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P18902

- RET4_BOVIN

UniProt

P18902 - RET4_BOVIN

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Protein

Retinol-binding protein 4

Gene

RBP4

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 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

  1. retinal binding Source: UniProtKB-KW
  2. retinol binding Source: UniProtKB-KW
  3. retinol transporter activity Source: Ensembl

GO - Biological processi

  1. cardiac muscle tissue development Source: Ensembl
  2. detection of light stimulus involved in visual perception Source: Ensembl
  3. embryonic organ morphogenesis Source: Ensembl
  4. embryonic retina morphogenesis in camera-type eye Source: Ensembl
  5. embryonic skeletal system development Source: Ensembl
  6. female genitalia morphogenesis Source: Ensembl
  7. gluconeogenesis Source: Ensembl
  8. glucose homeostasis Source: Ensembl
  9. heart trabecula formation Source: Ensembl
  10. lung development Source: Ensembl
  11. maintenance of gastrointestinal epithelium Source: Ensembl
  12. male gonad development Source: Ensembl
  13. negative regulation of cardiac muscle cell proliferation Source: Ensembl
  14. positive regulation of immunoglobulin secretion Source: Ensembl
  15. positive regulation of insulin secretion Source: Ensembl
  16. response to insulin Source: Ensembl
  17. response to retinoic acid Source: Ensembl
  18. retinal metabolic process Source: Ensembl
  19. retinol metabolic process Source: Ensembl
  20. spermatogenesis Source: Ensembl
  21. urinary bladder development Source: Ensembl
  22. uterus development Source: Ensembl
  23. vagina development Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

ReactomeiREACT_204227. Retinoid metabolism and transport.
REACT_211834. The canonical retinoid cycle in rods (twilight vision).
REACT_218434. Retinoid cycle disease events.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 183183Retinol-binding protein 4PRO_0000201028Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 160By similarity
Disulfide bondi70 ↔ 174By similarity
Disulfide bondi120 ↔ 129By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP18902.
PRIDEiP18902.

Expressioni

Gene expression databases

ExpressionAtlasiP18902. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000566.

Structurei

Secondary structure

1
183
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83
Helixi17 – 204
Beta strandi22 – 309
Beta strandi33 – 353
Beta strandi39 – 479
Beta strandi53 – 6210
Beta strandi68 – 7912
Beta strandi85 – 9410
Beta strandi100 – 10910
Beta strandi111 – 12313
Beta strandi127 – 14216
Helixi146 – 15813
Turni173 – 1753

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP18902.
SMRiP18902. Positions 1-176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18902.

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Phylogenomic databases

eggNOGiNOG40507.
HOVERGENiHBG004493.
InParanoidiP18902.

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.

P18902-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
ERDCRVSSFR VKENFDKARF AGTWYAMAKK DPEGLFLQDN IVAEFSVDEN
60 70 80 90 100
GHMSATAKGR VRLLNNWDVC ADMVGTFTDT EDPAKFKMKY WGVASFLQKG
110 120 130 140 150
NDDHWIIDTD YETFAVQYSC RLLNLDGTCA DSYSFVFARD PSGFSPEVQK
160 170 180
IVRQRQEELC LARQYRLIPH NGYCDGKSER NIL
Length:183
Mass (Da):21,069
Last modified:November 1, 1990 - v1
Checksum:iD6BA064CB9E67C09
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S65585 mRNA. Translation: AAB28336.1.
PIRiI46955.
S13186.
UniGeneiBt.5318.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S65585 mRNA. Translation: AAB28336.1 .
PIRi I46955.
S13186.
UniGenei Bt.5318.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P18902.
SMRi P18902. Positions 1-176.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000000566.

Proteomic databases

PaxDbi P18902.
PRIDEi P18902.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG40507.
HOVERGENi HBG004493.
InParanoidi P18902.

Enzyme and pathway databases

Reactomei REACT_204227. Retinoid metabolism and transport.
REACT_211834. The canonical retinoid cycle in rods (twilight vision).
REACT_218434. Retinoid cycle disease events.

Miscellaneous databases

EvolutionaryTracei P18902.

Gene expression databases

ExpressionAtlasi P18902. baseline and differential.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi 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 ]
PANTHERi PTHR11873. PTHR11873. 1 hit.
Pfami PF00061. Lipocalin. 1 hit.
[Graphical view ]
PIRSFi PIRSF036893. Lipocalin_ApoD. 1 hit.
PIRSF500204. RBP_purpurin. 1 hit.
PRINTSi PR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.
SUPFAMi SSF50814. SSF50814. 1 hit.
PROSITEi PS00213. LIPOCALIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiRET4_BOVIN
AccessioniPrimary (citable) accession number: P18902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: October 29, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3