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Peptidoglycan recognition protein LCy
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[SH2 domain-containing phosphatase anchor protein-1] In the nomenclature of CD antigens the protein has been given the designation CD307b. Sequence analysis shows that the protein is identical with FCRL2 [Fc receptor-like-2].
The cDNA encoding this glycoprotein has been cloned by Xu et al (2001) after an EST database search for proteins containing an ITIM motif. The presence of this sequence motif suggests that SPAP1 is an inhibitory receptor.
SPAP1 has been shown to exist in various isoforms: SPAP1A (SH2 domain-containing phosphatase anchor protein-1A) is a transmembrane protein of 255 amino acids that contains 2 ITIM motifs. SPAP1B (SH2 domain-containing phosphatase anchor protein-1B) is a splice variant of 192 amino acids that lacks the intracellular ITIM motifs. SPAP1C (SH2 domain-containing phosphatase anchor protein-1C) is a splice variant of 144 amino acids that lacks the transmembrane segment and, therefore, may be a soluble protein.
SPAP1A is expressed in spleen, peripheral blood, bone marrow, and B-cell lines, but not in other tissues. SPAP1C has been detected in Jurkat and B-cell lines. Expression of SPAP1B has not been detected in any samples tested. The ITIM motif of SPAP1A has been shown to recruit the SH2 domain containing tyrosine phosphatase SHP1, a major negative regulator of hematopoietic cell signaling. By functioning as an anchor protein for this phosphatase SPAP1 may play a role in hematopoietic cell signaling.
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