Retinol-binding protein 4 - Bos taurus (Bovine)

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P18902 (RET4_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 99. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Retinol-binding protein 4

Alternative name(s):
Plasma retinol-binding protein
Short name=PRBP
Short name=RBP

Gene names

Name:

RBP4

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	183 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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.
Sequence similarities	Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Secreted
Ligand	Retinol-binding Vitamin A
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cardiac muscle tissue development Inferred from electronic annotation. Source: Compara detection of light stimulus involved in visual perception Inferred from electronic annotation. Source: Compara embryonic organ morphogenesis Inferred from electronic annotation. Source: Compara embryonic retina morphogenesis in camera-type eye Inferred from electronic annotation. Source: Compara embryonic skeletal system development Inferred from electronic annotation. Source: Compara female genitalia morphogenesis Inferred from electronic annotation. Source: Compara gluconeogenesis Inferred from electronic annotation. Source: Compara glucose homeostasis Inferred from electronic annotation. Source: Compara heart trabecula formation Inferred from electronic annotation. Source: Compara lung development Inferred from electronic annotation. Source: Compara maintenance of gastrointestinal epithelium Inferred from electronic annotation. Source: Compara male gonad development Inferred from electronic annotation. Source: Compara negative regulation of cardiac muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of immunoglobulin secretion Inferred from electronic annotation. Source: Compara positive regulation of insulin secretion Inferred from electronic annotation. Source: Compara response to insulin stimulus Inferred from electronic annotation. Source: Compara response to retinoic acid Inferred from electronic annotation. Source: Compara retinal metabolic process Inferred from electronic annotation. Source: Compara retinol metabolic process Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: Compara urinary bladder development Inferred from electronic annotation. Source: Compara uterus development Inferred from electronic annotation. Source: Compara vagina development Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	retinal binding Inferred from electronic annotation. Source: UniProtKB-KW retinol binding Inferred from electronic annotation. Source: UniProtKB-KW retinol transporter activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 183

183

Retinol-binding protein 4

PRO_0000201028

Amino acid modifications

Disulfide bond

4 ↔ 160

By similarity

Disulfide bond

70 ↔ 174

By similarity

Disulfide bond

120 ↔ 129

By similarity

Secondary structure

183

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P18902 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: D6BA064CB9E67C09
Show »

FASTA

183

21,069

        10         20         30         40         50         60 
ERDCRVSSFR VKENFDKARF AGTWYAMAKK DPEGLFLQDN IVAEFSVDEN GHMSATAKGR 

        70         80         90        100        110        120 
VRLLNNWDVC ADMVGTFTDT EDPAKFKMKY WGVASFLQKG NDDHWIIDTD YETFAVQYSC 

       130        140        150        160        170        180 
RLLNLDGTCA DSYSFVFARD PSGFSPEVQK IVRQRQEELC LARQYRLIPH NGYCDGKSER 


NIL

« Hide

References

[1]	"The bovine plasma retinol-binding protein. Amino acid sequence, interaction with transthyretin, crystallization and preliminary X-ray data." Berni R., Stoppini M., Zapponi M.C., Meloni M.L., Monaco H.L., Zanotti G. Eur. J. Biochem. 192:507-513(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, CRYSTALLIZATION.
[2]	"Expression and cellular localization of retinol-binding protein messenger ribonucleic acid in bovine blastocysts and extraembryonic membranes." Liu K.H., Dore J.J. Jr., Roberts M.P., Krishnan R., Hopkins F.M., Godkin J.D. Biol. Reprod. 49:393-400(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-183.
[3]	"Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity." Monaco H.L., Zanotti G. Biopolymers 32:457-465(1992) [PubMed] [Europe PMC] [Abstract] Cited for: COMPARISON OF X-RAY STRUCTURES.
[4]	"Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding protein." Zanotti G., Berni R., Monaco H.L. J. Biol. Chem. 268:10728-10738(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S65585 mRNA. Translation: AAB28336.1.

IPI

IPI00697184.

PIR

I46955.
S13186.

UniGene

Bt.5318.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ERB	X-ray	1.90	A	1-183	[»]
1FEL	X-ray	1.80	A	1-183	[»]
1FEM	X-ray	1.90	A	1-183	[»]
1FEN	X-ray	1.90	A	1-183	[»]
1HBP	X-ray	1.90	A	1-183	[»]
1HBQ	X-ray	1.70	A	1-183	[»]
1KT3	X-ray	1.40	A	1-183	[»]
1KT4	X-ray	1.46	A	1-183	[»]
1KT5	X-ray	1.46	A	1-175	[»]
1KT6	X-ray	1.10	A	1-183	[»]
1KT7	X-ray	1.27	A	1-183	[»]

ProteinModelPortal

P18902.

SMR

P18902. Positions 1-176.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000000566.

Proteomic databases

PaxDb

P18902.

PRIDE

P18902.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

NOG40507.

HOVERGEN

HBG004493.

InParanoid

P18902.

OrthoDB

EOG4T4CWM.

Enzyme and pathway databases

BioCyc

CATTLE:281444-MONOMER.

Gene expression databases

ArrayExpress

P18902.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002449. Retinol-bd/Purpurin.
[Graphical view]

PANTHER

PTHR11873. PTHR11873. 1 hit.

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PIRSF

PIRSF036893. Lipocalin_ApoD. 1 hit.
PIRSF500204. RBP_purpurin. 1 hit.

PRINTS

PR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00213. LIPOCALIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P18902.

Entry information

Entry name

RET4_BOVIN

Accession

Primary (citable) accession number: P18902

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 29, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents