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Description

Neuropilin-1 (UniProt: O14786, also known as Vascular endothelial cell growth factor 165 receptor, CD304) is encoded by the NRP1 (also known as NRP, VEGF165R) gene (Gene ID: 8829) in human. Three isoforms of Neuropilin-1 have been reported that are produced by alternative splicing. Isoform 1 of Neuropilin-1 is a homodimer, single-pass type I membrane protein with three calcium-binding sites (aa 195, 209, and 250). It can also form heterodimers with neuropilin-2. This membrane-bound isoform serves as a receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, The PLGF-2 isoform of PGF, The VEGF165 isoform of VEGFA and VEGFB. Its co-expression with VEGFR-2 (KDR) results in increased VEGF165 binding to VEGFR-2 as well as increased chemotaxis. It has an extracellular domain (aa 22-856), a helical domain (aa 857-879), and the cytoplasmic domain (aa 880-923). It is produced with a signal peptide (aa 1-21) that is subsequently cleaved to generate the mature form. The soluble isoform 2 binds VEGF-165 and appears to inhibit its binding to cells. It may also induce apoptosis by sequestering VEGF-165. It may also bind various members of the semaphorin family and its expression has an adverse effect on blood vessel number and integrity. The expression of isoforms 1 and 2 does not seem to overlap. Isoform 1 is expressed by the blood vessels of different tissues. In the developing embryo it is found predominantly in the nervous system. In adult tissues, it is highly expressed in heart and placenta, moderately in lung, liver, skeletal muscle, kidney and pancreas, and low in adult brain. Isoform 2 is found in liver hepatocytes, kidney distal and proximal tubules.