Recombinant Human PTPRD Fc Chimera Protein, CF Summary
Accession # P23468
Human protein-tyrosine phosphatase delta (PTPRD) is a type I membrane protein. It contains a 1245 amino acid (aa) long extracellular domain (ECD), a 25 amino acid long transmembrane domain, and a 622 amino acid cytoplasmic domain. A cleavage during post-translational modification separates the extracellular domain from the transmembrane segment through a process called "ectodomain shedding" (1). The extracellular regions are comprised of three Ig-like C2 domains followed immediately by eight fibronectin type-III like domains (1). The human PTPRD extracellular domain shares 98% and 62% aa identity with mouse and rat PTPRD, respectively. Protein-tyrosine phosphatases (PTPs) constitute a structurally diverse family of tightly regulated enzymes with important regulatory roles (1-6). PTPRD is a member of the PTPs and is detected in brain and other tissues including colon and breast (1). It has been demonstrated that phosphorylated STAT3 (p-STAT3) is a direct substrate of PTPRD and that cancer-specific mutations in PTPRD abrogate its ability to dephosphorylate STAT3 (5). PTPRD interacts with NGL-3 (Netrin-G ligand-3) via its first two FNIII repeats to promote synapse formation (3). PTPRD can also bind to IL1RAPL1 and its paralog IL1RAPL2; the IL1RAPL1/PTPRD complex recruits RhoGAP2 at excitatory synapses to induce dendritic spine formation (4). Recent studies have indicated SALM5 forms heterotetramer with PTPRD to induce synaptic differentiation (6).
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- Lin, Z. et al. (2018) Nat, Commun. 9:268.
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