Probable transcription factor likely to be involved in early steps in the differentiation of amacrine and ganglion cells. Recognizes and binds to the DNA sequence 5'-ATGCAAAT-3'.
Interacting selectively and non-covalently with DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription. The transcription factor may or may not also interact selectively with a protein or macromolecular complex.
A novel POU-domain protein, retina-derived POU-domain factor-1 (RPF-1), has been identified through the isolation of cDNA and genomic DNA clones. In the adult, RPF-1 is expressed only within the CNS, where its expression is restricted to the medical habenulla, to a dispersed population of neurons in the dorsal hypothalamus, and to subsets of ganglion and amacrine cells in the retina. The human RPF-1 gene spans > 125 kb and gives rise to multiple differentially spliced transcripts. In the human retina, the most abundant mRNA isoforms are derived from an alternate splicing event that inserts an evolutionarily conserved peptide of 36 amino acids into the DNA recognition helix of the POU-specific domain. In vitro, the RPF-1 POU domain lacking the insert binds to a consensus Oct-1 binding site, whereas the alternately spliced POU domain does not. RPF-1 protein first appears in the developing mouse retina at e11, where it localizes to neuroblasts that have recently migrated from the mitotic zone to the future ganglion cell layer. These data suggest that RPF-1 is likely to be involved in early steps in the differentiation of amacrine and ganglion cells.
The process whose specific outcome is the progression of the central nervous system over time, from its formation to the mature structure. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain, spinal cord and spinal nerves. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
A novel POU-domain protein, retina-derived POU-domain factor-1 (RPF-1), has been identified through the isolation of cDNA and genomic DNA clones. In the adult, RPF-1 is expressed only within the CNS, where its expression is restricted to the medical habenulla, to a dispersed population of neurons in the dorsal hypothalamus, and to subsets of ganglion and amacrine cells in the retina. The human RPF-1 gene spans > 125 kb and gives rise to multiple differentially spliced transcripts. In the human retina, the most abundant mRNA isoforms are derived from an alternate splicing event that inserts an evolutionarily conserved peptide of 36 amino acids into the DNA recognition helix of the POU-specific domain. In vitro, the RPF-1 POU domain lacking the insert binds to a consensus Oct-1 binding site, whereas the alternately spliced POU domain does not. RPF-1 protein first appears in the developing mouse retina at e11, where it localizes to neuroblasts that have recently migrated from the mitotic zone to the future ganglion cell layer. These data suggest that RPF-1 is likely to be involved in early steps in the differentiation of amacrine and ganglion cells.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a ganglion mother cell regardless of its environment; upon determination, the cell fate cannot be reversed.
A novel POU-domain protein, retina-derived POU-domain factor-1 (RPF-1), has been identified through the isolation of cDNA and genomic DNA clones. In the adult, RPF-1 is expressed only within the CNS, where its expression is restricted to the medical habenulla, to a dispersed population of neurons in the dorsal hypothalamus, and to subsets of ganglion and amacrine cells in the retina. The human RPF-1 gene spans > 125 kb and gives rise to multiple differentially spliced transcripts. In the human retina, the most abundant mRNA isoforms are derived from an alternate splicing event that inserts an evolutionarily conserved peptide of 36 amino acids into the DNA recognition helix of the POU-specific domain. In vitro, the RPF-1 POU domain lacking the insert binds to a consensus Oct-1 binding site, whereas the alternately spliced POU domain does not. RPF-1 protein first appears in the developing mouse retina at e11, where it localizes to neuroblasts that have recently migrated from the mitotic zone to the future ganglion cell layer. These data suggest that RPF-1 is likely to be involved in early steps in the differentiation of amacrine and ganglion cells.
A novel POU-domain protein, retina-derived POU-domain factor-1 (RPF-1), has been identified through the isolation of cDNA and genomic DNA clones. In the adult, RPF-1 is expressed only within the CNS, where its expression is restricted to the medical habenulla, to a dispersed population of neurons in the dorsal hypothalamus, and to subsets of ganglion and amacrine cells in the retina. The human RPF-1 gene spans > 125 kb and gives rise to multiple differentially spliced transcripts. In the human retina, the most abundant mRNA isoforms are derived from an alternate splicing event that inserts an evolutionarily conserved peptide of 36 amino acids into the DNA recognition helix of the POU-specific domain. In vitro, the RPF-1 POU domain lacking the insert binds to a consensus Oct-1 binding site, whereas the alternately spliced POU domain does not. RPF-1 protein first appears in the developing mouse retina at e11, where it localizes to neuroblasts that have recently migrated from the mitotic zone to the future ganglion cell layer. These data suggest that RPF-1 is likely to be involved in early steps in the differentiation of amacrine and ganglion cells.
The synthesis of RNA from a DNA template by RNA polymerase II, originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs).
A novel POU-domain protein, retina-derived POU-domain factor-1 (RPF-1), has been identified through the isolation of cDNA and genomic DNA clones. In the adult, RPF-1 is expressed only within the CNS, where its expression is restricted to the medical habenulla, to a dispersed population of neurons in the dorsal hypothalamus, and to subsets of ganglion and amacrine cells in the retina. The human RPF-1 gene spans > 125 kb and gives rise to multiple differentially spliced transcripts. In the human retina, the most abundant mRNA isoforms are derived from an alternate splicing event that inserts an evolutionarily conserved peptide of 36 amino acids into the DNA recognition helix of the POU-specific domain. In vitro, the RPF-1 POU domain lacking the insert binds to a consensus Oct-1 binding site, whereas the alternately spliced POU domain does not. RPF-1 protein first appears in the developing mouse retina at e11, where it localizes to neuroblasts that have recently migrated from the mitotic zone to the future ganglion cell layer. These data suggest that RPF-1 is likely to be involved in early steps in the differentiation of amacrine and ganglion cells.
The series of events required for an organism to receive a visual stimulus, convert it to a molecular signal, and recognize and characterize the signal. Visual stimuli are detected in the form of photons and are processed to form an image.
A novel POU-domain protein, retina-derived POU-domain factor-1 (RPF-1), has been identified through the isolation of cDNA and genomic DNA clones. In the adult, RPF-1 is expressed only within the CNS, where its expression is restricted to the medical habenulla, to a dispersed population of neurons in the dorsal hypothalamus, and to subsets of ganglion and amacrine cells in the retina. The human RPF-1 gene spans > 125 kb and gives rise to multiple differentially spliced transcripts. In the human retina, the most abundant mRNA isoforms are derived from an alternate splicing event that inserts an evolutionarily conserved peptide of 36 amino acids into the DNA recognition helix of the POU-specific domain. In vitro, the RPF-1 POU domain lacking the insert binds to a consensus Oct-1 binding site, whereas the alternately spliced POU domain does not. RPF-1 protein first appears in the developing mouse retina at e11, where it localizes to neuroblasts that have recently migrated from the mitotic zone to the future ganglion cell layer. These data suggest that RPF-1 is likely to be involved in early steps in the differentiation of amacrine and ganglion cells.
Protein involved in the transfer of genetic information from DNA to messenger RNA (mRNA) by DNA-directed RNA polymerase. In the case of some RNA viruses, protein involved in the transfer of genetic information from RNA to messenger RNA (mRNA) by RNA-directed RNA polymerase.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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