The SRCR superfamily: a family reminiscent of the Ig superfamily

Resnick, David; Pearson, Adam J.; Krieger, Monty

doi:10.1016/0968-0004(94)90165-1

Cited by 335 publications

(249 citation statements)

References 19 publications

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“…Each extracellular SRCR domain of the chicken CD5 is encoded as a single exon as in humans and mouse. This is also typical for the other members [3,12] of the group B SRCR family. In all species studied, the highly conserved region in the cytoplasm that lies close to the membrane is a single exon but the fully conserved region near the C terminus spans exons 9 and 10.…”

Section: Discussionsupporting

confidence: 54%

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Structure and Chromosomal Localization of Chicken CD5

Koskinen¹,

Salomonsen

Goodchild

et al. 2001

Scand J Immunol

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CD5 is a transmembrane glycoprotein on all T cells and on a subpopulation of B cells. Based on the analysis of chicken CD5-cDNA we have previously shown that the structure of the CD5 protein is conserved between species. Here we report the isolation and chromosomal mapping of the chicken CD5 gene. The gene spans 3.4 kb and is extremely compact with a high GC-nucleotide content. There are 10 exons and the introns are spliced out similarly to those in the human CD5 gene. Each of the three extracellular scavenger receptor cysteine-rich (SRCR) domains is encoded as an exon of its own, as is the proline-rich hinge region that separates the first two membrane-distal SRCR domains. The fluorescence in situ hybridization (FISH) technique was used to map the gene to chromosome five. This is the first report describing the organization of the CD5 gene from a nonmammalian species.

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Section: Discussionsupporting

confidence: 54%

“…In human and mouse only a subpopulation of B cells (B-1a) carries CD5 [2]. The protein is composed of three extracellular SRCR domains, a transmembrane region and a long cytoplasmic part [3] that contains several possible sites for phosphorylation implying a role for CD5 in the signal transduction.…”

Section: Introductionmentioning

confidence: 99%

Structure and Chromosomal Localization of Chicken CD5

Koskinen¹,

Salomonsen

Goodchild

et al. 2001

Scand J Immunol

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“…Amino acid sequence alignment revealed that WS9-14 contains four repeats of the scavenger receptor cysteine-rich (SRCR) domains (19) at amino acids 58 -158, 190 -301, 326 -424, and 435-543 (Fig. 1B).…”

Section: Resultsmentioning

confidence: 99%

Regulation of a Novel Gene Encoding a Lysyl Oxidase-related Protein in Cellular Adhesion and Senescence

Saitō

Papaconstantinou

Sato

et al. 1997

Journal of Biological Chemistry

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We report here a novel cDNA clone with a predicted protein sequence similar to lysyl oxidase. This fulllength cDNA clone of 3432 base pairs (WS9-14) was isolated from human fibroblasts on the basis of its overexpression in senescent cells. It encodes an 87-kDa polypeptide, whose protein is a member of the scavenger receptor cysteine-rich family, because it contains four scavenger receptor cysteine-rich domains that are found in several secreted or cell surface proteins. The WS9-14 protein has a 48% identity with both lysyl oxidase and lysyl oxidase-like protein at a region corresponding to exons 2-6, implying the existence of a lysyl oxidase gene family. The pattern of WS9-14 gene expression by fibroblasts parallels pro-collagen I-␣1 expression. Its mRNA level is induced by transforming growth factor ␤-1 and indomethacin and inhibited by phorbol ester and retinoic acid. WS9-14 is abundantly expressed in all tumor cell lines examined that attach to culture dishes but not in cell lines that grow in suspension and is also up-regulated in senescent fibroblasts. These results suggest that WS9-14 gene encodes an extracellular protein that may be specifically involved in cell adhesion and senescence.

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“…The LDLRA domain, which contains six disulfidebound cysteines (C72, C79, C85, C92, C98 and C107), was originally found in the low density lipoprotein receptor as the binding site for low-density lipoprotein and calcium 13 , and has subsequently been described in numerous extracellular and membrane proteins. SRCR domains linked to serine protease domains have been reported in secreted or membrane-bound molecules with diverse biological roles in development and immunity 14 . The LDLRA and SRCR domains of TMPRSS3 may be involved in binding with extracellular molecules or the cell surface.…”

Section: Division Of Medical Genetics University Of Geneva Medicalmentioning

confidence: 99%

Insertion of β-satellite repeats identifies a transmembrane protease causing both congenital and childhood onset autosomal recessive deafness

et al. 2001

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Approximately 50% of childhood deafness is caused by mutations in specific genes. Autosomal recessive loci account for approximately 80% of nonsyndromic genetic deafness 1 . Here we report the identification of a new transmembrane serine protease (TMPRSS3; also known as ECHOS1) expressed in many tissues, including fetal cochlea, which is mutated in the families used to describe both the DFNB10 and DFNB8 loci. An 8-bp deletion and insertion of 18 monomeric (∼68-bp) β-satellite repeat units, normally present in tandem arrays of up to several hundred kilobases on the short arms of acrocentric chromosomes, causes congenital deafness (DFNB10). A mutation in a spliceacceptor site, resulting in a 4-bp insertion in the mRNA and a frameshift, was detected in childhood onset deafness (DFNB8). This is the first description of β-satellite insertion into an active gene resulting in a pathogenic state, and the first description of a protease involved in hearing loss.

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The SRCR superfamily: a family reminiscent of the Ig superfamily

Cited by 335 publications

References 19 publications

Structure and Chromosomal Localization of Chicken CD5

Structure and Chromosomal Localization of Chicken CD5

Regulation of a Novel Gene Encoding a Lysyl Oxidase-related Protein in Cellular Adhesion and Senescence

Insertion of β-satellite repeats identifies a transmembrane protease causing both congenital and childhood onset autosomal recessive deafness

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