Nrp1

Domain

The tandem CUB domains mediate binding to semaphorin, while the tandem F5/8 domains are responsible for heparin and VEGF binding. F5/8 domains mediate the recognition and binding to R/KXXR/K CendR motifs.

Function

Cell-surface 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. Mediates the chemorepulsant activity of semaphorins. Recognizes a C-end rule (CendR) motif R/KXXR/K on its ligands which causes cellular internalization and vascular leakage. It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB (By similarity). Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulates VEGF-induced angiogenesis. Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity). Regulates mitochondrial iron transport via interaction with ABCB8/MITOSUR (By similarity).

Sequence Similarities

Belongs to the neuropilin family.

Tissue Specificity

Found in the embryonic nervous system (PubMed:9288754). Expressed in dorsal root ganglia (PubMed:28270793).

Cellular localization

• Mitochondrion membrane
• Single-pass type I membrane protein
• Cell membrane
• Single-pass type I membrane protein
• Cytoplasm

Alternative names

CD304, Neuropilin-1, Vascular endothelial cell growth factor 165 receptor, Nrp1

Database links

swissprot:Q9QWJ9 entrezGene:246331

Other research areas

• Immunology & Infectious Disease