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GeneName nrp1a
Aliases ENSDARG:ENSDARG00000071865; neuropilin 1a, np-1, nrp1, npn-1A, znrp1, zgc:111785, zgc:136674
Description Neuropilin-1a
GenomicLocation chromosome 24 1172123-1331189 reverse strand
ExternalIDs Entrez:353246; EMBL:BC093101; UniGene:120508; ZFIN:ZDB-GENE-030519-2;
TranscriptID ENSDART:ENSDART00000129276; ENSDART:ENSDART00000130586; ENSDART:ENSDART00000129263; ENSDART:ENSDART00000106639
mRNA NCBI:NM_001040326
GeneDescription Neuropilin is a transmembrane protein, which contains two complement-binding (CUB) domains, two coagulation factor V/VIII homology (CF V/VIII) domains and a MAM domain in its extracellular domain, a single membrane-spanning domain and a short cytoplasmic domain of about 40 amino acids. Neuropilin (Nrp), one of these cell surface receptors, functions as the receptor for class 3 secreted vertebrate semaphorins (SEMA3A, SEMA3B, SEMA3C and SEMA3F) and several forms of vascular endothelial growth factors (VEGF) to mediate axon guidance, neural cell migration and angiogenesis in the development of the nervous system and the cardiovascular system (reviewed in Neufeld et al., 2002).
GeneFunction Lee et al. (2002) demonstrated that provide the first physiological demonstration that NRP1 regulates angiogenesis through a VEGF-dependent pathway.Wolman et al. (2004) showed along with together with combined partial knock-down experiments, provide evidence that axons may respond differentially to a single semaphorin, depending on their neuropilin composition. Together, these data support the hypothesis that Sema3D may act as a repellent through receptors containing Npn-1A and as an attractant via receptors containing Npn-1A and Npn-2B. Yu et al. (2004) Based on synteny, zebrafish nrp1b and the previously cloned nrp1a are orthologous to human nrp1, and zebrafish nrp2a and 2b orthologous to human nrp2. They have cloned and characterized the expression patterns of these four zebrafishneuropi lin genes in wild type embryos from the beginning of somitogenesis to 48 h post-fertilization. Zebrafish nrp1a is expressed in the neural tube including telencephalon, epithalamus, cells along the axonal trajectory of the posterior commissure and the medial longitudinal fascicle, hindbrain neurons, vagus motor neurons and spinal motoneurons. Zebrafish nrp1b is expressed in the nose, the cranial neural crest cell (NCC) derived tissue underlying the hypothalamus, endothelial precursors and the trunk and tail vasculature. Zebrafish nrp2a is expressed in telencephalon, anterior pituitary, oculomotor and trochlear motor neurons, cells along the supra-optic and posterior commissures, hindbrain rhombomere 1, hindbrain neurons, cranial NCCs and sclerotome. Zebrafish nrp2b is expressed in telencephalon, thalamus, hypothalamus, epiphysis, cells along the anterior and posterior commissures, post-optic and supra-optic commissures and the olfactory axonal trajectory, hindbrain neurons, cranial NCCs, somites and spinal cord neurons.Feldner et al. (2005) showed that knockdown of nrp1a alone or in combination with sema3A1, sema3A2, or VEGF perturbs outgrowth of ventral motor nerves. This finding suggested that interactions of several ligands with NRP1a in primary motor neurons play a role in the patterning of peripheral nerves in zebrafishKuan et al. (2007) reported here that nrp1a is selectively expressed in the left habenula of zebrafish larvae at the time when left and right habenular neurons are establishing different D-V projections onto the IPN. As with other habenular asymmetries, Nodal signaling and the left-sided parapineal mediate this L-R difference in nrp1a expression. Loss of Nrp1a prevents dorsal innervation of the IPN by left habenular neurons, as does depletion of a specific Semaphorin, Sema3D. Conversely, Sema3D overexpression results in ectopic axonal projections from the left habenula that extend beyond the IPN. These results indicate that Sema3D signaling through the asymmetrically distributed Nrp1a receptor in left and right habenular neurons mediates the differential D-V innervation of their shared synaptic target.

GeneStructure This gene encodes five transcript. transcript ENSDART00000129276 has 17 exons and 6364 bp long, the protien product ENSDARP00000105696 is 926 residue long. transcript ENSDART00000129263 has 17 exons and is 3875 bp long, the protien product ENSDARP00000112392 has 916 residues. transcript ENSDART00000130586 has 17 exons and is 3644 bp long and the protien product ENSDARP00000108513 has 923 residue. transcript ENSDART00000106639 has 17 exones and is 3174 bps long, the protien product ENSDARP00000097417 has 923 residues. transcript ENSDART00000150603 has 8 exons and is 1977 bps long, the protien product ENSDARP00000125126 has 438 residues.
Protein ENSDARP00000105696 ENSDARP00000108513 ENSDARP00000112392 ENSDARP00000097417
ProteinDomainandFamilies has domain InterPro:IPR000421; InterPro:IPR014648; InterPro:IPR000859; InterPro:IPR000998;
Motifs has motif Prosite:PS00740; Prosite:PS01285; Prosite:PS01286; PFAM:PF00431; PFAM:PF00629; PFAM:PF00754; PRINTS:PR00020; UniProt:NRP1A_DANRE;
Expression ArrayExpress:ENSDARG00000071865
GeneOntology GO:0016020; GO:0016021; GO:0005786; GO:0005579; GO:0007155; GO:0008045; GO:0001570; GO:0051216; GO:0048538; GO:0007508; GO:0001755; GO:0007399; GO:0030154; GO:0001525; GO:0009968; GO:0007411; GO:0030947; GO:0007413; GO:0045765; GO:0048010; GO:0004872; GO:0005021;
Orthologs Entrez:8829;
VariationAndRepeats RSID:rs40988283: RSID:rs40988283: RSID:rs40988283: RSID:rs40988283: RSID:rs252319327: RSID:rs252319327: RSID:rs252319327: RSID:rs41085313: RSID:rs41085313: RSID:rs41085313: RSID:rs41085313: RSID:rs41136283: RSID:rs41136283: RSID:rs41136283: RSID:rs41136283: RSID:rs41029061: RSID:rs41029061: RSID:rs41029061: RSID:rs41029061: RSID:rs40697737: RSID:rs40697737: RSID:rs40697737: RSID:rs40697737: RSID:rs40821686: RSID:rs40821686: RSID:rs40821686: RSID:rs40821686: RSID:rs40862474: RSID:rs40862474: RSID:rs40862474: RSID:rs40862474: RSID:rs40967578: RSID:rs40967578: RSID:rs40967578: RSID:rs40967578: RSID:rs40901700: RSID:rs40901700: RSID:rs40901700: RSID:rs40901700: RSID:rs40878807: RSID:rs40878807: RSID:rs40878807: RSID:rs41159763: RSID:rs41159763: RSID:rs41159763: RSID:rs41159763: [[RSID:rs40796930 rs40796930 rs40796930 rs40796930 rs40924737 rs40924737 rs40924737 rs40924737 rs41190266 rs41190266 rs41190266 rs41190266 rs41121731 rs41121731 rs41121731 rs41121731 rs40613388 rs40613388 rs40613388 rs40613388 rs41224537 rs41224537 rs41224537 rs41224537 rs41020682 rs41020682 rs41020682 rs41020682 rs40959375 rs40959375 rs40959375 rs40959375 rs41023776 rs41023776 rs41023776 rs41023776 rs40953626 rs40953626 rs40953626 rs40953626 rs41169192 rs41169192 rs41169192 rs41169192 rs41246668 rs41246668 rs41246668 rs41246668 rs40620249 rs40620249 rs40620249 rs40620249 rs41158138 rs41158138 rs41158138 rs41158138 rs41158138 rs41158138 rs41158138 rs41172386 rs41172386 rs41172386 RSID:rs41218737: RSID:rs41218737
DisordersAndMutations ZFINID:ZDB-GENO-071217-9;ZFINID:ZDB-GENO-071217-10;ZFINID:ZDB-GENO-071217-11;
RelatedPubMedArticles Lee P.; Goishi K.; Davidson A. J.; Mannix R.; Zon L.; Klagsbrun M.: Neuropilin-1 is required for vascular development and is a mediator of VEGF-dependent angiogenesis in zebrafish. Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10470-5. PMID: 12142468 Bovenkamp D. E.; Goishi K.; Bahary N.; Davidson A. J.; Zhou Y.; Becker T.; Becker C. G.; Zon L. I.; Klagsbrun M.: Expression and mapping of duplicate neuropilin-1 and neuropilin-2 genes in developing zebrafish. Gene Expr Patterns. 2004. 4(4):361-70. PMID: 15183302 Wolman M. A.; Liu Y.; Tawarayama H.; Shoji W.; and Halloran M. C. Repulsion and attraction of axons by Semaphorin3D are mediated by different neuropilins in vivo. J. Neurosci. 2004. 24(39):8428-8435. PMID: 15456815 Bovenkamp D. E.; Goishi K.; Bahary N.; Davidson A. J.; Zhou Y.; Becker T.; Becker C. G.; Zon L. I.; Klagsbrun M.: Expression and mapping of duplicate neuropilin-1 and neuropilin-2 genes in developing zebrafish. Gene Expr Patterns. 2004. 4(4):361-70. PMID: 15183302 Yu H. H.; Houart C.; Moens C. B.: Cloning and embryonic expression of zebrafish neuropilin genes. Gene Expr Patterns. 2004. 4(4):371-8. PMID: 15183303 Feldner J.; Becker T.; Goishi K.; Schweitzer J.; Lee P.; Schachner M.; Klagsbrun M.; Becker C. G.: Neuropilin-1a is involved in trunk motor axon outgrowth in embryonic zebrafish. Dev Dyn. 2005. 234(3):535-49. PMID: 16110501 Feldner J.; Becker T.; Goishi K.; Schweitzer J.; Lee P.; Schachner M.; Klagsbrun M.; Becker C. G.: Neuropilin-1a is involved in trunk motor axon outgrowth in embryonic zebrafish. Dev Dyn. 2005. 234(3):535-49. PMID: 16110501 Yu H. H.; Moens C. B.: Semaphorin signaling guides cranial neural crest cell migration in zebrafish. Dev Biol. 2005. 280(2):373-85. PMID: 15882579 Wolman M. A.; Regnery A. M.; Becker T.; Becker C. G.; Halloran M. C.: Semaphorin3D regulates axon axon interactions by modulating levels of L1 cell adhesion molecule. J Neurosci. 2007. 5;27(36):9653-63. PMID: 17804626 Kuan, Y. S., Yu H. H.; Moens, C. B.; and Halpern M. E. Neuropilin asymmetry mediates a left-right difference in habenular connectivity. Development. 2007. 134(5):857-865. PMID: 17251263 NCBI Resource Coordinators.: Database resources of the National Center for Biotechnology Information. Nucleic Acids Res. 41(Database issue):D8-D20. 2013. PMID:23193264
Kersey, P. J.; Allen, J. E.; Christensen, M.; et al.: Ensembl Genomes 2013: scaling up access to genome-wide data. Nucleic Acids Res. 2013. PMID:24163254
Sigrist, C. J. A.; de, Castro, E; Cerutti, L; Cuche, B. A.; Hulo, N.; Bridge, A.; Bougueleret, L. Xenarios, I.: New and continuing developments at PROSITE. Nucleic Acids Res. doi: 10.1093/nar/gks1067. 2012. PMID:23161676
Punta, M.; Coggill, P. C.; Eberhardt, et al.: The Pfam protein families database. Nucleic Acids Res. 40(Database Issue):D290-D301. 2012. PMID:22127870
Hunter, S.; Jones P.; Mitchell A.; et al.: Interpro in 2011: new developments in the family and domain prediction database. Nucleic Acids Res. doi: 10.1093/nar/gkr948. 2011. PMID:22096229
Carbon, S.; Ireland, A.; Mungall, C. J.; Shu, S.; Marshall, B.; Lewis, S.; AMIGO Hub; Web Presence Working Group.: AMIGO: online access to ontology and annotation data. Bioinformatics. 25(2):288-9. 2009. PMID:19033274
Ashburner, M.; Ball, C. A.; Blake, J. A.; et al. The Gene Ontology Consortium.: Gene ontology: tool for the unification of biology. Nat. Genet. 25(1):25-9. 2000. PMID:10802651
Sherry, S. T.; Ward, M. H.; Kholodov, M.; Baker, J.; Phan, L.; Smigielski, E. M.; Sirotkin, K.: dbSNP: the NCBI database of genetic variation. Nucleic Acids Res. 1;29(1):308-11. 2001. PMID:11125122
Bradford, Y.; Conlin, T.; Dunn, N.; et al.: ZFIN: enhancements and updates to the zebrafish model organism database. Nucleic Acids Res. 39(suppl 1):D822-D829. 2011. PMID:21036866
Kapushesky, M.; Adamusiak, T.; Burdett, T.; et al.: Gene Expression Atlas update--a value-added database of microarray and sequencing-based functional genomics experiments. Nucleic Acids Res. 40(Database isue):D1077-81. 2012. PMID:22064864

Web resources:
NCBI: http://www.ncbi.nlm.nih.gov/
PFAM: http://pfam.sanger.ac.uk/
PROSITE: http://prosite.expasy.org/
Interpro: http://www.ebi.ac.uk/interpro/
ZFIN: http://zfin.org/
Expression Atlas (EMBL): http://www.ebi.ac.uk/gxa/
Ensembl: http://asia.ensembl.org/Danio_rerio/
Database of Single Nucleotide Polymorphisms (dbSNP). Bethesda (MD): National Center for Biotechnology Information, National Library of Medicine.: http://www.ncbi.nlm.nih.gov/SNP/
PRINTS from Genomenet: http://www.genome.jp/
European Nucleotide Archive: http://www.ebi.ac.uk/ena/home
UNIGENE: http://www.ncbi.nlm.nih.gov/unigene/
AMIGO Gene Ontology: http://amigo.geneontology.org
Topic revision: r3 - 2013-07-06 - RamcharanAngom
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