P04916.

Organism-specific databases

RGD

3546; Rbp4.

Gene expression databases

ArrayExpress

P04916; -.

GermOnline

ENSRNOG00000015518; Rattus norvegicus.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0016918;	Molecular function: retinal binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019841;	Molecular function: retinol binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR012674; Calycin.
IPR002345; Lipocalin.
IPR000566; Lipocln_cytFABP.
IPR002449; Retinol_bd.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.128.20; Calycin; 1.

PANTHER

PTHR11873; Retinol_bd; 1.

Pfam

PF00061; Lipocalin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00179; LIPOCALIN.
PR01174; RETINOLBNDNG.

PROSITE

PS00213; LIPOCALIN; 1.

Genome annotation databases

Ensembl

ENSRNOG00000015518; Rattus norvegicus. [Contig view]

GeneID

25703; -.

KEGG

rno:25703; -.

Phylogenomic databases

HOVERGEN

P04916; -.

Other

NextBio

607739; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Retinol-binding; Secreted; Signal; Transport; Vitamin A.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`
`CHAIN`	`19 201`	`183`	`Retinol-binding protein 4.`	`PRO_0000017970`
`DISULFID`	`22 178`		`By similarity.`
`DISULFID`	`88 192`		`By similarity.`
`DISULFID`	`138 147`		`By similarity.`

Sequence information

Length: 201 AA [This is the length of the unprocessed precursor]

Molecular weight: 23220 Da [This is the MW of the unprocessed precursor]

CRC64: E6737E293B37A30A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEWVWALVLL AALGGGSAER DCRVSSFRVK ENFDKARFSG LWYAIAKKDP EGLFLQDNII 

        70         80         90        100        110        120 
AEFSVDEKGH MSATAKGRVR LLSNWEVCAD MVGTFTDTED PAKFKMKYWG VASFLQRGND 

       130        140        150        160        170        180 
DHWIIDTDYD TFALQYSCRL QNLDGTCADS YSFVFSRDPN GLTPETRRLV RQRQEELCLE 

       190        200 
RQYRWIEHNG YCQSRPSRNS L

P04916 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools