LOCUS       NP_659566                922 aa            linear   ROD 27-APR-2025
DEFINITION  neuropilin-1 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_659566
VERSION     NP_659566.1
DBSOURCE    REFSEQ: accession NM_145098.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Gomez,K., Duran,P., Tonello,R., Allen,H.N., Boinon,L.,
            Calderon-Rivera,A., Loya-Lopez,S., Nelson,T.S., Ran,D., Moutal,A.,
            Bunnett,N.W. and Khanna,R.
  TITLE     Neuropilin-1 is essential for vascular endothelial growth factor
            A-mediated increase of sensory neuron activity and development of
            pain-like behaviors
  JOURNAL   Pain 164 (12), 2696-2710 (2023)
   PUBMED   37366599
  REMARK    GeneRIF: Neuropilin-1 is essential for vascular endothelial growth
            factor A-mediated increase of sensory neuron activity and
            development of pain-like behaviors.
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Zhang,X., Wu,D., Tian,Y., Chen,X., Lan,J., Wei,F., Li,Y., Luo,Y.
            and Sun,X.
  TITLE     Ganoderma lucidum polysaccharides ameliorate
            lipopolysaccharide-induced acute pneumonia via inhibiting
            NRP1-mediated inflammation
  JOURNAL   Pharm Biol 60 (1), 2201-2209 (2022)
   PUBMED   36373992
REFERENCE   3  (residues 1 to 922)
  AUTHORS   Lim,K.H., Yang,S., Kim,S.H. and Joo,J.Y.
  TITLE     Identifying New COVID-19 Receptor Neuropilin-1 in Severe
            Alzheimer's Disease Patients Group Brain Using Genome-Wide
            Association Study Approach
  JOURNAL   Front Genet 12, 741175 (2021)
   PUBMED   34745215
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 922)
  AUTHORS   Wu,C.T., Lidsky,P.V., Xiao,Y., Lee,I.T., Cheng,R., Nakayama,T.,
            Jiang,S., Demeter,J., Bevacqua,R.J., Chang,C.A., Whitener,R.L.,
            Stalder,A.K., Zhu,B., Chen,H., Goltsev,Y., Tzankov,A., Nayak,J.V.,
            Nolan,G.P., Matter,M.S., Andino,R. and Jackson,P.K.
  TITLE     SARS-CoV-2 infects human pancreatic beta cells and elicits beta
            cell impairment
  JOURNAL   Cell Metab 33 (8), 1565-1576 (2021)
   PUBMED   34081912
REFERENCE   5  (residues 1 to 922)
  AUTHORS   Kuai,F., Zhou,L., Zhou,J., Sun,X. and Dong,W.
  TITLE     Long non-coding RNA THRIL inhibits miRNA-24-3p to upregulate
            neuropilin-1 to aggravate cerebral ischemia-reperfusion injury
            through regulating the nuclear factor kappaB p65 signaling
  JOURNAL   Aging (Albany NY) 13 (6), 9071-9084 (2021)
   PUBMED   33675584
  REMARK    GeneRIF: Long non-coding RNA THRIL inhibits miRNA-24-3p to
            upregulate neuropilin-1 to aggravate cerebral ischemia-reperfusion
            injury through regulating the nuclear factor kappaB p65 signaling.
REFERENCE   6  (residues 1 to 922)
  AUTHORS   Halder,J.B., Zhao,X., Soker,S., Paria,B.C., Klagsbrun,M., Das,S.K.
            and Dey,S.K.
  TITLE     Differential expression of VEGF isoforms and VEGF(164)-specific
            receptor neuropilin-1 in the mouse uterus suggests a role for
            VEGF(164) in vascular permeability and angiogenesis during
            implantation
  JOURNAL   Genesis 26 (3), 213-224 (2000)
   PUBMED   10705382
REFERENCE   7  (residues 1 to 922)
  AUTHORS   Chedotal,A., Del Rio,J.A., Ruiz,M., He,Z., Borrell,V., de
            Castro,F., Ezan,F., Goodman,C.S., Tessier-Lavigne,M., Sotelo,C. and
            Soriano,E.
  TITLE     Semaphorins III and IV repel hippocampal axons via two distinct
            receptors
  JOURNAL   Development 125 (21), 4313-4323 (1998)
   PUBMED   9753685
REFERENCE   8  (residues 1 to 922)
  AUTHORS   Soker,S., Takashima,S., Miao,H.Q., Neufeld,G. and Klagsbrun,M.
  TITLE     Neuropilin-1 is expressed by endothelial and tumor cells as an
            isoform-specific receptor for vascular endothelial growth factor
  JOURNAL   Cell 92 (6), 735-745 (1998)
   PUBMED   9529250
REFERENCE   9  (residues 1 to 922)
  AUTHORS   Kolodkin,A.L., Levengood,D.V., Rowe,E.G., Tai,Y.T., Giger,R.J. and
            Ginty,D.D.
  TITLE     Neuropilin is a semaphorin III receptor
  JOURNAL   Cell 90 (4), 753-762 (1997)
   PUBMED   9288754
REFERENCE   10 (residues 1 to 922)
  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
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085689.1.
            
            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 :: BC085689.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN09345330
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..922
                     /product="neuropilin-1 isoform 1 precursor"
                     /note="vascular endothelial cell growth factor 165
                     receptor"
                     /calculated_mol_wt=101032
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2069
     mat_peptide     22..922
                     /product="Neuropilin-1. /id=PRO_0000021861"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWJ9.1)"
                     /calculated_mol_wt=101032
     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 (Q9QWJ9.1)"
     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:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QWJ9.1)"
     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 (Q9QWJ9.1)"
     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            order(478,503,510)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            522
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QWJ9.1)"
     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 (Q9QWJ9.1)"
     Region          650..810
                     /region_name="MAM"
                     /note="MAM domain, meprin/A5/mu; pfam00629"
                     /db_xref="CDD:459878"
     Site            829
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:O14786; propagated from
                     UniProtKB/Swiss-Prot (Q9QWJ9.1)"
     Site            841
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QWJ9.1)"
     Region          844..922
                     /region_name="DUF3481"
                     /note="C-terminal domain of neuropilin glycoprotein;
                     pfam11980"
                     /db_xref="CDD:403259"
     Site            856..880
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWJ9.1)"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97333; propagated from
                     UniProtKB/Swiss-Prot (Q9QWJ9.1)"
     CDS             1..922
                     /gene="Nrp1"
                     /gene_synonym="Nrp"
                     /coded_by="NM_145098.2:541..3309"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:246331"
                     /db_xref="RGD:621588"
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 pggvfcrydr leiwdgfpev gphigrycgq ktpgrirsss
      241 gilsmvfytd saiakegfsa nysvlqssis edfkcmealg mesgeihsdq itassqygtn
      301 wsversrlny pengwtpged syrewiqvdl gllrfvtavg tqgaisketk kkyyvktyrv
      361 dissngedwi tlkegnkaii fqgntnptdv vfgvfpkpli trfvrikpas wetgismrfe
      421 vygckitdyp csgmlgmvsg lisdsqitas nqgdrnwmpe nirlvtsrtg walppsphpy
      481 inewlqvdlg dekivrgvii qggkhrenkv fmrkfkiays nngsdwkmim ddskrkaksf
      541 egnnnydtpe lraftplstr firiyperat hsglglrmel lgcevevpta gpttpngnpv
      601 decdddqanc hsgtgddfql tggttvlate kptiidstiq sefptygfnc efgwgshktf
      661 chwehdshaq lrwrvltskt gpiqdhtgdg nfiysqaden qkgkvarlvs pvvysqssah
      721 cmtfwyhmsg shvgtlrvkl hyqkpeeydq lvwmvvghqg dhwkegrvll hkslklyqvi
      781 fegeigkgnl ggiavddisi nnhipqedca kptdldkknt eikidetgst pgyeegkgdk
      841 nisrkpgnvl ktldpiliti iamsalgvll gavcgvvlyc acwhngmser nlsalenynf
      901 elvdgvklkk dklnpqsnys ea
//
