ID NRP2_HUMAN Reviewed; 931 AA. AC O60462; A0A024R3W6; A0A024R412; E9PF66; O14820; O14821; Q53TQ4; AC Q53TS3; Q7LBX6; Q7LBX7; Q9H2D4; Q9H2D5; Q9H2E2; Q9H2E3; Q9H2E4; AC X5D2Q8; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 3. DT 13-FEB-2019, entry version 179. DE RecName: Full=Neuropilin-2; DE AltName: Full=Vascular endothelial cell growth factor 165 receptor 2; DE Flags: Precursor; GN Name=NRP2; Synonyms=VEGF165R2; 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] (ISOFORMS A0 AND A17), AND VARIANT LYS-602. RX PubMed=9331348; DOI=10.1016/S0896-6273(00)80371-2; RA Chen H., Chedotal A., He Z.-G., Goodman C.S., Tessier-Lavigne M.; RT "Neuropilin-2, a novel member of the neuropilin family, is a high RT affinity receptor for the semaphorins Sema E and Sema IV but not Sema RT III."; RL Neuron 19:547-559(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A22). 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 [GENOMIC DNA / MRNA] (ISOFORMS B0; B5 AND S9), RP VARIANT LYS-602, ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION. RX PubMed=11112349; DOI=10.1006/geno.2000.6381; RA Rossignol M., Gagnon M.L., Klagsbrun M.; RT "Genomic organization of human neuropilin-1 and neuropilin-2 genes: RT identification and distribution of splice variants and soluble RT isoforms."; RL Genomics 70:211-222(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-123. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B0 AND B5). RC TISSUE=Brain; 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 [7] 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 [8] 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 [9] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN RP CYTOMEGALOVIRUS PROTEIN GL; UL128; UL130 AND UL131A (MICROBIAL RP INFECTION). RX PubMed=30057110; DOI=10.1016/j.cell.2018.06.028; RA Martinez-Martin N., Marcandalli J., Huang C.S., Arthur C.P., RA Perotti M., Foglierini M., Ho H., Dosey A.M., Shriver S., Payandeh J., RA Leitner A., Lanzavecchia A., Perez L., Ciferri C.; RT "An Unbiased Screen for Human Cytomegalovirus Identifies Neuropilin-2 RT as a Central Viral Receptor."; RL Cell 0:0-0(2018). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 23-595 ALONE AND IN COMPLEX RP WITH ANTIBODY, SUBUNIT, CALCIUM-BINDING SITES, DISULFIDE BONDS, AND RP GLYCOSYLATION AT ASN-152 AND ASN-157. 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). RN [11] RP VARIANTS CYS-334 AND TRP-428. RX PubMed=22365152; DOI=10.1016/j.ajhg.2012.01.006; RA Veeramah K.R., O'Brien J.E., Meisler M.H., Cheng X., Dib-Hajj S.D., RA Waxman S.G., Talwar D., Girirajan S., Eichler E.E., Restifo L.L., RA Erickson R.P., Hammer M.F.; RT "de novo pathogenic SCN8A mutation identified by whole-genome RT sequencing of a family quartet affected by infantile epileptic RT encephalopathy and SUDEP."; RL Am. J. Hum. Genet. 90:502-510(2012). CC -!- FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165 CC and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for human CC cytomegalovirus pentamer-dependent entry in epithelial and CC endothelial cells. {ECO:0000269|PubMed:30057110}. CC -!- SUBUNIT: Heterodimer with NRP1. Binds PLXNB1. CC {ECO:0000269|PubMed:17989695}. CC -!- SUBUNIT: (Microbial infection) Interacts with human CC cytomegalovirus proteins gL, UL128, UL130 and UL131A. CC {ECO:0000269|PubMed:30057110}. CC -!- INTERACTION: CC P97953-1:Vegfc (xeno); NbExp=3; IntAct=EBI-12586256, EBI-16148671; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11112349}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:11112349}. CC -!- SUBCELLULAR LOCATION: Isoform s9: Secreted CC {ECO:0000269|PubMed:11112349}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=A22; CC IsoId=O60462-1; Sequence=Displayed; CC Name=A0; CC IsoId=O60462-2; Sequence=VSP_004342; CC Name=A17; CC IsoId=O60462-3; Sequence=VSP_004341; CC Name=B0; CC IsoId=O60462-4; Sequence=VSP_004341, VSP_041160; CC Name=B5; CC IsoId=O60462-5; Sequence=VSP_041160; CC Name=s9; CC IsoId=O60462-6; Sequence=VSP_044908, VSP_044909; 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; AF022859; AAC51788.1; -; mRNA. DR EMBL; AF022860; AAC51789.1; -; mRNA. DR EMBL; AF016098; AAC12922.1; -; mRNA. DR EMBL; AF280544; AAG41403.1; -; mRNA. DR EMBL; AF280545; AAG41404.1; -; mRNA. DR EMBL; AF280546; AAG41405.1; -; mRNA. DR EMBL; KJ534899; AHW56539.1; -; mRNA. DR EMBL; AF281074; AAG41897.1; -; Genomic_DNA. DR EMBL; AF281074; AAG41898.1; -; Genomic_DNA. DR EMBL; AF281074; AAG41899.1; -; Genomic_DNA. DR EMBL; AF281074; AAG41900.1; -; Genomic_DNA. DR EMBL; AC007362; AAX93216.1; -; Genomic_DNA. DR EMBL; AC007561; AAY14875.1; -; Genomic_DNA. DR EMBL; KF459587; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471063; EAW70362.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70363.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70364.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70366.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70368.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70369.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70371.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70372.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70373.1; -; Genomic_DNA. DR EMBL; BC101525; AAI01526.1; -; mRNA. DR EMBL; BC104770; AAI04771.1; -; mRNA. DR EMBL; BC143238; AAI43239.1; -; mRNA. DR EMBL; BC117413; AAI17414.1; -; mRNA. DR CCDS; CCDS2364.1; -. [O60462-1] DR CCDS; CCDS2365.1; -. [O60462-5] DR CCDS; CCDS46496.1; -. [O60462-3] DR CCDS; CCDS46497.1; -. [O60462-2] DR CCDS; CCDS46498.1; -. [O60462-4] DR CCDS; CCDS46499.1; -. [O60462-6] DR RefSeq; NP_003863.2; NM_003872.2. [O60462-3] DR RefSeq; NP_061004.3; NM_018534.3. [O60462-5] DR RefSeq; NP_957716.1; NM_201264.1. [O60462-6] DR RefSeq; NP_957718.1; NM_201266.1. [O60462-1] DR RefSeq; NP_957719.1; NM_201267.1. [O60462-4] DR RefSeq; NP_958436.1; NM_201279.1. [O60462-2] DR RefSeq; XP_005246990.2; XM_005246933.3. DR RefSeq; XP_005246991.2; XM_005246934.3. DR RefSeq; XP_016860674.1; XM_017005185.1. DR RefSeq; XP_016860675.1; XM_017005186.1. DR UniGene; Hs.471200; -. DR UniGene; Hs.660596; -. DR PDB; 2QQJ; X-ray; 1.95 A; A=275-595. DR PDB; 2QQK; X-ray; 2.75 A; A=23-595. DR PDB; 2QQL; X-ray; 3.10 A; A=23-595. DR PDB; 2QQO; X-ray; 2.30 A; A/B=145-595. DR PDB; 4QDQ; X-ray; 1.95 A; A/B=276-595. DR PDB; 4QDR; X-ray; 2.40 A; A=276-595. DR PDB; 4QDS; X-ray; 2.40 A; A/B=275-457. DR PDB; 5DN2; X-ray; 1.95 A; A/B/C/D=275-429. DR PDB; 5DQ0; X-ray; 1.80 A; A=275-430. DR PDB; 6GH8; X-ray; 2.44 A; A/C=27-146. DR PDBsum; 2QQJ; -. DR PDBsum; 2QQK; -. DR PDBsum; 2QQL; -. DR PDBsum; 2QQO; -. DR PDBsum; 4QDQ; -. DR PDBsum; 4QDR; -. DR PDBsum; 4QDS; -. DR PDBsum; 5DN2; -. DR PDBsum; 5DQ0; -. DR PDBsum; 6GH8; -. DR ProteinModelPortal; O60462; -. DR SMR; O60462; -. DR BioGrid; 114355; 21. DR CORUM; O60462; -. DR DIP; DIP-5745N; -. DR IntAct; O60462; 2. DR STRING; 9606.ENSP00000353582; -. DR iPTMnet; O60462; -. DR PhosphoSitePlus; O60462; -. DR SwissPalm; O60462; -. DR BioMuta; NRP2; -. DR jPOST; O60462; -. DR PaxDb; O60462; -. DR PeptideAtlas; O60462; -. DR PRIDE; O60462; -. DR ProteomicsDB; 49409; -. DR ProteomicsDB; 49410; -. [O60462-2] DR ProteomicsDB; 49411; -. [O60462-3] DR ProteomicsDB; 49412; -. [O60462-4] DR ProteomicsDB; 49413; -. [O60462-5] DR DNASU; 8828; -. DR Ensembl; ENST00000272849; ENSP00000272849; ENSG00000118257. [O60462-5] DR Ensembl; ENST00000357118; ENSP00000349632; ENSG00000118257. [O60462-4] DR Ensembl; ENST00000357785; ENSP00000350432; ENSG00000118257. [O60462-3] DR Ensembl; ENST00000360409; ENSP00000353582; ENSG00000118257. [O60462-1] DR Ensembl; ENST00000412873; ENSP00000407626; ENSG00000118257. [O60462-2] DR Ensembl; ENST00000417189; ENSP00000387519; ENSG00000118257. [O60462-6] DR GeneID; 8828; -. DR KEGG; hsa:8828; -. DR UCSC; uc002vau.4; human. [O60462-1] DR UCSC; uc002vav.4; human. DR UCSC; uc002vaw.3; human. DR UCSC; uc002vax.4; human. DR UCSC; uc002vay.4; human. DR CTD; 8828; -. DR DisGeNET; 8828; -. DR EuPathDB; HostDB:ENSG00000118257.16; -. DR GeneCards; NRP2; -. DR HGNC; HGNC:8005; NRP2. DR HPA; HPA039980; -. DR HPA; HPA054974; -. DR MIM; 602070; gene. DR neXtProt; NX_O60462; -. DR OpenTargets; ENSG00000118257; -. DR PharmGKB; PA31784; -. DR eggNOG; ENOG410IHB5; Eukaryota. DR eggNOG; ENOG410ZPIE; LUCA. DR GeneTree; ENSGT00940000155270; -. DR HOVERGEN; HBG000502; -. DR InParanoid; O60462; -. DR KO; K06819; -. DR OMA; NCNFDLP; -. DR OrthoDB; 124611at2759; -. DR PhylomeDB; O60462; -. DR TreeFam; TF316506; -. DR Reactome; R-HSA-194306; Neurophilin interactions with VEGF and VEGFR. DR Reactome; R-HSA-447038; NrCAM interactions. DR SIGNOR; O60462; -. DR ChiTaRS; NRP2; human. DR EvolutionaryTrace; O60462; -. DR GeneWiki; NRP2; -. DR GenomeRNAi; 8828; -. DR PRO; PR:O60462; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000118257; Expressed in 176 organ(s), highest expression level in lower esophagus. DR ExpressionAtlas; O60462; baseline and differential. DR Genevisible; O60462; HS. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB. DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0002116; C:semaphorin receptor complex; NAS:BHF-UCL. DR GO; GO:0019955; F:cytokine binding; NAS:BHF-UCL. DR GO; GO:0019838; F:growth factor binding; TAS:BHF-UCL. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017154; F:semaphorin receptor activity; NAS:UniProtKB. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; TAS:ProtInc. DR GO; GO:0001525; P:angiogenesis; NAS:UniProtKB. 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:0007155; P:cell adhesion; NAS:UniProtKB. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl. DR GO; GO:1904835; P:dorsal root ganglion morphogenesis; IEA:Ensembl. 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:0050919; P:negative chemotaxis; 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; IEA:Ensembl. DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; TAS:BHF-UCL. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; TAS:BHF-UCL. DR GO; GO:0099175; P:regulation of postsynapse organization; 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: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:0061551; P:trigeminal ganglion development; IEA:Ensembl. DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome. 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 GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. 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; IPR027143; Neuropilin-2. DR InterPro; IPR022579; Neuropilin_C. DR InterPro; IPR035914; Sperma_CUB_dom_sf. DR PANTHER; PTHR44185; PTHR44185; 1. DR PANTHER; PTHR44185:SF2; PTHR44185:SF2; 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; PS50060; MAM_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Complete proteome; KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein; KW Heparin-binding; Host-virus interaction; Membrane; Metal-binding; KW Neurogenesis; Polymorphism; Receptor; Reference proteome; Repeat; KW Secreted; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 20 Or 22. {ECO:0000255}. FT CHAIN 21 931 Neuropilin-2. FT /FTId=PRO_0000021863. FT TOPO_DOM 21 864 Extracellular. {ECO:0000255}. FT TRANSMEM 865 889 Helical. {ECO:0000255}. FT TOPO_DOM 890 931 Cytoplasmic. {ECO:0000255}. FT DOMAIN 28 142 CUB 1. {ECO:0000255|PROSITE- FT ProRule:PRU00059}. FT DOMAIN 149 267 CUB 2. {ECO:0000255|PROSITE- FT ProRule:PRU00059}. FT DOMAIN 277 427 F5/8 type C 1. {ECO:0000255|PROSITE- FT ProRule:PRU00081}. FT DOMAIN 434 592 F5/8 type C 2. {ECO:0000255|PROSITE- FT ProRule:PRU00081}. FT DOMAIN 642 802 MAM. {ECO:0000255|PROSITE- FT ProRule:PRU00128}. FT COMPBIAS 671 674 Poly-Ser. FT METAL 197 197 Calcium. {ECO:0000244|PDB:2QQO, FT ECO:0000269|PubMed:17989695}. FT METAL 211 211 Calcium. {ECO:0000244|PDB:2QQO, FT ECO:0000269|PubMed:17989695}. FT METAL 252 252 Calcium. {ECO:0000244|PDB:2QQO, FT ECO:0000269|PubMed:17989695}. FT CARBOHYD 152 152 N-linked (GlcNAc...) asparagine. FT {ECO:0000244|PDB:2QQK, FT ECO:0000269|PubMed:17989695}. FT CARBOHYD 157 157 N-linked (GlcNAc...) asparagine. FT {ECO:0000244|PDB:2QQK, FT ECO:0000269|PubMed:17989695}. FT CARBOHYD 629 629 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 839 839 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 28 55 {ECO:0000269|PubMed:17989695}. FT DISULFID 83 105 {ECO:0000269|PubMed:17989695}. FT DISULFID 149 175 {ECO:0000269|PubMed:17989695}. FT DISULFID 208 230 {ECO:0000269|PubMed:17989695}. FT DISULFID 277 427 {ECO:0000269|PubMed:17989695}. FT DISULFID 434 592 {ECO:0000269|PubMed:17989695}. FT VAR_SEQ 548 555 LFEGNMHY -> VGCSWRPL (in isoform s9). FT {ECO:0000303|PubMed:11112349}. FT /FTId=VSP_044908. FT VAR_SEQ 556 931 Missing (in isoform s9). FT {ECO:0000303|PubMed:11112349}. FT /FTId=VSP_044909. FT VAR_SEQ 809 830 Missing (in isoform A0). FT {ECO:0000303|PubMed:9331348}. FT /FTId=VSP_004342. FT VAR_SEQ 809 813 Missing (in isoform A17 and isoform B0). FT {ECO:0000303|PubMed:11112349, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9331348}. FT /FTId=VSP_004341. FT VAR_SEQ 814 931 VDIPEIHEREGYEDEIDDEYEVDWSNSSSATSGSGAPSTDK FT EKSWLYTLDPILITIIAMSSLGVLLGATCAGLLLYCTCSYS FT GLSSRSCTTLENYNFELYDGLKHKVKMNHQKCCSEA -> G FT GTLLPGTEPTVDTVPMQPIPAYWYYVMAAGGAVLVLVSVAL FT ALVLHYHRFRYAAKKTDHSITYKTSHYTNGAPLAVEPTLTI FT KLEQDRGSHC (in isoform B0 and isoform FT B5). {ECO:0000303|PubMed:11112349, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_041160. FT VARIANT 123 123 K -> R (in dbSNP:rs849541). FT {ECO:0000269|PubMed:15815621}. FT /FTId=VAR_047754. FT VARIANT 334 334 R -> C (rare variant; may act as a FT phenotype modifier in EIEE13 patients FT carrying SCN8A mutations; FT dbSNP:rs114144673). FT {ECO:0000269|PubMed:22365152}. FT /FTId=VAR_067537. FT VARIANT 428 428 R -> W (rare variant; may act as a FT phenotype modifier in EIEE13 patients FT carrying SCN8A mutations; FT dbSNP:rs139711818). FT {ECO:0000269|PubMed:22365152}. FT /FTId=VAR_067538. FT VARIANT 602 602 E -> K (in dbSNP:rs1128169). FT {ECO:0000269|PubMed:11112349, FT ECO:0000269|PubMed:9331348}. FT /FTId=VAR_065167. FT STRAND 30 33 {ECO:0000244|PDB:6GH8}. FT STRAND 38 41 {ECO:0000244|PDB:6GH8}. FT TURN 43 46 {ECO:0000244|PDB:6GH8}. FT STRAND 54 60 {ECO:0000244|PDB:6GH8}. FT STRAND 68 72 {ECO:0000244|PDB:6GH8}. FT STRAND 84 95 {ECO:0000244|PDB:6GH8}. FT STRAND 98 104 {ECO:0000244|PDB:6GH8}. FT STRAND 106 108 {ECO:0000244|PDB:6GH8}. FT STRAND 116 125 {ECO:0000244|PDB:6GH8}. FT STRAND 136 141 {ECO:0000244|PDB:6GH8}. FT STRAND 151 153 {ECO:0000244|PDB:2QQO}. FT STRAND 155 161 {ECO:0000244|PDB:2QQO}. FT TURN 163 166 {ECO:0000244|PDB:2QQO}. FT STRAND 174 180 {ECO:0000244|PDB:2QQO}. FT STRAND 186 195 {ECO:0000244|PDB:2QQO}. FT STRAND 210 219 {ECO:0000244|PDB:2QQO}. FT TURN 220 222 {ECO:0000244|PDB:2QQO}. FT STRAND 225 229 {ECO:0000244|PDB:2QQO}. FT STRAND 231 233 {ECO:0000244|PDB:2QQK}. FT STRAND 238 240 {ECO:0000244|PDB:2QQO}. FT STRAND 242 250 {ECO:0000244|PDB:2QQO}. FT STRAND 255 257 {ECO:0000244|PDB:2QQL}. FT STRAND 259 267 {ECO:0000244|PDB:2QQO}. FT TURN 283 285 {ECO:0000244|PDB:5DQ0}. FT STRAND 286 288 {ECO:0000244|PDB:4QDR}. FT HELIX 290 292 {ECO:0000244|PDB:5DQ0}. FT STRAND 293 296 {ECO:0000244|PDB:5DQ0}. FT STRAND 302 304 {ECO:0000244|PDB:5DQ0}. FT HELIX 306 308 {ECO:0000244|PDB:5DQ0}. FT STRAND 324 326 {ECO:0000244|PDB:2QQL}. FT STRAND 329 345 {ECO:0000244|PDB:5DQ0}. FT TURN 350 352 {ECO:0000244|PDB:5DQ0}. FT STRAND 355 371 {ECO:0000244|PDB:5DQ0}. FT STRAND 376 381 {ECO:0000244|PDB:2QQL}. FT STRAND 388 391 {ECO:0000244|PDB:5DQ0}. FT STRAND 394 417 {ECO:0000244|PDB:5DQ0}. FT STRAND 420 428 {ECO:0000244|PDB:5DQ0}. FT HELIX 429 431 {ECO:0000244|PDB:2QQJ}. FT STRAND 432 434 {ECO:0000244|PDB:4QDQ}. FT TURN 440 442 {ECO:0000244|PDB:2QQJ}. FT STRAND 443 445 {ECO:0000244|PDB:2QQK}. FT HELIX 447 449 {ECO:0000244|PDB:2QQJ}. FT STRAND 450 453 {ECO:0000244|PDB:2QQJ}. FT STRAND 456 459 {ECO:0000244|PDB:4QDQ}. FT HELIX 462 465 {ECO:0000244|PDB:2QQJ}. FT TURN 467 469 {ECO:0000244|PDB:2QQJ}. FT STRAND 470 472 {ECO:0000244|PDB:2QQL}. FT STRAND 477 480 {ECO:0000244|PDB:2QQJ}. FT TURN 483 485 {ECO:0000244|PDB:2QQJ}. FT STRAND 488 504 {ECO:0000244|PDB:2QQJ}. FT HELIX 515 517 {ECO:0000244|PDB:2QQO}. FT STRAND 521 534 {ECO:0000244|PDB:2QQJ}. FT TURN 541 544 {ECO:0000244|PDB:2QQJ}. FT STRAND 553 557 {ECO:0000244|PDB:2QQJ}. FT STRAND 559 578 {ECO:0000244|PDB:2QQJ}. FT STRAND 585 593 {ECO:0000244|PDB:2QQJ}. SQ SEQUENCE 931 AA; 104831 MW; 270CBAE69A0A797C CRC64; MDMFPLTWVF LALYFSRHQV RGQPDPPCGG RLNSKDAGYI TSPGYPQDYP SHQNCEWIVY APEPNQKIVL NFNPHFEIEK HDCKYDFIEI RDGDSESADL LGKHCGNIAP PTIISSGSML YIKFTSDYAR QGAGFSLRYE IFKTGSEDCS KNFTSPNGTI ESPGFPEKYP HNLDCTFTIL AKPKMEIILQ FLIFDLEHDP LQVGEGDCKY DWLDIWDGIP HVGPLIGKYC GTKTPSELRS STGILSLTFH TDMAVAKDGF SARYYLVHQE PLENFQCNVP LGMESGRIAN EQISASSTYS DGRWTPQQSR LHGDDNGWTP NLDSNKEYLQ VDLRFLTMLT AIATQGAISR ETQNGYYVKS YKLEVSTNGE DWMVYRHGKN HKVFQANNDA TEVVLNKLHA PLLTRFVRIR PQTWHSGIAL RLELFGCRVT DAPCSNMLGM LSGLIADSQI SASSTQEYLW SPSAARLVSS RSGWFPRIPQ AQPGEEWLQV DLGTPKTVKG VIIQGARGGD SITAVEARAF VRKFKVSYSL NGKDWEYIQD PRTQQPKLFE GNMHYDTPDI RRFDPIPAQY VRVYPERWSP AGIGMRLEVL GCDWTDSKPT VETLGPTVKS EETTTPYPTE EEATECGENC SFEDDKDLQL PSGFNCNFDF LEEPCGWMYD HAKWLRTTWA SSSSPNDRTF PDDRNFLRLQ SDSQREGQYA RLISPPVHLP RSPVCMEFQY QATGGRGVAL QVVREASQES KLLWVIREDQ GGEWKHGRII LPSYDMEYQI VFEGVIGKGR SGEIAIDDIR ISTDVPLENC MEPISAFAGE NFKVDIPEIH EREGYEDEID DEYEVDWSNS SSATSGSGAP STDKEKSWLY TLDPILITII AMSSLGVLLG ATCAGLLLYC TCSYSGLSSR SCTTLENYNF ELYDGLKHKV KMNHQKCCSE A //