Neuropilin 1

PDB rendering based on 1kex.

Available structures
PDB	1KEX, 2QQI, 2QQM, 2QQN, 3I97

Identifiers

Symbols

NRP1; BDCA4; CD304; DKFZp686A03134; DKFZp781F1414; NP1; NRP; VEGF165R

External IDs

OMIM: 602069 MGI: 106206 HomoloGene: 2876 GeneCards: NRP1 Gene

Gene Ontology
Molecular function	• receptor activity • vascular endothelial growth factor receptor activity • protein binding • heparin binding • semaphorin receptor activity • growth factor binding • identical protein binding • metal ion binding
Cellular component	• extracellular region • neurofilament • plasma membrane • plasma membrane • cell surface • integral to membrane • axon • growth cone • neuronal cell body
Biological process	• patterning of blood vessels • cell adhesion • signal transduction • cell-cell signaling • multicellular organismal development • nervous system development • axon guidance • axonal fasciculation • heart development • positive regulation of cell proliferation • response to wounding • organ morphogenesis • dendrite development • cell migration • trigeminal nerve morphogenesis • cell differentiation • vascular endothelial growth factor receptor signaling pathway • sympathetic nervous system development • negative regulation of axon extension involved in axon guidance • dichotomous subdivision of terminal units involved in salivary gland branching
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 10:
33.47 – 33.63 Mb

Chr 8:
130.88 – 131.03 Mb

PubMed search

[1]

[2]

Neuropilin-1 is a protein that in humans is encoded by the NRP1 gene.^[1]^[2]^[3]. This is one of two human neuropilins.

NRP1 is a membrane-bound coreceptor to a tyrosine kinase receptor for both vascular endothelial growth factor (VEGF; MIM 192240) and semaphorin (see SEMA3A; MIM 603961) family members. NRP1 plays versatile roles in angiogenesis, axon guidance, cell survival, migration, and invasion.[supplied by OMIM]^[3]

Interactions

Neuropilin 1 has been shown to interact with Vascular endothelial growth factor A.^[4]^[1]

References

^ ^a ^b Soker S, Takashima S, Miao HQ, Neufeld G, Klagsbrun M (Apr 1998). "Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor". Cell 92 (6): 735–45. doi:10.1016/S0092-8674(00)81402-6. PMID 9529250.
^ Chen H, Chedotal A, He Z, Goodman CS, Tessier-Lavigne M (Nov 1997). "Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III". Neuron 19 (3): 547–59. doi:10.1016/S0896-6273(00)80371-2. PMID 9331348.
^ ^a ^b "Entrez Gene: NRP1 neuropilin 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8829.
^ Mamluk, Roni; Gechtman Ze'ev, Kutcher Matthew E, Gasiunas Nijole, Gallagher John, Klagsbrun Michael (Jul. 2002). "Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain". J. Biol. Chem. (United States) 277 (27): 24818–25. doi:10.1074/jbc.M200730200. ISSN 0021-9258. PMID 11986311.

Zachary I, Gliki G (2001). "Signaling transduction mechanisms mediating biological actions of the vascular endothelial growth factor family.". Cardiovasc. Res. 49 (3): 568–81. doi:10.1016/S0008-6363(00)00268-6. PMID 11166270.
He Z, Tessier-Lavigne M (1997). "Neuropilin is a receptor for the axonal chemorepellent Semaphorin III.". Cell 90 (4): 739–51. doi:10.1016/S0092-8674(00)80534-6. PMID 9288753.
Giger RJ, Urquhart ER, Gillespie SK, et al. (1999). "Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity.". Neuron 21 (5): 1079–92. doi:10.1016/S0896-6273(00)80625-X. PMID 9856463.
Chen H, He Z, Bagri A, Tessier-Lavigne M (1999). "Semaphorin-neuropilin interactions underlying sympathetic axon responses to class III semaphorins.". Neuron 21 (6): 1283–90. doi:10.1016/S0896-6273(00)80648-0. PMID 9883722.
Takahashi T, Nakamura F, Jin Z, et al. (1999). "Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors.". Nat. Neurosci. 1 (6): 487–93. doi:10.1038/2203. PMID 10196546.
Rossignol M, Beggs AH, Pierce EA, Klagsbrun M (1999). "Human neuropilin-1 and neuropilin-2 map to 10p12 and 2q34, respectively.". Genomics 57 (3): 459–60. doi:10.1006/geno.1999.5790. PMID 10329017.
Makinen T, Olofsson B, Karpanen T, et al. (1999). "Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1.". J. Biol. Chem. 274 (30): 21217–22. doi:10.1074/jbc.274.30.21217. PMID 10409677.
Cai H, Reed RR (1999). "Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1.". J. Neurosci. 19 (15): 6519–27. PMID 10414980.
Takahashi T, Fournier A, Nakamura F, et al. (1999). "Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors.". Cell 99 (1): 59–69. doi:10.1016/S0092-8674(00)80062-8. PMID 10520994.
Tamagnone L, Artigiani S, Chen H, et al. (1999). "Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates.". Cell 99 (1): 71–80. doi:10.1016/S0092-8674(00)80063-X. PMID 10520995.
Gagnon ML, Bielenberg DR, Gechtman Z, et al. (2000). "Identification of a natural soluble neuropilin-1 that binds vascular endothelial growth factor: In vivo expression and antitumor activity.". Proc. Natl. Acad. Sci. U.S.A. 97 (6): 2573–8. doi:10.1073/pnas.040337597. PMC 15970. PMID 10688880. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=15970.
Gluzman-Poltorak Z, Cohen T, Herzog Y, Neufeld G (2000). "Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165 [corrected].". J. Biol. Chem. 275 (24): 18040–5. doi:10.1074/jbc.M909259199. PMID 10748121.
Fuh G, Garcia KC, de Vos AM (2000). "The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1.". J. Biol. Chem. 275 (35): 26690–5. doi:10.1074/jbc.M003955200. PMID 10842181.
Rossignol M, Gagnon ML, Klagsbrun M (2001). "Genomic organization of human neuropilin-1 and neuropilin-2 genes: identification and distribution of splice variants and soluble isoforms.". Genomics 70 (2): 211–22. doi:10.1006/geno.2000.6381. PMID 11112349.
Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing.". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1083732.
Whitaker GB, Limberg BJ, Rosenbaum JS (2001). "Vascular endothelial growth factor receptor-2 and neuropilin-1 form a receptor complex that is responsible for the differential signaling potency of VEGF(165) and VEGF(121).". J. Biol. Chem. 276 (27): 25520–31. doi:10.1074/jbc.M102315200. PMID 11333271.
Walter JW, North PE, Waner M, et al. (2002). "Somatic mutation of vascular endothelial growth factor receptors in juvenile hemangioma.". Genes Chromosomes Cancer 33 (3): 295–303. doi:10.1002/gcc.10028. PMID 11807987.

PDB gallery

1kex: Crystal Structure of the b1 Domain of Human Neuropilin-1

2orx: Structural Basis for Ligand Binding and Heparin Mediated Activation of Neuropilin

2orz: Structural Basis for Ligand Binding and Heparin Mediated Activation of Neuropilin

Neuropilin 1

Interactions

References

Further reading