ID   NRP1_MOUSE              Reviewed;         923 AA.
AC   P97333; Q6PAR3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 213.
DE   RecName: Full=Neuropilin-1;
DE   AltName: Full=A5 protein;
DE   AltName: CD_antigen=CD304;
DE   Flags: Precursor;
GN   Name=Nrp1 {ECO:0000312|MGI:MGI:106206}; Synonyms=Nrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Embryonic brain;
RX   PubMed=8748368;
RX   DOI=10.1002/(sici)1097-4695(199601)29:1<1::aid-neu1>3.0.co;2-f;
RA   Kawakami A., Kitsukawa T., Takagi S., Fujisawa H.;
RT   "Developmentally regulated expression of a cell surface protein,
RT   neuropilin, in the mouse nervous system.";
RL   J. Neurobiol. 29:1-17(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261 AND ASN-522.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-894, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   INTERACTION WITH FER.
RX   PubMed=20133938; DOI=10.1074/jbc.m109.080689;
RA   Jiang S.X., Whitehead S., Aylsworth A., Slinn J., Zurakowski B., Chan K.,
RA   Li J., Hou S.T.;
RT   "Neuropilin 1 directly interacts with Fer kinase to mediate semaphorin 3A-
RT   induced death of cortical neurons.";
RL   J. Biol. Chem. 285:9908-9918(2010).
RN   [7]
RP   FUNCTION.
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., Guergueltcheva V.,
RA   Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
RT   "CMT2D neuropathy is linked to the neomorphic binding activity of glycyl-
RT   tRNA synthetase.";
RL   Nature 526:710-714(2015).
RN   [8]
RP   ERRATUM OF PUBMED:26503042.
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., Guergueltcheva V.,
RA   Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
RT   "Corrigendum: CMT2D neuropathy is linked to the neomorphic binding activity
RT   of glycyl-tRNA synthetase.";
RL   Nature 532:402-402(2016).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=30623799; DOI=10.1016/j.isci.2018.12.005;
RA   Issitt T., Bosseboeuf E., De Winter N., Dufton N., Gestri G., Senatore V.,
RA   Chikh A., Randi A.M., Raimondi C.;
RT   "Neuropilin-1 Controls Endothelial Homeostasis by Regulating Mitochondrial
RT   Function and Iron-Dependent Oxidative Stress.";
RL   IScience 11:205-223(2019).
CC   -!- FUNCTION: Receptor involved in the development of the cardiovascular
CC       system, in angiogenesis, in the formation of certain neuronal circuits
CC       and in organogenesis outside the nervous system (By similarity).
CC       Mediates the chemorepulsant activity of semaphorins (PubMed:26503042).
CC       Recognizes a C-end rule (CendR) motif R/KXXR/K on its ligands which
CC       causes cellular internalization and vascular leakage (By similarity).
CC       Binds to semaphorin 3A (SEMA3A), the PLGF-2 isoform of PGF, the VEGF165
CC       isoform of VEGFA and VEGFB (By similarity). Coexpression with KDR
CC       results in increased VEGF165 binding to KDR as well as increased
CC       chemotaxis. Regulates VEGF-induced angiogenesis (By similarity).
CC       Binding to VEGFA initiates a signaling pathway needed for motor neuron
CC       axon guidance and cell body migration, including for the caudal
CC       migration of facial motor neurons from rhombomere 4 to rhombomere 6
CC       during embryonic development (PubMed:26503042). Regulates mitochondrial
CC       iron transport via interaction with ABCB8/MITOSUR (By similarity).
CC       {ECO:0000250|UniProtKB:O14786, ECO:0000269|PubMed:26503042}.
CC   -!- SUBUNIT: Homodimer, and heterodimer with NRP2 (By similarity). Binds
CC       PLXNB1 (By similarity). Interacts with FER (PubMed:20133938). Interacts
CC       with VEGFA (PubMed:26503042). Interacts with ABCB8/MITOSUR in
CC       mitochondria (By similarity). {ECO:0000250|UniProtKB:O14786,
CC       ECO:0000269|PubMed:20133938, ECO:0000269|PubMed:26503042}.
CC   -!- INTERACTION:
CC       P97333; P70206: Plxna1; NbExp=4; IntAct=EBI-1555129, EBI-771260;
CC       P97333; P70207: Plxna2; NbExp=3; IntAct=EBI-1555129, EBI-771272;
CC       P97333; P34152: Ptk2; NbExp=2; IntAct=EBI-1555129, EBI-77070;
CC       P97333; O08665: Sema3a; NbExp=3; IntAct=EBI-1555129, EBI-8586029;
CC       P97333; P08648: ITGA5; Xeno; NbExp=3; IntAct=EBI-1555129, EBI-1382311;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000250|UniProtKB:O14786}; Single-pass type I membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O14786}; Single-
CC       pass type I membrane protein {ECO:0000255}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O14786}.
CC   -!- TISSUE SPECIFICITY: Nervous system.
CC   -!- DOMAIN: The tandem CUB domains mediate binding to semaphorin, while the
CC       tandem F5/8 domains are responsible for heparin and VEGF binding. F5/8
CC       domains mediate the recognition and binding to R/KXXR/K CendR motifs.
CC       {ECO:0000250|UniProtKB:O14786}.
CC   -!- DISRUPTION PHENOTYPE: Knockout embryos display higher susceptibility to
CC       oxidative stress in endothelium cells located in the intersomitic
CC       vessels. {ECO:0000269|PubMed:30623799}.
CC   -!- SIMILARITY: Belongs to the neuropilin family. {ECO:0000305}.
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DR   EMBL; D50086; BAA08789.1; -; mRNA.
DR   EMBL; CH466525; EDL11828.1; -; Genomic_DNA.
DR   EMBL; BC060129; AAH60129.1; -; mRNA.
DR   CCDS; CCDS22790.1; -.
DR   RefSeq; NP_032763.2; NM_008737.2.
DR   RefSeq; XP_006530829.1; XM_006530766.3.
DR   PDB; 4GZ9; X-ray; 2.70 A; A=22-586.
DR   PDB; 4GZA; X-ray; 7.00 A; H=22-586.
DR   PDB; 7M0R; EM; 3.70 A; E/F=22-588.
DR   PDBsum; 4GZ9; -.
DR   PDBsum; 4GZA; -.
DR   PDBsum; 7M0R; -.
DR   AlphaFoldDB; P97333; -.
DR   EMDB; EMD-23613; -.
DR   SMR; P97333; -.
DR   BioGRID; 201848; 27.
DR   CORUM; P97333; -.
DR   DIP; DIP-39360N; -.
DR   IntAct; P97333; 16.
DR   MINT; P97333; -.
DR   STRING; 10090.ENSMUSP00000026917; -.
DR   GlyConnect; 2556; 1 N-Linked glycan (1 site).
DR   GlyCosmos; P97333; 6 sites, 1 glycan.
DR   GlyGen; P97333; 7 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; P97333; -.
DR   PhosphoSitePlus; P97333; -.
DR   SwissPalm; P97333; -.
DR   CPTAC; non-CPTAC-3597; -.
DR   CPTAC; non-CPTAC-3661; -.
DR   MaxQB; P97333; -.
DR   PaxDb; 10090-ENSMUSP00000026917; -.
DR   PeptideAtlas; P97333; -.
DR   ProteomicsDB; 293739; -.
DR   Pumba; P97333; -.
DR   TopDownProteomics; P97333; -.
DR   ABCD; P97333; 6 sequenced antibodies.
DR   Antibodypedia; 3859; 1077 antibodies from 42 providers.
DR   DNASU; 18186; -.
DR   Ensembl; ENSMUST00000026917.10; ENSMUSP00000026917.9; ENSMUSG00000025810.10.
DR   GeneID; 18186; -.
DR   KEGG; mmu:18186; -.
DR   UCSC; uc009nzr.2; mouse.
DR   AGR; MGI:106206; -.
DR   CTD; 8829; -.
DR   MGI; MGI:106206; Nrp1.
DR   VEuPathDB; HostDB:ENSMUSG00000025810; -.
DR   eggNOG; ENOG502QUEH; Eukaryota.
DR   GeneTree; ENSGT00940000157169; -.
DR   HOGENOM; CLU_015228_6_1_1; -.
DR   InParanoid; P97333; -.
DR   OMA; QEDCTKP; -.
DR   OrthoDB; 5293253at2759; -.
DR   PhylomeDB; P97333; -.
DR   TreeFam; TF316506; -.
DR   Reactome; R-MMU-194306; Neurophilin interactions with VEGF and VEGFR.
DR   Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
DR   Reactome; R-MMU-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR   Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR   Reactome; R-MMU-445144; Signal transduction by L1.
DR   BioGRID-ORCS; 18186; 4 hits in 77 CRISPR screens.
DR   ChiTaRS; Nrp1; mouse.
DR   PRO; PR:P97333; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P97333; Protein.
DR   Bgee; ENSMUSG00000025810; Expressed in internal carotid artery and 273 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IDA:BHF-UCL.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; IDA:BHF-UCL.
DR   GO; GO:0005925; C:focal adhesion; IDA:BHF-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005883; C:neurofilament; IDA:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:ARUK-UCL.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0097443; C:sorting endosome; IDA:BHF-UCL.
DR   GO; GO:0019838; F:growth factor binding; IPI:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
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; IPI:ARUK-UCL.
DR   GO; GO:0017154; F:semaphorin receptor activity; IDA:MGI.
DR   GO; GO:0038085; F:vascular endothelial growth factor binding; IPI:BHF-UCL.
DR   GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IMP:BHF-UCL.
DR   GO; GO:0001525; P:angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0048844; P:artery morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0048675; P:axon extension; IGI:MGI.
DR   GO; GO:0048846; P:axon extension involved in axon guidance; IDA:MGI.
DR   GO; GO:0007411; P:axon guidance; IDA:MGI.
DR   GO; GO:0007413; P:axonal fasciculation; IMP:MGI.
DR   GO; GO:0060385; P:axonogenesis involved in innervation; IMP:BHF-UCL.
DR   GO; GO:0150020; P:basal dendrite arborization; IGI:ARUK-UCL.
DR   GO; GO:0150018; P:basal dendrite development; IMP:ARUK-UCL.
DR   GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:MGI.
DR   GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0060980; P:cell migration involved in coronary vasculogenesis; IC:BHF-UCL.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISO:MGI.
DR   GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL.
DR   GO; GO:0071679; P:commissural neuron axon guidance; IMP:BHF-UCL.
DR   GO; GO:0060982; P:coronary artery morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IMP:MGI.
DR   GO; GO:1904835; P:dorsal root ganglion morphogenesis; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0035767; P:endothelial cell chemotaxis; ISO:MGI.
DR   GO; GO:0043542; P:endothelial cell migration; IMP:BHF-UCL.
DR   GO; GO:0021612; P:facial nerve structural organization; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903375; P:facioacoustic ganglion development; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IMP:BHF-UCL.
DR   GO; GO:0007507; P:heart development; IGI:MGI.
DR   GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0008045; P:motor neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0097475; P:motor neuron migration; IMP:UniProtKB.
DR   GO; GO:0030517; P:negative regulation of axon extension; IGI:MGI.
DR   GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IDA:MGI.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:BHF-UCL.
DR   GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR   GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0048666; P:neuron development; IMP:BHF-UCL.
DR   GO; GO:0001764; P:neuron migration; IMP:BHF-UCL.
DR   GO; GO:0038189; P:neuropilin signaling pathway; IMP:BHF-UCL.
DR   GO; GO:1905040; P:otic placode development; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:MGI.
DR   GO; GO:0050918; P:positive chemotaxis; IMP:BHF-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IMP:BHF-UCL.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP: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; ISO:MGI.
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:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR   GO; GO:0099173; P:postsynapse organization; IDA:SynGO.
DR   GO; GO:1902946; P:protein localization to early endosome; IMP:BHF-UCL.
DR   GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IDA:MGI.
DR   GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IMP:BHF-UCL.
DR   GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0061441; P:renal artery morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0009611; P:response to wounding; IBA:GO_Central.
DR   GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:MGI.
DR   GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; IMP:BHF-UCL.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:BHF-UCL.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; IDA:MGI.
DR   GO; GO:0097374; P:sensory neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0002040; P:sprouting angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISO:MGI.
DR   GO; GO:0061549; P:sympathetic ganglion development; IMP:BHF-UCL.
DR   GO; GO:0048485; P:sympathetic nervous system development; IMP:MGI.
DR   GO; GO:0097490; P:sympathetic neuron projection extension; IMP:BHF-UCL.
DR   GO; GO:0097491; P:sympathetic neuron projection guidance; IMP:BHF-UCL.
DR   GO; GO:0061551; P:trigeminal ganglion development; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0021636; P:trigeminal nerve morphogenesis; IMP:MGI.
DR   GO; GO:0021637; P:trigeminal nerve structural organization; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0001570; P:vasculogenesis; IBA:GO_Central.
DR   GO; GO:0038190; P:VEGF-activated neuropilin signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0036486; P:ventral trunk neural crest cell migration; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0021649; P:vestibulocochlear nerve structural organization; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00057; FA58C; 2.
DR   CDD; cd06263; MAM; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 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; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46806:SF4; NEUROPILIN-1; 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; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
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.
DR   Genevisible; P97333; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Angiogenesis; Calcium; Cell membrane; Cytoplasm;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Heparan sulfate; Heparin-binding; Membrane; Metal-binding; Mitochondrion;
KW   Neurogenesis; Phosphoprotein; Proteoglycan; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..923
FT                   /note="Neuropilin-1"
FT                   /id="PRO_0000021860"
FT   TOPO_DOM        22..856
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        857..879
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        880..923
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..141
FT                   /note="CUB 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          147..265
FT                   /note="CUB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          275..424
FT                   /note="F5/8 type C 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DOMAIN          431..583
FT                   /note="F5/8 type C 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DOMAIN          645..811
FT                   /note="MAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT   REGION          820..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         195
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   BINDING         209
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   BINDING         250
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   MOD_RES         894
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        612
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine;
FT                   alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   CARBOHYD        612
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine;
FT                   alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   CARBOHYD        829
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   CARBOHYD        842
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..54
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   DISULFID        82..104
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   DISULFID        147..173
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   DISULFID        206..228
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   DISULFID        275..424
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   DISULFID        431..583
FT                   /evidence="ECO:0000250|UniProtKB:O14786"
FT   CONFLICT        68
FT                   /note="M -> I (in Ref. 1; BAA08789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="S -> C (in Ref. 1; BAA08789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        601
FT                   /note="D -> H (in Ref. 1; BAA08789)"
FT                   /evidence="ECO:0000305"
FT   STRAND          27..32
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   TURN            42..46
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          53..59
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   HELIX           80..82
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          84..94
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          97..103
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          115..124
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          146..151
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          153..159
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   TURN            161..164
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          172..178
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          185..193
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          208..217
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   TURN            218..220
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          223..227
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          240..248
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          257..264
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   TURN            281..283
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          284..286
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   HELIX           288..290
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          291..294
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   HELIX           299..301
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   HELIX           303..305
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          326..342
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   TURN            347..349
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          352..368
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          373..378
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          385..389
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          391..414
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          417..424
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   HELIX           426..428
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          429..431
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   TURN            437..439
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          440..442
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   HELIX           444..446
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          447..449
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   TURN            450..453
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   HELIX           459..462
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   TURN            464..466
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          471..473
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          485..501
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          503..507
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          512..525
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          534..537
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          544..547
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          550..570
FT                   /evidence="ECO:0007829|PDB:4GZ9"
FT   STRAND          573..583
FT                   /evidence="ECO:0007829|PDB:4GZ9"
SQ   SEQUENCE   923 AA;  103000 MW;  23209818C5C42137 CRC64;
     MERGLPLLCA TLALALALAG AFRSDKCGGT IKIENPGYLT SPGYPHSYHP SEKCEWLIQA
     PEPYQRIMIN FNPHFDLEDR DCKYDYVEVI DGENEGGRLW GKFCGKIAPS PVVSSGPFLF
     IKFVSDYETH GAGFSIRYEI FKRGPECSQN YTAPTGVIKS PGFPEKYPNS LECTYIIFAP
     KMSEIILEFE SFDLEQDSNP PGGMFCRYDR LEIWDGFPEV GPHIGRYCGQ KTPGRIRSSS
     GVLSMVFYTD SAIAKEGFSA NYSVLQSSIS EDFKCMEALG MESGEIHSDQ ITASSQYGTN
     WSVERSRLNY PENGWTPGED SYKEWIQVDL GLLRFVTAVG TQGAISKETK KKYYVKTYRV
     DISSNGEDWI SLKEGNKAII FQGNTNPTDV VLGVFSKPLI TRFVRIKPVS WETGISMRFE
     VYGCKITDYP CSGMLGMVSG LISDSQITAS NQADRNWMPE NIRLVTSRTG WALPPSPHPY
     TNEWLQVDLG DEKIVRGVII QGGKHRENKV FMRKFKIAYS NNGSDWKTIM DDSKRKAKSF
     EGNNNYDTPE LRTFSPLSTR FIRIYPERAT HSGLGLRMEL LGCEVEAPTA GPTTPNGNPV
     DECDDDQANC HSGTGDDFQL TGGTTVLATE KPTIIDSTIQ SEFPTYGFNC EFGWGSHKTF
     CHWEHDSHAQ LRWSVLTSKT GPIQDHTGDG NFIYSQADEN QKGKVARLVS PVVYSQSSAH
     CMTFWYHMSG SHVGTLRVKL RYQKPEEYDQ LVWMVVGHQG DHWKEGRVLL HKSLKLYQVI
     FEGEIGKGNL GGIAVDDISI NNHISQEDCA KPTDLDKKNT EIKIDETGST PGYEGEGEGD
     KNISRKPGNV LKTLDPILIT IIAMSALGVL LGAVCGVVLY CACWHNGMSE RNLSALENYN
     FELVDGVKLK KDKLNPQSNY SEA
//