Catalysis of the hydrolysis of nonterminal peptide bonds in a polypeptide chain by a mechanism using a cysteine residue at the enzyme active center, and requiring the presence of calcium.
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
Mutations in the Drosophila melanogaster small optic lobes (sol) gene cause a sever reduction in the neuropiles of the medulla and lobula complexes of the adult optic lobes. The predicted protein product of sol contains zinc-finger-like repeats, a calpain-like protease domain, and a C-terminal region of unknown function. We have isolated human brain cDNA for SOLH, a human homologue of sol. The human SOLH gene consists of 14 exons distributed over more than 45 kb of genomic DNA. The encoded SOLH protein of 1086 amino acids has strong similarity to the D. melanogaster protein. The calpain-like domain and C-terminal region are highly conserved (58% identity), and similar Cys2-Cys2 zinc fingers are present in the N-terminal region. A reported Caenorhabditis elegans homologue contains the calpain domain and C-terminal region, but appears to lack the zinc finger region. A single copy of the zinc finger sequence is present in adjacent C. elegans genomic cosmid DNA sequence, and we show that it is part of the C. elegans sol-like transcript. Northern analysis of human tissues revealed a SOLH transcript of approximately 5 kb that was strongest in human brain. We have mapped the SOLH gene to chromosome 16p13.3 by in situ hybridization. SOLH is a candidate gene for CATM (hereditary cataracts with microphthalmia), which maps in this region.
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
Mutations in the Drosophila melanogaster small optic lobes (sol) gene cause a sever reduction in the neuropiles of the medulla and lobula complexes of the adult optic lobes. The predicted protein product of sol contains zinc-finger-like repeats, a calpain-like protease domain, and a C-terminal region of unknown function. We have isolated human brain cDNA for SOLH, a human homologue of sol. The human SOLH gene consists of 14 exons distributed over more than 45 kb of genomic DNA. The encoded SOLH protein of 1086 amino acids has strong similarity to the D. melanogaster protein. The calpain-like domain and C-terminal region are highly conserved (58% identity), and similar Cys2-Cys2 zinc fingers are present in the N-terminal region. A reported Caenorhabditis elegans homologue contains the calpain domain and C-terminal region, but appears to lack the zinc finger region. A single copy of the zinc finger sequence is present in adjacent C. elegans genomic cosmid DNA sequence, and we show that it is part of the C. elegans sol-like transcript. Northern analysis of human tissues revealed a SOLH transcript of approximately 5 kb that was strongest in human brain. We have mapped the SOLH gene to chromosome 16p13.3 by in situ hybridization. SOLH is a candidate gene for CATM (hereditary cataracts with microphthalmia), which maps in this region.
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.
Mutations in the Drosophila melanogaster small optic lobes (sol) gene cause a sever reduction in the neuropiles of the medulla and lobula complexes of the adult optic lobes. The predicted protein product of sol contains zinc-finger-like repeats, a calpain-like protease domain, and a C-terminal region of unknown function. We have isolated human brain cDNA for SOLH, a human homologue of sol. The human SOLH gene consists of 14 exons distributed over more than 45 kb of genomic DNA. The encoded SOLH protein of 1086 amino acids has strong similarity to the D. melanogaster protein. The calpain-like domain and C-terminal region are highly conserved (58% identity), and similar Cys2-Cys2 zinc fingers are present in the N-terminal region. A reported Caenorhabditis elegans homologue contains the calpain domain and C-terminal region, but appears to lack the zinc finger region. A single copy of the zinc finger sequence is present in adjacent C. elegans genomic cosmid DNA sequence, and we show that it is part of the C. elegans sol-like transcript. Northern analysis of human tissues revealed a SOLH transcript of approximately 5 kb that was strongest in human brain. We have mapped the SOLH gene to chromosome 16p13.3 by in situ hybridization. SOLH is a candidate gene for CATM (hereditary cataracts with microphthalmia), which maps in this region.
Mutations in the Drosophila melanogaster small optic lobes (sol) gene cause a sever reduction in the neuropiles of the medulla and lobula complexes of the adult optic lobes. The predicted protein product of sol contains zinc-finger-like repeats, a calpain-like protease domain, and a C-terminal region of unknown function. We have isolated human brain cDNA for SOLH, a human homologue of sol. The human SOLH gene consists of 14 exons distributed over more than 45 kb of genomic DNA. The encoded SOLH protein of 1086 amino acids has strong similarity to the D. melanogaster protein. The calpain-like domain and C-terminal region are highly conserved (58% identity), and similar Cys2-Cys2 zinc fingers are present in the N-terminal region. A reported Caenorhabditis elegans homologue contains the calpain domain and C-terminal region, but appears to lack the zinc finger region. A single copy of the zinc finger sequence is present in adjacent C. elegans genomic cosmid DNA sequence, and we show that it is part of the C. elegans sol-like transcript. Northern analysis of human tissues revealed a SOLH transcript of approximately 5 kb that was strongest in human brain. We have mapped the SOLH gene to chromosome 16p13.3 by in situ hybridization. SOLH is a candidate gene for CATM (hereditary cataracts with microphthalmia), which maps in this region.
Enzyme which catalyzes hydrolysis reaction, i.e. the addition of the hydrogen and hydroxyl ions of water to a molecule with its consequent splitting into two or more simpler molecules.
Proteolytic enzyme with a cysteine residue (Cys) in its active site. There are many families of thiol proteases. The most well known one is the papain family (C1 in MEROPS classification) which is known to exist in most eukaryotes.
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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