Retinol binding protein 1, cellular, also known as RBP1, is a protein that in humans is encoded by the RBP1gene.[5][6][7]
Function
RBP1 is the carrier protein involved in the transport of retinol (vitamin A alcohol) from the liver storage site to peripheral tissue. Vitamin A is a fat-soluble vitamin necessary for growth, reproduction, differentiation of epithelial tissues, and vision. The gene harbors four exons encoding 24, 59, 33, and 16 amino acid residues, respectively. The second intervening sequence alone occupies 19 kb of the 21 kb of the gene.[5]
Clinical significance
Cellular retinol-binding protein-1 (CRBP-1) contributes to the maintenance of the differentiative state of endometrial cells through the regulation of bioavailability of retinol. On the converse, loss of CRBP-1 is associated with development of endometrial cancer.[8]
^De Baere E, Speleman F, Van Roy N, De Paepe A, Messiaen L (1998). "Assignment of the cellular retinol-binding protein 1 gene (RBP1) and of the coatomer beta subunit gene (COPB2) to human chromosome band 3q23 by in situ hybridization". Cytogenet. Cell Genet. 82 (3–4): 226–7. doi:10.1159/000015107. PMID9858824.
^Orlandi A, Ferlosio A, Ciucci A, Francesconi A, Lifschitz-Mercer B, Gabbiani G, Spagnoli LG, Czernobilsky B (June 2006). "Cellular retinol binding protein-1 expression in endometrial hyperplasia and carcinoma: diagnostic and possible therapeutic implications". Mod. Pathol. 19 (6): 797–803. doi:10.1038/modpathol.3800586. PMID16575402.
1crb: CRYSTALLOGRAPHIC STUDIES ON A FAMILY OF CELLULAR LIPOPHILIC TRANSPORT PROTEINS. REFINEMENT OF P2 MYELIN PROTEIN AND THE STRUCTURE DETERMINATION AND REFINEMENT OF CELLULAR RETINOL-BINDING PROTEIN IN COMPLEX WITH ALL-TRANS-RETINOL
1jbh: Solution structure of cellular retinol binding protein type-I in the ligand-free state
1kgl: Solution structure of cellular retinol binding protein type-I in complex with all-trans-retinol
1mx7: Two homologous rat cellular retinol-binding proteins differ in local structure and flexibility
1mx8: Two homologous rat cellular retinol-binding proteins differ in local structure and flexibility