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, Pancreas,
RC 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 Genevisible; P97333; MM.
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.
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
//
