his gene encodes a member of a small family of proteins which bind single stranded DNA/RNA. These proteins are characterized by the presence of two sets of ribonucleoprotein consensus sequence (RNP-CS) that contain conserved motifs, RNP1 and RNP2, originally described in RNA binding proteins, and required for DNA binding. These proteins have been implicated in such diverse functions as DNA replication, gene transcription, cell cycle progression and apoptosis. Several transcript variants, resulting from alternative splicing and encoding different isoforms, have been described. A pseudogene for this locus is found on chromosome 12.
A synthesized peptide derived from human RBMS3, corresponding to a region within the internal amino acids.
This gene encodes an RNA-binding protein that belongs to the c-myc gene single-strand binding protein family. These proteins are characterized by the presence of two sets of ribonucleoprotein consensus sequence (RNP-CS) that contain conserved motifs, RNP1 and RNP2, originally described in RNA binding proteins, and required for DNA binding. These proteins have been implicated in such diverse functions as DNA replication, gene transcription, cell cycle progression and apoptosis. The encoded protein was isolated by virtue of its binding to an upstream element of the alpha2(I) collagen promoter. The observation that this protein localizes mostly in the cytoplasm suggests that it may be involved in a cytoplasmic function such as controlling RNA metabolism, rather than transcription. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
A synthesized peptide derived from Human RBP1.
A synthesized peptide derived from human RBP3.
Interphotoreceptor retinol-binding protein is a large glycoprotein known to bind retinoids and found primarily in the interphotoreceptor matrix of the retina between the retinal pigment epithelium and the photoreceptor cells. It is thought to transport retinoids between the retinal pigment epithelium and the photoreceptors, a critical role in the visual process.The human IRBP gene is approximately 9.5 kbp in length and consists of four exons separated by three introns. The introns are 1.6-1.9 kbp long. The gene is transcribed by photoreceptor and retinoblastoma cells into an approximately 4.3-kilobase mRNA that is translated and processed into a glycosylated protein of 135,000 Da. The amino acid sequence of human IRBP can be divided into four contiguous homology domains with 33-38% identity, suggesting a series of gene duplication events. In the gene, the boundaries of these domains are not defined by exon-intron junctions, as might have been expected. The first three homology domains and part of the fourth are all encoded by the first large exon, which is 3,180 base pairs long. The remainder of the fourth domain is encoded in the last three exons, which are 191, 143, and approximately 740 base pairs long, respectively.
A synthesized peptide derived from human RBP4, corresponding to a region within the internal amino acids.
Retinol (also known as vitamin A) is unstable and insoluble in the aqueous solution. However, retinol becomes quite stable and soluble in plasma due to its tight interaction with retinol-binding protein 4 (RBP4), also known as plasma retinol-binding protein. A prototypic member of the lipocalin superfamily, RBP4 has a beta -barrel structure with a well-defined cavity. It is secreted from the liver, a process requiring the availability of retinol. RBP4 delivers retinol from the liver to the peripheral tissues. In plasma, the RBP4-retinol complex interacts with transthyretin (TTR), also known as thyroxine-binding protein and prealbumin. The retinol-RBP4-TTR complex prevents the loss of RBP4 by filtration through the kidney and increases the stability of the retinol-RBP4 complex. Defects in RBP4 cause retinol-binding protein deficiency, which affects night vision.
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