Disease relevance of CRIP1

• The putative protein, named p135, contained a cysteine-rich zinc finger domain near the N terminus with homology to ICP0 of herpes simplex virus type 1, to protein 61 of varicella-zoster virus, to early protein 0 of pseudorabies virus, and to other viral and cellular proteins [1].
• The deduced amino acid sequence revealed the presence of cysteine-rich zinc finger domain similar to that of the immediate-early gene ICP0 of herpes simplex virus type 1 and the gene 61 polypeptide of varicella-zoster virus [2].
• Nondefective rotavirus mutants with an NSP1 gene which has a deletion of 500 nucleotides, including a cysteine-rich zinc finger motif-encoding region (nucleotides 156 to 248), or which has a nonsense codon at nucleotides 153-155 [3].
• The integrin alpha(v)beta(3) has been shown to function as one of the integrin receptors on cultured cells for foot-and-mouth disease virus (FMDV), and high-efficiency utilization of the bovine homolog of this integrin is dependent on the cysteine-rich repeat region of the bovine beta(3) subunit [4].

High impact information on CRIP1

• RNA blot analysis using DNA probes corresponding to the mucin-like and cysteine-rich regions detected a nearly identical pattern of transcripts, demonstrating that the characterized clones are not artifacts of cDNA library construction [5].
• In addition, cyanogen bromide cleavage of bIGFBP-2 revealed that the N- and C-terminal cysteine-rich domains were not linked by disulfide bonds [6].
• A new family of cysteine-rich antimicrobial peptides from bovine neutrophils was isolated and characterized [7].
• By analogy with other proteins containing these cysteine-rich repeats, it is possible that, in gall-bladder mucin, this domain serves as a binding site for hydrophobic ligands such as bilirubin, cholesterol and other biliary lipids [8].
• NADH:ubiquinone oxidoreductase from bovine mitochondria. cDNA sequence of a 19 kDa cysteine-rich subunit [9].

Biological context of CRIP1

• The sequence of the 23-kDa subunit is closely related to potential proteins, which also contain the cysteine-rich sequence motifs, encoded in the frxB ORFs in chloroplast genomes.(ABSTRACT TRUNCATED AT 250 WORDS)[10]
• The predicted amino acid sequences of this 54-kDa protein portion contain a conserved cysteine-rich stretch remarkably similar to a "zinc finger-type" binding domain found in many gene-regulatory proteins [11].
• The PCR analysis used targets in the MOMP gene, the 16S rRNA gene, and the 60-kDa cysteine-rich protein gene [12].
• The cysteine-rich protein 61 (Cyr61) is a signaling molecule with functions in cell migration, adhesion, and proliferation [13].
• The rotavirus nonstructural protein NS53 (NSVP1), the product of genome segment 5, possesses RNA-binding activity and contains a highly conserved cysteine-rich motif located in the amino-terminal half of the protein [14].

Anatomical context of CRIP1

• This study describes the isolation, primary structure, cDNA cloning, and tissue expression profile of two cysteine-rich AMPs from the hemolymph of the cattle tick Boophilus microplus [15].
• In this study, a novel cysteine-rich AMP has been isolated and characterized from the hemocytes of the cattle tick, Boophilus microplus [16].
• Experiments were carried out exposing immature bovine oocytes to 4 degrees C for 24 h in the presence of type I alanine rich alpha helical antifreeze polypeptides (AFP) from winter flounder, type II cysteine-rich AFP from sea raven or type III AFP from ocean pout [17].
• Isolation and native characterization of cysteine-rich collagens from bovine placental tissues and uterus and their relationship to types IV and V collagens [18].

Associations of CRIP1 with chemical compounds

• The mature protein contains eight cysteine residues spaced at regular intervals through the protein, but the cysteine-rich motifs that are often associated with tetranuclear or binuclear centres in other proteins are not present [9].
• Exon III encoded the signal peptide, a cysteine-rich NH2-terminal region and six repeats of a Gly-X-Y triplet with one irregular triplet [19].
• Ligand regulation of bovine protein kinase C alpha response via either cysteine-rich repeat of conserved region C1 [20].
• The extracellular domain of gE has two conserved cysteine-rich regions: C1 and C2 [21].

References