LOCUS       NP_032763                923 aa            linear   ROD 16-OCT-2024
DEFINITION  neuropilin-1 isoform 1 precursor [Mus musculus].
ACCESSION   NP_032763
VERSION     NP_032763.2
DBSOURCE    REFSEQ: accession NM_008737.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   Grebinoski,S., Pieklo,G., Zhang,Q., Visperas,A., Cui,J., Goulet,J.,
            Xiao,H., Brunazzi,E.A., Cardello,C., Herrada,A.A., Das,J.,
            Workman,C.J. and Vignali,D.A.A.
  TITLE     Regulatory T Cell Insufficiency in Autoimmune Diabetes Is Driven by
            Selective Loss of Neuropilin-1 on Intraislet Regulatory T Cells
  JOURNAL   J Immunol 213 (6), 779-794 (2024)
   PUBMED   39109924
  REMARK    GeneRIF: Regulatory T Cell Insufficiency in Autoimmune Diabetes Is
            Driven by Selective Loss of Neuropilin-1 on Intraislet Regulatory T
            Cells.
REFERENCE   2  (residues 1 to 923)
  AUTHORS   Barao,S., Xu,Y., Llongueras,J.P., Vistein,R., Goff,L.,
            Nielsen,K.J., Bae,B.I., Smith,R.S., Walsh,C.A., Stein-O'Brien,G.
            and Muller,U.
  TITLE     Conserved transcriptional regulation by BRN1 and BRN2 in
            neocortical progenitors drives mammalian neural specification and
            neocortical expansion
  JOURNAL   Nat Commun 15 (1), 8043 (2024)
   PUBMED   39271675
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 923)
  AUTHORS   Erickson,A.G., Motta,A., Kastriti,M.E., Edwards,S., Coulpier,F.,
            Theoulle,E., Murtazina,A., Poverennaya,I., Wies,D., Ganofsky,J.,
            Canu,G., Lallemend,F., Topilko,P., Hadjab,S., Fried,K.,
            Ruhrberg,C., Schwarz,Q., Castellani,V., Bonanomi,D. and Adameyko,I.
  TITLE     Motor innervation directs the correct development of the mouse
            sympathetic nervous system
  JOURNAL   Nat Commun 15 (1), 7065 (2024)
   PUBMED   39152112
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 923)
  AUTHORS   Bessa,P., Newman,A.G., Yan,K., Schaub,T., Dannenberg,R., Lajko,D.,
            Eilenberger,J., Brunet,T., Textoris-Taube,K., Kemmler,E., Deng,P.,
            Banerjee,P., Ravindran,E., Preissner,R., Rosario,M. and
            Tarabykin,V.
  TITLE     Semaphorin heterodimerization in cis regulates membrane targeting
            and neocortical wiring
  JOURNAL   Nat Commun 15 (1), 7059 (2024)
   PUBMED   39152101
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 923)
  AUTHORS   Li,Y., Wang,Z., Xu,H., Hong,Y., Shi,M., Hu,B., Wang,X., Ma,S.,
            Wang,M., Cao,C., Zhu,H., Hu,D., Xu,C., Lin,Y., Xu,G., Yao,Y. and
            Zeng,R.
  TITLE     Targeting the transmembrane cytokine co-receptor neuropilin-1 in
            distal tubules improves renal injury and fibrosis
  JOURNAL   Nat Commun 15 (1), 5731 (2024)
   PUBMED   38977708
  REMARK    GeneRIF: Targeting the transmembrane cytokine co-receptor
            neuropilin-1 in distal tubules improves renal injury and fibrosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 923)
  AUTHORS   Kitsukawa,T., Shimizu,M., Sanbo,M., Hirata,T., Taniguchi,M.,
            Bekku,Y., Yagi,T. and Fujisawa,H.
  TITLE     Neuropilin-semaphorin III/D-mediated chemorepulsive signals play a
            crucial role in peripheral nerve projection in mice
  JOURNAL   Neuron 19 (5), 995-1005 (1997)
   PUBMED   9390514
REFERENCE   7  (residues 1 to 923)
  AUTHORS   Chen,H., Chedotal,A., He,Z., Goodman,C.S. and Tessier-Lavigne,M.
  TITLE     Neuropilin-2, a novel member of the neuropilin family, is a high
            affinity receptor for the semaphorins Sema E and Sema IV but not
            Sema III
  JOURNAL   Neuron 19 (3), 547-559 (1997)
   PUBMED   9331348
  REMARK    Erratum:[Neuron 1997 Sep;19(3):559]
REFERENCE   8  (residues 1 to 923)
  AUTHORS   He,Z. and Tessier-Lavigne,M.
  TITLE     Neuropilin is a receptor for the axonal chemorepellent Semaphorin
            III
  JOURNAL   Cell 90 (4), 739-751 (1997)
   PUBMED   9288753
REFERENCE   9  (residues 1 to 923)
  AUTHORS   Kawakami,A., Kitsukawa,T., Takagi,S. and Fujisawa,H.
  TITLE     Developmentally regulated expression of a cell surface protein,
            neuropilin, in the mouse nervous system
  JOURNAL   J Neurobiol 29 (1), 1-17 (1996)
   PUBMED   8748368
REFERENCE   10 (residues 1 to 923)
  AUTHORS   Kitsukawa,T., Shimono,A., Kawakami,A., Kondoh,H. and Fujisawa,H.
  TITLE     Overexpression of a membrane protein, neuropilin, in chimeric mice
            causes anomalies in the cardiovascular system, nervous system and
            limbs
  JOURNAL   Development 121 (12), 4309-4318 (1995)
   PUBMED   8575331
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC139349.4 and AC102856.5.
            
            On Jul 2, 2009 this sequence version replaced NP_032763.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060129.1, D50086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 75.78 cM"
     Protein         1..923
                     /product="neuropilin-1 isoform 1 precursor"
                     /note="transmembrane receptor; A5 protein; Neuropilin-1
                     precursor (A5 protein)"
                     /calculated_mol_wt=100950
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2069
     mat_peptide     22..923
                     /product="Neuropilin-1. /id=PRO_0000021860"
                     /note="propagated from UniProtKB/Swiss-Prot (P97333.2)"
                     /calculated_mol_wt=100950
     Region          27..140
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(36,38,40,68,74,111,135,137,139..140)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          147..264
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            150
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97333.2)"
     Site            order(157,159,186,191,235,259,261,263..264)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Site            261
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19656770; propagated from
                     UniProtKB/Swiss-Prot (P97333.2)"
     Region          277..423
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            300
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97333.2)"
     Site            order(316,344,353)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Region          435..582
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            522
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19656770; propagated from
                     UniProtKB/Swiss-Prot (P97333.2)"
     Site            612
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine,
                     alternate. /evidence=ECO:0000250|UniProtKB:O14786;
                     O-linked (Xyl...) (heparan sulfate) serine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O14786; propagated from
                     UniProtKB/Swiss-Prot (P97333.2)"
     Region          650..810
                     /region_name="MAM"
                     /note="MAM domain, meprin/A5/mu; pfam00629"
                     /db_xref="CDD:459878"
     Region          820..845
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97333.2)"
     Site            829
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:O14786; propagated from
                     UniProtKB/Swiss-Prot (P97333.2)"
     Site            842
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97333.2)"
     Region          845..923
                     /region_name="DUF3481"
                     /note="C-terminal domain of neuropilin glycoprotein;
                     pfam11980"
                     /db_xref="CDD:403259"
     Site            857..879
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97333.2)"
     Site            894
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P97333.2)"
     CDS             1..923
                     /gene="Nrp1"
                     /gene_synonym="C530029I03; NP-1; NPN-1; Npn1; Nrp"
                     /coded_by="NM_008737.3:489..3260"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS22790.1"
                     /db_xref="GeneID:18186"
                     /db_xref="MGI:MGI:106206"
ORIGIN      
        1 merglpllca tlalalalag afrsdkcggt ikienpgylt spgyphsyhp sekcewliqa
       61 pepyqrimin fnphfdledr dckydyvevi dgeneggrlw gkfcgkiaps pvvssgpflf
      121 ikfvsdyeth gagfsiryei fkrgpecsqn ytaptgviks pgfpekypns lectyiifap
      181 kmseiilefe sfdleqdsnp pggmfcrydr leiwdgfpev gphigrycgq ktpgrirsss
      241 gvlsmvfytd saiakegfsa nysvlqssis edfkcmealg mesgeihsdq itassqygtn
      301 wsversrlny pengwtpged sykewiqvdl gllrfvtavg tqgaisketk kkyyvktyrv
      361 dissngedwi slkegnkaii fqgntnptdv vlgvfskpli trfvrikpvs wetgismrfe
      421 vygckitdyp csgmlgmvsg lisdsqitas nqadrnwmpe nirlvtsrtg walppsphpy
      481 tnewlqvdlg dekivrgvii qggkhrenkv fmrkfkiays nngsdwktim ddskrkaksf
      541 egnnnydtpe lrtfsplstr firiyperat hsglglrmel lgceveapta gpttpngnpv
      601 decdddqanc hsgtgddfql tggttvlate kptiidstiq sefptygfnc efgwgshktf
      661 chwehdshaq lrwsvltskt gpiqdhtgdg nfiysqaden qkgkvarlvs pvvysqssah
      721 cmtfwyhmsg shvgtlrvkl ryqkpeeydq lvwmvvghqg dhwkegrvll hkslklyqvi
      781 fegeigkgnl ggiavddisi nnhisqedca kptdldkknt eikidetgst pgyegegegd
      841 knisrkpgnv lktldpilit iiamsalgvl lgavcgvvly cacwhngmse rnlsalenyn
      901 felvdgvklk kdklnpqsny sea
//
