Leucine Rich Repeat Containing Protein 32 (LRRC32)

GARP; Glycoprotein A Repetitions Predominant; Garpin

SPN	K049
HGNC	4161
MGI	93882
PubMed	22070912
RGD	1309087
UniProt	Q14392

A leucine-rich repeat (LRR) is a protein structural motif that forms an α/β horseshoe fold. It is composed of repeating 20-30 amino acid stretches that are unusually rich in the hydrophobic amino acid leucine. Typically, each repeat unit has beta strand-turn-alpha helix structure, and the assembled domain, composed of many such repeats, has a horseshoe shape with an interior parallel beta sheet and an exterior array of helices.

In an effort to isolate as many candidate oncogenes as possible from the region 11q13.5-q14, Ollendorff et al. (1992) isolated a sequence, containing a gene they provisionally named GARP. They cloned the homologous sequence in the mouse and located it on chromosome 7. The murine and human genes were mapped by in situ hybridization.

Reference

"The GARP gene encodes a new member of the family of leucine-rich repeat-containing proteins."
Cell Growth Differ. 5:213-219(1994) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]

"Signal peptide cleavage is essential for surface expression of a regulatory T cell surface protein, leucine rich repeat containing 32 (LRRC32)."
BMC Biochem. 12:27-27(2011) [PubMed] [Europe PMC] [Abstract]