NRP2_HUMAN
ID NRP2_HUMAN Reviewed; 931 AA.
AC O60462; A0A024R3W6; A0A024R412; E9PF66; O14820; O14821; Q53TQ4; Q53TS3;
AC Q7LBX6; Q7LBX7; Q9H2D4; Q9H2D5; Q9H2E2; Q9H2E3; Q9H2E4; X5D2Q8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 199.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 affinity
RT receptor for the semaphorins Sema E and Sema IV but not Sema 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 isoform-
RT 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), VARIANT
RP 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 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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Tessier-Lavigne M.,
RA Comoglio P.M.;
RT "Plexins are a large family of receptors for transmembrane, secreted and
RT GPI-anchored semaphorins in vertebrates.";
RL Cell 99:71-80(1999).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN CYTOMEGALOVIRUS
RP PROTEIN GL; UL128; UL130 AND UL131A (MICROBIAL INFECTION).
RX PubMed=30057110; DOI=10.1016/j.cell.2018.06.028;
RA Martinez-Martin N., Marcandalli J., Huang C.S., Arthur C.P., Perotti M.,
RA Foglierini M., Ho H., Dosey A.M., Shriver S., Payandeh J., Leitner A.,
RA Lanzavecchia A., Perez L., Ciferri C.;
RT "An Unbiased Screen for Human Cytomegalovirus Identifies Neuropilin-2 as a
RT 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 WITH
RP 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., Bagri A.,
RA Tessier-Lavigne M., Koch A.W., Wu Y., Watts R.J., Wiesmann C.;
RT "Structural studies of neuropilin/antibody complexes provide insights into
RT 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 sequencing of
RT a family quartet affected by infantile epileptic encephalopathy and
RT SUDEP.";
RL Am. J. Hum. Genet. 90:502-510(2012).
CC -!- FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165 and
CC 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 endothelial
CC cells. {ECO:0000269|PubMed:30057110}.
CC -!- SUBUNIT: Heterodimer with NRP1. Binds PLXNB1.
CC {ECO:0000269|PubMed:17989695}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC proteins gL, UL128, UL130 and UL131A. {ECO:0000269|PubMed:30057110}.
CC -!- INTERACTION:
CC O60462; P97953-1: Vegfc; Xeno; NbExp=3; IntAct=EBI-12586256, EBI-16148671;
CC O60462-6; O60462-6: NRP2; NbExp=4; IntAct=EBI-16148700, EBI-16148700;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11112349}; Single-
CC 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, while the
CC tandem F5/8 domains are responsible for heparin and VEGF binding.
CC -!- SIMILARITY: Belongs to the neuropilin family. {ECO:0000305}.
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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 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 PDB; 6TDB; X-ray; 2.45 A; A/B/C/D=275-430.
DR PDB; 6TJT; X-ray; 1.31 A; A/B=275-430.
DR PDB; 7M22; EM; 3.65 A; N=23-595.
DR PDB; 7T4S; EM; 3.10 A; F=1-864.
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 PDBsum; 6TDB; -.
DR PDBsum; 6TJT; -.
DR PDBsum; 7M22; -.
DR PDBsum; 7T4S; -.
DR AlphaFoldDB; O60462; -.
DR SMR; O60462; -.
DR BioGRID; 114355; 44.
DR CORUM; O60462; -.
DR DIP; DIP-5745N; -.
DR IntAct; O60462; 19.
DR STRING; 9606.ENSP00000353582; -.
DR ChEMBL; CHEMBL4295667; -.
DR DrugBank; DB16453; ATYR1923.
DR GlyGen; O60462; 4 sites.
DR iPTMnet; O60462; -.
DR PhosphoSitePlus; O60462; -.
DR SwissPalm; O60462; -.
DR BioMuta; NRP2; -.
DR EPD; O60462; -.
DR jPOST; O60462; -.
DR MassIVE; O60462; -.
DR PaxDb; O60462; -.
DR PeptideAtlas; O60462; -.
DR PRIDE; O60462; -.
DR ProteomicsDB; 20039; -.
DR ProteomicsDB; 49409; -. [O60462-1]
DR ProteomicsDB; 49410; -. [O60462-2]
DR ProteomicsDB; 49411; -. [O60462-3]
DR ProteomicsDB; 49412; -. [O60462-4]
DR ProteomicsDB; 49413; -. [O60462-5]
DR ABCD; O60462; 8 sequenced antibodies.
DR Antibodypedia; 34173; 448 antibodies from 35 providers.
DR DNASU; 8828; -.
DR Ensembl; ENST00000272849.7; ENSP00000272849.3; ENSG00000118257.17. [O60462-5]
DR Ensembl; ENST00000357118.8; ENSP00000349632.4; ENSG00000118257.17. [O60462-4]
DR Ensembl; ENST00000357785.10; ENSP00000350432.5; ENSG00000118257.17. [O60462-3]
DR Ensembl; ENST00000360409.7; ENSP00000353582.3; ENSG00000118257.17. [O60462-1]
DR Ensembl; ENST00000412873.2; ENSP00000407626.2; ENSG00000118257.17. [O60462-2]
DR Ensembl; ENST00000417189.5; ENSP00000387519.1; ENSG00000118257.17. [O60462-6]
DR GeneID; 8828; -.
DR KEGG; hsa:8828; -.
DR MANE-Select; ENST00000357785.10; ENSP00000350432.5; NM_003872.3; NP_003863.2. [O60462-3]
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 GeneCards; NRP2; -.
DR HGNC; HGNC:8005; NRP2.
DR HPA; ENSG00000118257; Low tissue specificity.
DR MIM; 602070; gene.
DR neXtProt; NX_O60462; -.
DR OpenTargets; ENSG00000118257; -.
DR PharmGKB; PA31784; -.
DR VEuPathDB; HostDB:ENSG00000118257; -.
DR eggNOG; ENOG502QVB7; Eukaryota.
DR GeneTree; ENSGT00940000155270; -.
DR HOGENOM; CLU_015228_6_1_1; -.
DR InParanoid; O60462; -.
DR OMA; XYDFIEI; -.
DR PhylomeDB; O60462; -.
DR TreeFam; TF316506; -.
DR PathwayCommons; O60462; -.
DR Reactome; R-HSA-194306; Neurophilin interactions with VEGF and VEGFR.
DR Reactome; R-HSA-447038; NrCAM interactions.
DR SignaLink; O60462; -.
DR SIGNOR; O60462; -.
DR BioGRID-ORCS; 8828; 12 hits in 1066 CRISPR screens.
DR ChiTaRS; NRP2; human.
DR EvolutionaryTrace; O60462; -.
DR GeneWiki; NRP2; -.
DR GenomeRNAi; 8828; -.
DR Pharos; O60462; Tbio.
DR PRO; PR:O60462; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O60462; protein.
DR Bgee; ENSG00000118257; Expressed in sural nerve and 159 other tissues.
DR ExpressionAtlas; O60462; baseline and differential.
DR Genevisible; O60462; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005021; F:vascular endothelial growth factor 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; IBA:GO_Central.
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: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; 2.60.120.290; -; 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; PTHR46806:SF2; PTHR46806: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; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Heparin-binding;
KW Host-virus interaction; Membrane; Metal-binding; Neurogenesis; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /note="Or 22"
FT /evidence="ECO:0000255"
FT CHAIN 21..931
FT /note="Neuropilin-2"
FT /id="PRO_0000021863"
FT TOPO_DOM 21..864
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 865..889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..142
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 149..267
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 277..427
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 434..592
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 642..802
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 298..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17989695,
FT ECO:0007744|PDB:2QQO"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17989695,
FT ECO:0007744|PDB:2QQO"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17989695,
FT ECO:0007744|PDB:2QQO"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17989695,
FT ECO:0007744|PDB:2QQK"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17989695,
FT ECO:0007744|PDB:2QQK"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..55
FT /evidence="ECO:0000269|PubMed:17989695"
FT DISULFID 83..105
FT /evidence="ECO:0000269|PubMed:17989695"
FT DISULFID 149..175
FT /evidence="ECO:0000269|PubMed:17989695"
FT DISULFID 208..230
FT /evidence="ECO:0000269|PubMed:17989695"
FT DISULFID 277..427
FT /evidence="ECO:0000269|PubMed:17989695"
FT DISULFID 434..592
FT /evidence="ECO:0000269|PubMed:17989695"
FT VAR_SEQ 548..555
FT /note="LFEGNMHY -> VGCSWRPL (in isoform s9)"
FT /evidence="ECO:0000303|PubMed:11112349"
FT /id="VSP_044908"
FT VAR_SEQ 556..931
FT /note="Missing (in isoform s9)"
FT /evidence="ECO:0000303|PubMed:11112349"
FT /id="VSP_044909"
FT VAR_SEQ 809..830
FT /note="Missing (in isoform A0)"
FT /evidence="ECO:0000303|PubMed:9331348"
FT /id="VSP_004342"
FT VAR_SEQ 809..813
FT /note="Missing (in isoform A17 and isoform B0)"
FT /evidence="ECO:0000303|PubMed:11112349,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9331348"
FT /id="VSP_004341"
FT VAR_SEQ 814..931
FT /note="VDIPEIHEREGYEDEIDDEYEVDWSNSSSATSGSGAPSTDKEKSWLYTLDPI
FT LITIIAMSSLGVLLGATCAGLLLYCTCSYSGLSSRSCTTLENYNFELYDGLKHKVKMNH
FT QKCCSEA -> GGTLLPGTEPTVDTVPMQPIPAYWYYVMAAGGAVLVLVSVALALVLHY
FT HRFRYAAKKTDHSITYKTSHYTNGAPLAVEPTLTIKLEQDRGSHC (in isoform
FT B0 and isoform B5)"
FT /evidence="ECO:0000303|PubMed:11112349,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_041160"
FT VARIANT 123
FT /note="K -> R (in dbSNP:rs849541)"
FT /evidence="ECO:0000269|PubMed:15815621"
FT /id="VAR_047754"
FT VARIANT 334
FT /note="R -> C (rare variant; may act as a phenotype
FT modifier in EIEE13 patients carrying SCN8A mutations;
FT dbSNP:rs114144673)"
FT /evidence="ECO:0000269|PubMed:22365152"
FT /id="VAR_067537"
FT VARIANT 428
FT /note="R -> W (rare variant; may act as a phenotype
FT modifier in EIEE13 patients carrying SCN8A mutations;
FT dbSNP:rs139711818)"
FT /evidence="ECO:0000269|PubMed:22365152"
FT /id="VAR_067538"
FT VARIANT 602
FT /note="E -> K (in dbSNP:rs1128169)"
FT /evidence="ECO:0000269|PubMed:11112349,
FT ECO:0000269|PubMed:9331348"
FT /id="VAR_065167"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:6GH8"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6GH8"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:6GH8"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:6GH8"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:6GH8"
FT STRAND 84..95
FT /evidence="ECO:0007829|PDB:6GH8"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:6GH8"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6GH8"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:6GH8"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6GH8"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2QQO"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:2QQO"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:2QQO"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:2QQO"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:2QQO"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:2QQO"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:2QQO"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:2QQO"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2QQK"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:2QQO"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:2QQO"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2QQL"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:2QQO"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:6TJT"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:4QDR"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6TJT"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:6TJT"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:6TJT"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:6TJT"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2QQL"
FT STRAND 329..345
FT /evidence="ECO:0007829|PDB:6TJT"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:6TJT"
FT STRAND 355..371
FT /evidence="ECO:0007829|PDB:6TJT"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6TJT"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:6TJT"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:6TJT"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:6TJT"
FT STRAND 394..417
FT /evidence="ECO:0007829|PDB:6TJT"
FT STRAND 420..428
FT /evidence="ECO:0007829|PDB:6TJT"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:2QQJ"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:4QDQ"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:2QQJ"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:2QQK"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:2QQJ"
FT STRAND 450..453
FT /evidence="ECO:0007829|PDB:2QQJ"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:4QDQ"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:2QQJ"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:2QQJ"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:2QQL"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:2QQJ"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:2QQJ"
FT STRAND 488..504
FT /evidence="ECO:0007829|PDB:2QQJ"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:2QQO"
FT STRAND 521..534
FT /evidence="ECO:0007829|PDB:2QQJ"
FT TURN 541..544
FT /evidence="ECO:0007829|PDB:2QQJ"
FT STRAND 553..557
FT /evidence="ECO:0007829|PDB:2QQJ"
FT STRAND 559..578
FT /evidence="ECO:0007829|PDB:2QQJ"
FT STRAND 585..593
FT /evidence="ECO:0007829|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
