ID NRP1_HUMAN Reviewed; 923 AA. AC O14786; B0LPG9; O60461; Q5T7F1; Q5T7F2; Q5T7F3; Q86T59; Q96I90; AC Q96IH5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 3. DT 13-FEB-2019, entry version 203. DE RecName: Full=Neuropilin-1; DE AltName: Full=Vascular endothelial cell growth factor 165 receptor; DE AltName: CD_antigen=CD304; DE Flags: Precursor; GN Name=NRP1; Synonyms=NRP, VEGF165R; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-179. RX PubMed=9288753; DOI=10.1016/S0092-8674(00)80534-6; RA He Z., Tessier-Lavigne M.; RT "Neuropilin is a receptor for the axonal chemorepellent semaphorin RT III."; RL Cell 90:739-751(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 22-39, AND RP VARIANT ALA-179. RC TISSUE=Mammary gland; RX PubMed=9529250; DOI=10.1016/S0092-8674(00)81402-6; RA Soker S., Takashima S., Miao H.-Q., Neufeld G., Klagsbrun M.; RT "Neuropilin-1 is expressed by endothelial and tumor cells as an RT isoform-specific receptor for vascular endothelial growth factor."; RL Cell 92:735-745(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 22-31, AND RP VARIANT ALA-179. RC TISSUE=Prostatic adenocarcinoma; RX PubMed=10688880; DOI=10.1073/pnas.040337597; RA Gagnon M.L., Bielenberg D.R., Gechtman Z., Miao H.-Q., Takashima S., RA Soker S., Klagsbrun M.; RT "Identification of a natural soluble neuropilin-1 that binds vascular RT endothelial growth factor: in vivo expression and antitumor RT activity."; RL Proc. Natl. Acad. Sci. U.S.A. 97:2573-2578(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP ALA-179. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP ALA-179. RC TISSUE=Skeletal muscle; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-179. RG SeattleSNPs variation discovery resource; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-179. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT RP ALA-179. RC TISSUE=Kidney, and Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP INTERACTION WITH PLXNB1. RX PubMed=10520995; DOI=10.1016/S0092-8674(00)80063-X; RA Tamagnone L., Artigiani S., Chen H., He Z., Ming G.-L., Song H.-L., RA Chedotal A., Winberg M.L., Goodman C.S., Poo M.-M., RA Tessier-Lavigne M., Comoglio P.M.; RT "Plexins are a large family of receptors for transmembrane, secreted RT and GPI-anchored semaphorins in vertebrates."; RL Cell 99:71-80(1999). RN [11] RP CHARACTERIZATION. RX PubMed=10748121; DOI=10.1074/jbc.M909259199; RA Gluzman-Poltorak Z., Cohen T., Herzog Y., Neufeld G.; RT "Neuropilin-2 is a receptor for the vascular endothelial growth factor RT (VEGF) forms VEGF-145 and VEGF-165."; RL J. Biol. Chem. 275:18040-18045(2000). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-150. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [13] RP GLYCOSYLATION AT SER-612. RX PubMed=16763549; DOI=10.1038/sj.emboj.7601188; RA Shintani Y., Takashima S., Asano Y., Kato H., Liao Y., Yamazaki S., RA Tsukamoto O., Seguchi O., Yamamoto H., Fukushima T., Sugahara K., RA Kitakaze M., Hori M.; RT "Glycosaminoglycan modification of neuropilin-1 modulates VEGFR2 RT signaling."; RL EMBO J. 25:3045-3055(2006). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-150; ASN-261 AND ASN-522. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP INTERACTION WITH VEGFA. RX PubMed=26503042; DOI=10.1038/nature15510; RA He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y., RA Dumitru C.D., Lettieri K., Shubayev V., Jordanova A., RA Guergueltcheva V., Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.; RT "CMT2D neuropathy is linked to the neomorphic binding activity of RT glycyl-tRNA synthetase."; RL Nature 526:710-714(2015). RN [17] RP ERRATUM. RX PubMed=26789244; DOI=10.1038/nature16499; RA He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y., RA Dan Dumitru C., Lettieri K., Shubayev V., Jordanova A., RA Guergueltcheva V., Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.; RT "Corrigendum: CMT2D neuropathy is linked to the neomorphic binding RT activity of glycyl-tRNA synthetase."; RL Nature 532:402-402(2016). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 273-427. RX PubMed=12517344; DOI=10.1016/S0969-2126(02)00941-3; RA Lee C.C., Kreusch A., McMullan D., Ng K., Spraggon G.; RT "Crystal structure of the human neuropilin-1 b1 domain."; RL Structure 11:99-108(2003). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 141-586 ALONE AND IN COMPLEX RP WITH ANTIBODY, GLYCOSYLATION AT ASN-150 AND ASN-261, SUBUNIT, RP CALCIUM-BINDING SITES, HEPARIN-BINDING, AND DISULFIDE BONDS. RX PubMed=17989695; DOI=10.1038/sj.emboj.7601906; RA Appleton B.A., Wu P., Maloney J., Yin J., Liang W.C., Stawicki S., RA Mortara K., Bowman K.K., Elliott J.M., Desmarais W., Bazan J.F., RA Bagri A., Tessier-Lavigne M., Koch A.W., Wu Y., Watts R.J., RA Wiesmann C.; RT "Structural studies of neuropilin/antibody complexes provide insights RT into semaphorin and VEGF binding."; RL EMBO J. 26:4902-4912(2007). CC -!- FUNCTION: The membrane-bound isoform 1 is a receptor involved in CC the development of the cardiovascular system, in angiogenesis, in CC the formation of certain neuronal circuits and in organogenesis CC outside the nervous system. It mediates the chemorepulsant CC activity of semaphorins. It binds to semaphorin 3A, The PLGF-2 CC isoform of PGF, The VEGF165 isoform of VEGFA and VEGFB. CC Coexpression with KDR results in increased VEGF165 binding to KDR CC as well as increased chemotaxis. Regulate VEGF-induced CC angiogenesis. Binding to VEGFA initiates a signaling pathway CC needed for motor neuron axon guidance and cell body migration, CC including for the caudal migration of facial motor neurons from CC rhombomere 4 to rhombomere 6 during embryonic development (By CC similarity). {ECO:0000250|UniProtKB:P97333}. CC -!- FUNCTION: The soluble isoform 2 binds VEGF-165 and appears to CC inhibit its binding to cells. It may also induce apoptosis by CC sequestering VEGF-165. May bind as well various members of the CC semaphorin family. Its expression has an averse effect on blood CC vessel number and integrity. CC -!- SUBUNIT: Homodimer, and heterodimer with NRP2. Interacts with FER CC (By similarity). Binds PLXNB1. Interacts with VEGFA CC (PubMed:26503042). {ECO:0000250, ECO:0000269|PubMed:10520995, CC ECO:0000269|PubMed:17989695, ECO:0000269|PubMed:26503042}. CC -!- INTERACTION: CC P21333:FLNA; NbExp=2; IntAct=EBI-1187100, EBI-350432; CC P08648:ITGA5; NbExp=2; IntAct=EBI-1187100, EBI-1382311; CC P35968:KDR; NbExp=2; IntAct=EBI-1187100, EBI-1005487; CC P15692:VEGFA; NbExp=4; IntAct=EBI-1187100, EBI-1026643; CC P15692-4:VEGFA; NbExp=4; IntAct=EBI-6285281, EBI-1026691; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. CC -!- SUBCELLULAR LOCATION: Isoform 2: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=Membrane-bound; CC IsoId=O14786-1; Sequence=Displayed; CC Name=2; Synonyms=Soluble, SNRP1; CC IsoId=O14786-2; Sequence=VSP_004339, VSP_004340; CC Name=3; CC IsoId=O14786-3; Sequence=VSP_053498, VSP_004339, VSP_004340; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: The expression of isoforms 1 and 2 does not CC seem to overlap. Isoform 1 is expressed by the blood vessels of CC different tissues. In the developing embryo it is found CC predominantly in the nervous system. In adult tissues, it is CC highly expressed in heart and placenta; moderately in lung, liver, CC skeletal muscle, kidney and pancreas; and low in adult brain. CC Isoform 2 is found in liver hepatocytes, kidney distal and CC proximal tubules. CC -!- DOMAIN: The tandem CUB domains mediate binding to semaphorin, CC while the tandem F5/8 domains are responsible for heparin and VEGF CC binding. CC -!- SIMILARITY: Belongs to the neuropilin family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF018956; AAC51759.1; -; mRNA. DR EMBL; AF016050; AAC12921.1; -; mRNA. DR EMBL; AF145712; AAF44344.1; -; mRNA. DR EMBL; BT006995; AAP35641.1; -; mRNA. DR EMBL; BX510902; CAD91133.1; -; mRNA. DR EMBL; EU332859; ABY87548.1; -; Genomic_DNA. DR EMBL; AL353600; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121748; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471072; EAW85942.1; -; Genomic_DNA. DR EMBL; CH471072; EAW85944.1; -; Genomic_DNA. DR EMBL; BC007533; AAH07533.1; -; mRNA. DR EMBL; BC007737; AAH07737.1; -; mRNA. DR CCDS; CCDS31179.1; -. [O14786-3] DR CCDS; CCDS31180.1; -. [O14786-2] DR CCDS; CCDS7177.1; -. [O14786-1] DR RefSeq; NP_001019799.1; NM_001024628.2. DR RefSeq; NP_001019800.1; NM_001024629.2. DR RefSeq; NP_001316997.1; NM_001330068.1. DR RefSeq; NP_003864.4; NM_003873.5. DR UniGene; Hs.131704; -. DR UniGene; Hs.653996; -. DR PDB; 1KEX; X-ray; 1.90 A; A=273-427. DR PDB; 2QQI; X-ray; 1.80 A; A=273-586. DR PDB; 2QQM; X-ray; 2.00 A; A=141-586. DR PDB; 2QQN; X-ray; 2.20 A; A=273-427. DR PDB; 3I97; X-ray; 2.90 A; A/B=273-427. DR PDB; 4DEQ; X-ray; 2.65 A; A/B=274-429. DR PDB; 4RN5; X-ray; 1.73 A; A=273-427. DR PDB; 5C7G; X-ray; 1.45 A; A=273-427. DR PDB; 5IJR; X-ray; 1.52 A; A/B=273-427. DR PDB; 5IYY; X-ray; 1.60 A; A/B=273-427. DR PDB; 5J1X; X-ray; 2.10 A; A/B/C/D=273-427. DR PDB; 5JGI; X-ray; 1.38 A; A/B=273-427. DR PDB; 5JGQ; X-ray; 1.60 A; A/B=273-427. DR PDB; 5JHK; X-ray; 1.80 A; A/B=273-427. DR PDB; 5L73; X-ray; 2.24 A; A/B=628-813. DR PDB; 6FMC; X-ray; 0.90 A; A=273-427. DR PDB; 6FMF; X-ray; 2.81 A; A=273-427. DR PDBsum; 1KEX; -. DR PDBsum; 2QQI; -. DR PDBsum; 2QQM; -. DR PDBsum; 2QQN; -. DR PDBsum; 3I97; -. DR PDBsum; 4DEQ; -. DR PDBsum; 4RN5; -. DR PDBsum; 5C7G; -. DR PDBsum; 5IJR; -. DR PDBsum; 5IYY; -. DR PDBsum; 5J1X; -. DR PDBsum; 5JGI; -. DR PDBsum; 5JGQ; -. DR PDBsum; 5JHK; -. DR PDBsum; 5L73; -. DR PDBsum; 6FMC; -. DR PDBsum; 6FMF; -. DR ProteinModelPortal; O14786; -. DR SMR; O14786; -. DR BioGrid; 114356; 49. DR CORUM; O14786; -. DR DIP; DIP-5743N; -. DR IntAct; O14786; 11. DR MINT; O14786; -. DR STRING; 9606.ENSP00000265371; -. DR BindingDB; O14786; -. DR ChEMBL; CHEMBL5174; -. DR DrugBank; DB00039; Palifermin. DR DrugBank; DB04895; Pegaptanib. DR GuidetoPHARMACOLOGY; 2998; -. DR GlyConnect; 1557; -. DR iPTMnet; O14786; -. DR PhosphoSitePlus; O14786; -. DR SwissPalm; O14786; -. DR BioMuta; NRP1; -. DR EPD; O14786; -. DR jPOST; O14786; -. DR MaxQB; O14786; -. DR PaxDb; O14786; -. DR PeptideAtlas; O14786; -. DR PRIDE; O14786; -. DR ProteomicsDB; 48233; -. DR ProteomicsDB; 48234; -. [O14786-2] DR DNASU; 8829; -. DR Ensembl; ENST00000265371; ENSP00000265371; ENSG00000099250. [O14786-1] DR Ensembl; ENST00000374821; ENSP00000363954; ENSG00000099250. [O14786-3] DR Ensembl; ENST00000374822; ENSP00000363955; ENSG00000099250. [O14786-2] DR Ensembl; ENST00000374867; ENSP00000364001; ENSG00000099250. [O14786-1] DR GeneID; 8829; -. DR KEGG; hsa:8829; -. DR UCSC; uc001iwx.5; human. [O14786-1] DR CTD; 8829; -. DR DisGeNET; 8829; -. DR EuPathDB; HostDB:ENSG00000099250.17; -. DR GeneCards; NRP1; -. DR HGNC; HGNC:8004; NRP1. DR HPA; CAB004511; -. DR HPA; HPA030278; -. DR MIM; 602069; gene. DR neXtProt; NX_O14786; -. DR OpenTargets; ENSG00000099250; -. DR PharmGKB; PA31783; -. DR eggNOG; ENOG410IE8T; Eukaryota. DR eggNOG; ENOG410YRBE; LUCA. DR GeneTree; ENSGT00940000157169; -. DR HOGENOM; HOG000039978; -. DR HOVERGEN; HBG000502; -. DR InParanoid; O14786; -. DR KO; K06724; -. DR OMA; HTAGDGN; -. DR OrthoDB; 124611at2759; -. DR PhylomeDB; O14786; -. DR TreeFam; TF316506; -. DR Reactome; R-HSA-194306; Neurophilin interactions with VEGF and VEGFR. DR Reactome; R-HSA-376176; Signaling by ROBO receptors. DR Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion. DR Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion. DR Reactome; R-HSA-399956; CRMPs in Sema3A signaling. DR Reactome; R-HSA-445144; Signal transduction by L1. DR Reactome; R-HSA-447041; CHL1 interactions. DR SIGNOR; O14786; -. DR ChiTaRS; NRP1; human. DR EvolutionaryTrace; O14786; -. DR GeneWiki; Neuropilin_1; -. DR GenomeRNAi; 8829; -. DR PRO; PR:O14786; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000099250; Expressed in 225 organ(s), highest expression level in caput epididymis. DR ExpressionAtlas; O14786; baseline and differential. DR Genevisible; O14786; HS. DR GO; GO:0030424; C:axon; ISS:BHF-UCL. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0031410; C:cytoplasmic vesicle; TAS:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL. DR GO; GO:0005769; C:early endosome; ISS:BHF-UCL. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:BHF-UCL. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0030426; C:growth cone; IEA:Ensembl. DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl. DR GO; GO:0005883; C:neurofilament; IEA:Ensembl. DR GO; GO:0043005; C:neuron projection; ISS:ARUK-UCL. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0043235; C:receptor complex; TAS:BHF-UCL. DR GO; GO:0002116; C:semaphorin receptor complex; NAS:BHF-UCL. DR GO; GO:0097443; C:sorting endosome; ISS:BHF-UCL. DR GO; GO:0015026; F:coreceptor activity; TAS:BHF-UCL. DR GO; GO:0019955; F:cytokine binding; NAS:BHF-UCL. DR GO; GO:0019838; F:growth factor binding; IPI:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; IMP:BHF-UCL. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0017154; F:semaphorin receptor activity; NAS:BHF-UCL. DR GO; GO:0038085; F:vascular endothelial growth factor binding; IPI:BHF-UCL. DR GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; ISS:BHF-UCL. DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:BHF-UCL. DR GO; GO:0001525; P:angiogenesis; IMP:BHF-UCL. DR GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; ISS:BHF-UCL. DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc. DR GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL. DR GO; GO:0048846; P:axon extension involved in axon guidance; ISS:BHF-UCL. DR GO; GO:0007411; P:axon guidance; TAS:ProtInc. DR GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl. DR GO; GO:0060385; P:axonogenesis involved in innervation; ISS:BHF-UCL. DR GO; GO:0150020; P:basal dendrite arborization; ISS:ARUK-UCL. DR GO; GO:0150018; P:basal dendrite development; ISS:ARUK-UCL. DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISS:BHF-UCL. DR GO; GO:0021785; P:branchiomotor neuron axon guidance; IEA:Ensembl. DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:BHF-UCL. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IMP:BHF-UCL. DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:BHF-UCL. DR GO; GO:0071679; P:commissural neuron axon guidance; ISS:BHF-UCL. DR GO; GO:0060982; P:coronary artery morphogenesis; IEA:Ensembl. DR GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IEA:Ensembl. DR GO; GO:1904835; P:dorsal root ganglion morphogenesis; IEA:Ensembl. DR GO; GO:0035767; P:endothelial cell chemotaxis; IMP:BHF-UCL. DR GO; GO:0043542; P:endothelial cell migration; IMP:BHF-UCL. DR GO; GO:0097102; P:endothelial tip cell fate specification; ISS:BHF-UCL. DR GO; GO:0021612; P:facial nerve structural organization; IEA:Ensembl. DR GO; GO:1903375; P:facioacoustic ganglion development; IEA:Ensembl. DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IEA:Ensembl. DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:BHF-UCL. DR GO; GO:0097475; P:motor neuron migration; ISS:UniProtKB. DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IEA:Ensembl. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0021675; P:nerve development; ISS:BHF-UCL. DR GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; ISS:BHF-UCL. DR GO; GO:0001764; P:neuron migration; ISS:BHF-UCL. DR GO; GO:0038189; P:neuropilin signaling pathway; IMP:BHF-UCL. DR GO; GO:1905040; P:otic placode development; IEA:Ensembl. DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL. DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0050918; P:positive chemotaxis; ISS:BHF-UCL. DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:BHF-UCL. DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISS:BHF-UCL. DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl. DR GO; GO:0060301; P:positive regulation of cytokine activity; TAS:BHF-UCL. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; TAS:BHF-UCL. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL. DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:BHF-UCL. DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:BHF-UCL. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL. DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:BHF-UCL. DR GO; GO:1902336; P:positive regulation of retinal ganglion cell axon guidance; ISS:BHF-UCL. DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; TAS:BHF-UCL. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:BHF-UCL. DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:BHF-UCL. DR GO; GO:0099173; P:postsynapse organization; IEA:Ensembl. DR GO; GO:1902946; P:protein localization to early endosome; ISS:BHF-UCL. DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IMP:BHF-UCL. DR GO; GO:0090259; P:regulation of retinal ganglion cell axon guidance; ISS:BHF-UCL. DR GO; GO:0060627; P:regulation of vesicle-mediated transport; TAS:BHF-UCL. DR GO; GO:0061441; P:renal artery morphogenesis; IEA:Ensembl. DR GO; GO:0009611; P:response to wounding; IEA:Ensembl. DR GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; ISS:BHF-UCL. DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:BHF-UCL. DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; NAS:BHF-UCL. DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IEA:Ensembl. DR GO; GO:1902285; P:semaphorin-plexin signaling pathway involved in neuron projection guidance; ISS:BHF-UCL. DR GO; GO:0097374; P:sensory neuron axon guidance; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0002040; P:sprouting angiogenesis; ISS:BHF-UCL. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:BHF-UCL. DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IMP:BHF-UCL. DR GO; GO:0061549; P:sympathetic ganglion development; ISS:BHF-UCL. DR GO; GO:0097490; P:sympathetic neuron projection extension; ISS:BHF-UCL. DR GO; GO:0097491; P:sympathetic neuron projection guidance; ISS:BHF-UCL. DR GO; GO:1901998; P:toxin transport; IEA:Ensembl. DR GO; GO:0061551; P:trigeminal ganglion development; IEA:Ensembl. DR GO; GO:0021637; P:trigeminal nerve structural organization; IEA:Ensembl. DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0038190; P:VEGF-activated neuropilin signaling pathway; IMP:BHF-UCL. DR GO; GO:1902378; P:VEGF-activated neuropilin signaling pathway involved in axon guidance; IEA:Ensembl. DR GO; GO:0036486; P:ventral trunk neural crest cell migration; IEA:Ensembl. DR GO; GO:0021649; P:vestibulocochlear nerve structural organization; IEA:Ensembl. DR CDD; cd00041; CUB; 2. DR CDD; cd00057; FA58C; 2. DR CDD; cd06263; MAM; 1. DR Gene3D; 2.60.120.260; -; 2. DR Gene3D; 2.60.120.290; -; 2. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000859; CUB_dom. DR InterPro; IPR000421; FA58C. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR000998; MAM_dom. DR InterPro; IPR014648; Neuropilin. DR InterPro; IPR022579; Neuropilin_C. DR InterPro; IPR027146; NRP1. DR InterPro; IPR035914; Sperma_CUB_dom_sf. DR PANTHER; PTHR44185; PTHR44185; 1. DR PANTHER; PTHR44185:SF1; PTHR44185:SF1; 1. DR Pfam; PF00431; CUB; 2. DR Pfam; PF11980; DUF3481; 1. DR Pfam; PF00754; F5_F8_type_C; 2. DR Pfam; PF00629; MAM; 1. DR PIRSF; PIRSF036960; Neuropilin; 1. DR PRINTS; PR00020; MAMDOMAIN. DR SMART; SM00042; CUB; 2. DR SMART; SM00231; FA58C; 2. DR SMART; SM00137; MAM; 1. DR SUPFAM; SSF49785; SSF49785; 2. DR SUPFAM; SSF49854; SSF49854; 2. DR SUPFAM; SSF49899; SSF49899; 1. DR PROSITE; PS01180; CUB; 2. DR PROSITE; PS01285; FA58C_1; 2. DR PROSITE; PS01286; FA58C_2; 2. DR PROSITE; PS50022; FA58C_3; 2. DR PROSITE; PS00740; MAM_1; 1. DR PROSITE; PS50060; MAM_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Angiogenesis; Calcium; KW Cell membrane; Complete proteome; Developmental protein; KW Differentiation; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Heparan sulfate; Heparin-binding; Membrane; KW Metal-binding; Neurogenesis; Phosphoprotein; Polymorphism; KW Proteoglycan; Receptor; Reference proteome; Repeat; Secreted; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 21 {ECO:0000269|PubMed:10688880, FT ECO:0000269|PubMed:9529250}. FT CHAIN 22 923 Neuropilin-1. FT /FTId=PRO_0000021859. FT TOPO_DOM 22 856 Extracellular. {ECO:0000255}. FT TRANSMEM 857 879 Helical. {ECO:0000255}. FT TOPO_DOM 880 923 Cytoplasmic. {ECO:0000255}. FT DOMAIN 27 141 CUB 1. {ECO:0000255|PROSITE- FT ProRule:PRU00059}. FT DOMAIN 147 265 CUB 2. {ECO:0000255|PROSITE- FT ProRule:PRU00059}. FT DOMAIN 275 424 F5/8 type C 1. {ECO:0000255|PROSITE- FT ProRule:PRU00081}. FT DOMAIN 431 583 F5/8 type C 2. {ECO:0000255|PROSITE- FT ProRule:PRU00081}. FT DOMAIN 645 811 MAM. {ECO:0000255|PROSITE- FT ProRule:PRU00128}. FT METAL 195 195 Calcium. {ECO:0000244|PDB:2QQM, FT ECO:0000269|PubMed:17989695}. FT METAL 209 209 Calcium. {ECO:0000244|PDB:2QQM, FT ECO:0000269|PubMed:17989695}. FT METAL 250 250 Calcium. {ECO:0000244|PDB:2QQM, FT ECO:0000269|PubMed:17989695}. FT MOD_RES 894 894 Phosphoserine. FT {ECO:0000250|UniProtKB:P97333}. FT CARBOHYD 150 150 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:17989695, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 261 261 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:17989695, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 300 300 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 522 522 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 612 612 O-linked (Xyl...) (chondroitin sulfate) FT serine; alternate. FT {ECO:0000269|PubMed:16763549}. FT CARBOHYD 612 612 O-linked (Xyl...) (heparan sulfate) FT serine; alternate. FT {ECO:0000269|PubMed:16763549}. FT CARBOHYD 842 842 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 27 54 {ECO:0000305|PubMed:17989695}. FT DISULFID 82 104 {ECO:0000305|PubMed:17989695}. FT DISULFID 147 173 {ECO:0000269|PubMed:17989695}. FT DISULFID 206 228 {ECO:0000269|PubMed:17989695}. FT DISULFID 275 424 {ECO:0000269|PubMed:17989695}. FT DISULFID 431 583 {ECO:0000269|PubMed:17989695}. FT VAR_SEQ 587 621 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_053498. FT VAR_SEQ 642 644 EFP -> GIK (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:10688880, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.4}. FT /FTId=VSP_004339. FT VAR_SEQ 645 923 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:10688880, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.4}. FT /FTId=VSP_004340. FT VARIANT 179 179 V -> A (in dbSNP:rs7079053). FT {ECO:0000269|PubMed:10688880, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17974005, FT ECO:0000269|PubMed:9288753, FT ECO:0000269|PubMed:9529250, FT ECO:0000269|Ref.4, ECO:0000269|Ref.6, FT ECO:0000269|Ref.8}. FT /FTId=VAR_046536. FT VARIANT 561 561 F -> L (in dbSNP:rs2228637). FT /FTId=VAR_046537. FT VARIANT 733 733 V -> I (in dbSNP:rs2228638). FT /FTId=VAR_056957. FT CONFLICT 26 26 K -> E (in Ref. 1; AAC51759). FT {ECO:0000305}. FT CONFLICT 219 219 D -> G (in Ref. 5; CAD91133). FT {ECO:0000305}. FT CONFLICT 749 749 D -> H (in Ref. 2; AAC12921). FT {ECO:0000305}. FT CONFLICT 855 855 D -> E (in Ref. 1; AAC51759). FT {ECO:0000305}. FT STRAND 149 151 {ECO:0000244|PDB:2QQM}. FT STRAND 153 159 {ECO:0000244|PDB:2QQM}. FT TURN 161 164 {ECO:0000244|PDB:2QQM}. FT STRAND 172 178 {ECO:0000244|PDB:2QQM}. FT HELIX 180 182 {ECO:0000244|PDB:2QQM}. FT STRAND 185 193 {ECO:0000244|PDB:2QQM}. FT STRAND 208 217 {ECO:0000244|PDB:2QQM}. FT TURN 218 220 {ECO:0000244|PDB:2QQM}. FT STRAND 223 227 {ECO:0000244|PDB:2QQM}. FT STRAND 235 238 {ECO:0000244|PDB:2QQM}. FT STRAND 240 248 {ECO:0000244|PDB:2QQM}. FT STRAND 257 264 {ECO:0000244|PDB:2QQM}. FT TURN 273 275 {ECO:0000244|PDB:4RN5}. FT TURN 281 283 {ECO:0000244|PDB:6FMC}. FT STRAND 284 286 {ECO:0000244|PDB:5JGI}. FT HELIX 288 290 {ECO:0000244|PDB:6FMC}. FT STRAND 291 294 {ECO:0000244|PDB:6FMC}. FT HELIX 299 301 {ECO:0000244|PDB:6FMC}. FT HELIX 303 306 {ECO:0000244|PDB:6FMC}. FT STRAND 318 323 {ECO:0000244|PDB:3I97}. FT STRAND 326 342 {ECO:0000244|PDB:6FMC}. FT TURN 347 349 {ECO:0000244|PDB:6FMC}. FT STRAND 352 368 {ECO:0000244|PDB:6FMC}. FT STRAND 369 371 {ECO:0000244|PDB:1KEX}. FT STRAND 373 378 {ECO:0000244|PDB:5C7G}. FT STRAND 385 389 {ECO:0000244|PDB:6FMC}. FT STRAND 391 414 {ECO:0000244|PDB:6FMC}. FT STRAND 417 424 {ECO:0000244|PDB:6FMC}. FT HELIX 426 428 {ECO:0000244|PDB:2QQI}. FT TURN 437 439 {ECO:0000244|PDB:2QQI}. FT HELIX 444 446 {ECO:0000244|PDB:2QQI}. FT STRAND 447 449 {ECO:0000244|PDB:2QQI}. FT TURN 450 453 {ECO:0000244|PDB:2QQI}. FT HELIX 459 462 {ECO:0000244|PDB:2QQI}. FT TURN 464 466 {ECO:0000244|PDB:2QQM}. FT STRAND 471 473 {ECO:0000244|PDB:2QQM}. FT STRAND 485 502 {ECO:0000244|PDB:2QQI}. FT TURN 506 508 {ECO:0000244|PDB:2QQM}. FT STRAND 515 525 {ECO:0000244|PDB:2QQI}. FT STRAND 534 537 {ECO:0000244|PDB:2QQI}. FT STRAND 544 547 {ECO:0000244|PDB:2QQI}. FT STRAND 550 566 {ECO:0000244|PDB:2QQI}. FT STRAND 570 572 {ECO:0000244|PDB:2QQI}. FT STRAND 576 584 {ECO:0000244|PDB:2QQI}. FT HELIX 643 645 {ECO:0000244|PDB:5L73}. FT TURN 646 648 {ECO:0000244|PDB:5L73}. FT STRAND 667 671 {ECO:0000244|PDB:5L73}. FT STRAND 674 677 {ECO:0000244|PDB:5L73}. FT STRAND 680 682 {ECO:0000244|PDB:5L73}. FT TURN 686 689 {ECO:0000244|PDB:5L73}. FT STRAND 690 696 {ECO:0000244|PDB:5L73}. FT HELIX 699 701 {ECO:0000244|PDB:5L73}. FT STRAND 705 713 {ECO:0000244|PDB:5L73}. FT STRAND 720 728 {ECO:0000244|PDB:5L73}. FT STRAND 733 742 {ECO:0000244|PDB:5L73}. FT STRAND 744 746 {ECO:0000244|PDB:5L73}. FT STRAND 749 757 {ECO:0000244|PDB:5L73}. FT STRAND 761 770 {ECO:0000244|PDB:5L73}. FT STRAND 777 785 {ECO:0000244|PDB:5L73}. FT STRAND 792 800 {ECO:0000244|PDB:5L73}. FT TURN 806 808 {ECO:0000244|PDB:5L73}. FT STRAND 809 811 {ECO:0000244|PDB:5L73}. SQ SEQUENCE 923 AA; 103134 MW; 1EAC2FA6C8FD6A0B CRC64; MERGLPLLCA VLALVLAPAG AFRNDKCGDT IKIESPGYLT SPGYPHSYHP SEKCEWLIQA PDPYQRIMIN FNPHFDLEDR DCKYDYVEVF DGENENGHFR GKFCGKIAPP PVVSSGPFLF IKFVSDYETH GAGFSIRYEI FKRGPECSQN YTTPSGVIKS PGFPEKYPNS LECTYIVFVP KMSEIILEFE SFDLEPDSNP PGGMFCRYDR LEIWDGFPDV GPHIGRYCGQ KTPGRIRSSS GILSMVFYTD SAIAKEGFSA NYSVLQSSVS EDFKCMEALG MESGEIHSDQ ITASSQYSTN WSAERSRLNY PENGWTPGED SYREWIQVDL GLLRFVTAVG TQGAISKETK KKYYVKTYKI DVSSNGEDWI TIKEGNKPVL FQGNTNPTDV VVAVFPKPLI TRFVRIKPAT WETGISMRFE VYGCKITDYP CSGMLGMVSG LISDSQITSS NQGDRNWMPE NIRLVTSRSG WALPPAPHSY INEWLQIDLG EEKIVRGIII QGGKHRENKV FMRKFKIGYS NNGSDWKMIM DDSKRKAKSF EGNNNYDTPE LRTFPALSTR FIRIYPERAT HGGLGLRMEL LGCEVEAPTA GPTTPNGNLV DECDDDQANC HSGTGDDFQL TGGTTVLATE KPTVIDSTIQ SEFPTYGFNC EFGWGSHKTF CHWEHDNHVQ LKWSVLTSKT GPIQDHTGDG NFIYSQADEN QKGKVARLVS PVVYSQNSAH CMTFWYHMSG SHVGTLRVKL RYQKPEEYDQ LVWMAIGHQG DHWKEGRVLL HKSLKLYQVI FEGEIGKGNL GGIAVDDISI NNHISQEDCA KPADLDKKNP EIKIDETGST PGYEGEGEGD KNISRKPGNV LKTLDPILIT IIAMSALGVL LGAVCGVVLY CACWHNGMSE RNLSALENYN FELVDGVKLK KDKLNTQSTY SEA //