[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1723146 [NCBI, ExPASy, EBI, Israel, Japan] Trout W.E., McDonnell J.J., Kramer K.K., Baumbach G.A., Roberts R.M.; "The retinol-binding protein of the expanding pig blastocyst: molecular cloning and expression in trophectoderm and embryonic disc."; Mol. Endocrinol. 5:1533-1540(1991).
[2]	PROTEIN SEQUENCE OF 19-51, AND DEVELOPMENTAL STAGE. PubMed=2340335 [NCBI, ExPASy, EBI, Israel, Japan] Harney J.P., Mirando M.A., Smith L.C., Bazer F.W.; "Retinol-binding protein: a major secretory product of the pig conceptus."; Biol. Reprod. 42:523-532(1990).
[3]	X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND SEQUENCE REVISION TO 134 AND 185. DOI=10.1107/S0907444998002303; PubMed=9757135 [NCBI, ExPASy, EBI, Israel, Japan] Zanotti G., Panzalorto M., Marcato A., Malpeli G., Folli C., Berni R.; "Structure of pig plasma retinol-binding protein at 1.65-A resolution."; Acta Crystallogr. D 54:1049-1052(1998).

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.
DEVELOPMENTAL STAGE: Produced between days 10 and 15 of pregnancy and at day 15 found in both the peri-implantation conceptus (trophectoderm and yolk sac) and the endometrial surface and glandular epithelium. Found in allantoic fluid at day 30 of gestation.
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

M68860; AAA31113.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A39486; A39486.

NP_999222.1; -.

3D structure databases

PDB

1AQB; X-ray; 1.65 A; A=19-201.

[ExPASy / RCSB / EBI]

PDBsum

1AQB; -.

ModBase

P27485.

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).
GO:0005215;	Molecular function: transporter activity (inferred from electronic annotation from InterPro).
GO:0006810;	Biological process: transport (inferred from electronic annotation from InterPro).
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

GeneID

397124; -.

KEGG

ssc:397124; -.

Phylogenomic databases

HOVERGEN

P27485; -.

Other

P27485; -.

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

Keywords

3D-structure; 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_0000017968`
`DISULFID`	`22 178`
`DISULFID`	`88 192`
`DISULFID`	`138 147`
`CONFLICT`	`134 134`		`V -> A (in Ref. 1; AAA31113).`
`CONFLICT`	`185 185`		`I -> L (in Ref. 1; AAA31113).`
`HELIX`	`24 26`	`3`
`HELIX`	`35 38`	`4`
`STRAND`	`40 48`	`9`
`STRAND`	`51 53`	`3`
`STRAND`	`55 65`	`11`
`STRAND`	`71 80`	`10`
`STRAND`	`86 97`	`12`
`STRAND`	`103 112`	`10`
`STRAND`	`118 127`	`10`
`STRAND`	`129 141`	`13`
`STRAND`	`145 158`	`14`
`HELIX`	`164 176`	`13`

Sequence information

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

Molecular weight: 23067 Da [This is the MW of the unprocessed precursor]

CRC64: A20E39D3C9471DC8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEWVWALVLL AALGSAQAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP EGLFLQDNIV 

        70         80         90        100        110        120 
AEFSVDENGH MSATAKGRVR LLNNWDVCAD MVGTFTDTED PAKFKMKYWG VASFLQKGND 

       130        140        150        160        170        180 
DHWIIDTDYD TYAVQYSCRL QNLDGTCADS YSFVFARDPH GFSPEVQKIV RQRQEELCLA 

       190        200 
RQYRIITHNG YCDGKSERNI L

P27485 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