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P18902 (RET4_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinol-binding protein 4
Alternative name(s):
Plasma retinol-binding protein
Short name=PRBP
Short name=RBP
Gene names
Name:RBP4
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length183 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processTransport
   Cellular componentSecreted
   LigandRetinol-binding
Vitamin A
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle tissue development

Inferred from electronic annotation. Source: Ensembl

detection of light stimulus involved in visual perception

Inferred from electronic annotation. Source: Ensembl

embryonic organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic retina morphogenesis in camera-type eye

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal system development

Inferred from electronic annotation. Source: Ensembl

female genitalia morphogenesis

Inferred from electronic annotation. Source: Ensembl

gluconeogenesis

Inferred from electronic annotation. Source: Ensembl

glucose homeostasis

Inferred from electronic annotation. Source: Ensembl

heart trabecula formation

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

maintenance of gastrointestinal epithelium

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of immunoglobulin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

retinal metabolic process

Inferred from electronic annotation. Source: Ensembl

retinol metabolic process

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

urinary bladder development

Inferred from electronic annotation. Source: Ensembl

uterus development

Inferred from electronic annotation. Source: Ensembl

vagina development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionretinal 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: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 183183Retinol-binding protein 4
PRO_0000201028

Amino acid modifications

Disulfide bond4 ↔ 160 By similarity
Disulfide bond70 ↔ 174 By similarity
Disulfide bond120 ↔ 129 By similarity

Secondary structure

........................... 183
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18902 [UniParc].

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

FASTA18321,069
        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.
PIRI46955.
S13186.
UniGeneBt.5318.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ERBX-ray1.90A1-183[»]
1FELX-ray1.80A1-183[»]
1FEMX-ray1.90A1-183[»]
1FENX-ray1.90A1-183[»]
1HBPX-ray1.90A1-183[»]
1HBQX-ray1.70A1-183[»]
1KT3X-ray1.40A1-183[»]
1KT4X-ray1.46A1-183[»]
1KT5X-ray1.46A1-175[»]
1KT6X-ray1.10A1-183[»]
1KT7X-ray1.27A1-183[»]
ProteinModelPortalP18902.
SMRP18902. Positions 1-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000000566.

Proteomic databases

PaxDbP18902.
PRIDEP18902.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG40507.
HOVERGENHBG004493.
InParanoidP18902.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002449. Retinol-bd/Purpurin.
[Graphical view]
PANTHERPTHR11873. PTHR11873. 1 hit.
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFPIRSF036893. Lipocalin_ApoD. 1 hit.
PIRSF500204. RBP_purpurin. 1 hit.
PRINTSPR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP18902.

Entry information

Entry nameRET4_BOVIN
AccessionPrimary (citable) accession number: P18902
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references