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0NELL1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameNELL1
DescriptionProtein kinase c-binding protein nell1 precursor (nel-like protein 1) (nel-related protein 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0007399 neurogenesis (TAS)
Domain Architecture (Details)
InterPro domains assigned to SynO:
Laminins are large heterotrimeric glycoproteins involved in basement membrane function . The laminin globular (G) domain can be found in one to several copies in various laminin family members.ncluding a large number of extracellular proteins. The C-terminus of the laminin alpha chain contains a tandem repeat of five laminin G domains.hich are critical for heparin-binding and cell attachment activity . Laminin alpha4 is distributed in a variety of tissues including peripheral nerves.orsal root ganglion.keletal muscle and capillaries; in the neuromuscular junction.t is required for synaptic specialisation . The structure of the laminin-G domain has been predicted to resemble that of pentraxin .Laminin G domains can vary in their function.nd a variety of binding functions have been ascribed to different LamG modules. For example.he laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains.here only domains LG4 and LG5 contain binding sites for heparin.ulphatides and the cell surface receptor dystroglycan . Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion.ignalling.igration.ssembly and differentiation. Proteins with laminin-G domains include:Laminin.Merosin.Agrin.Neurexins.Vitamin K dependent protein S.Sex steroid binding protein SBP/SHBG.Drosophila proteins Slit.rumbs.at.several proteoglycan precursors.
  IPR001791:Laminin G
InterPro domains unassigned to SynO:
Laminins are large heterotrimeric glycoproteins involved in basement membrane function . The laminin globular (G) domain can be found in one to several copies in various laminin family members.ncluding a large number of extracellular proteins. Laminin G domains can vary in their function.nd a variety of binding functions has been ascribed to different LamG modules. For example.he laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains.here only domains LG4 and LG5 contain binding sites for heparin.ulphatides and the cell surface receptor dystroglycan . Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion.ignalling.igration.ssembly and differentiation.This entry represents the thrombospondin-type laminin G domain found in various laminins.he N-terminus of thrombospondin (TspN) and pentraxins. Both laminin G and TspN-containing proteins belong to an extensive class of multi-domain adhesive proteins in the matrix that surrounds animal cells.cting as molecular bridges between cells and matrix.nd participating in cell-cell communication . Pentraxins include C-reactive proteins (CRP) and serum amyloid protein (SAP).
  IPR003129:Laminin G, Thrombospondin-type, N-terminal
The vWF domain is found in various plasma proteins:complement factors B.2.R3 and CR4; the integrins (I-domains); collagen types VI.II.II and XIV; and other extracellular proteins . Although the majority of VWA-containing proteins are extracellular.he most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription.NA repair.ibosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Proteinsthat incorporate vWF domains participate in numerous biological events(e.g. cell adhesion.igration.oming.attern formation.nd signaltransduction).nvolving interaction with a large array of ligands . A number of human diseases arise from mutations in VWA domains. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of alpha-helices and beta-strands .The domain is named after the von Willebrand factor (VWF) type C repeat which is found in multidomain protein/multifunctional proteins involved in maintaining homeostasis . For the von Willebrand factor the duplicated VWFC domain is thought to participate in oligomerization.ut not in the initial dimerization step . The presence of this region in a number of other complex-forming proteins points to the possible involvment of the VWFC domain in complex formation.
  IPR001007:von Willebrand factor, type C
A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown .o be present in a large number of membrane-bound and extracellular.ostly animal.roteins. Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N-terminus of some EGF-like domains . Calcium-binding may be crucial for numerous protein-protein interactions.For human coagulation factor IX it has been shown that the calcium-ligands form a pentagonal bipyramid. The first.hird and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated (see aspartic acid and asparagine hydroxylation site) . A conserved aromatic residue.s well as the second conserved negative residue.re thought to be involved in stabilizing the calcium-binding site.As in non-calcium binding EGF-like domains.here are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes .
  IPR013091:EGF calcium-binding
A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown .o be present in a large number of membrane-bound and extracellular.ostly animal.roteins. Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N-terminus of some EGF-like domains . Calcium-binding may be crucial for numerous protein-protein interactions.For human coagulation factor IX it has been shown that the calcium-ligands form a pentagonal bipyramid. The first.hird and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated (see aspartic acid and asparagine hydroxylation site) . A conserved aromatic residue.s well as the second conserved negative residue.re thought to be involved in stabilizing the calcium-binding site.As in non-calcium binding EGF-like domains.here are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes .
  IPR001881:EGF-like calcium-binding
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.This entry contains EGF domains found in a variety of extracellular and membrane proteins
  IPR013111:EGF, extracellular
Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain.hich consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse.nd include the lectins: legume lectins.ereal lectins.iral lectins.nd animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds.he binding of nitrogen-fixing bacteria to root hairs.he inhibition of fungal growth or insect feeding.nd in hormonally regulated plant growth . Protein members include concanavalin A (Con A).avin.solectin I.ectin IV.oybean agglutinin and lentil lectin. Animal lectins include the galectins.hich are S-type lactose-binding and IgE-binding proteins such as S-lectin.LC protein.alectin1.alectin2.alectin3 CRD.nd Congerin I . Other members with a Con A-like domain include the glucanases and xylanases. Bacterial and fungal beta-glucanases.uch as Bacillus 1-3.-4-beta-glucanse.arry out the acid catalysis of beta-glucans found in microorganisms and plants . Similarly.appa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls . Xylanase and cellobiohydrolase I degrade hemicellulose and cellulose.espectively . There are many Con A-like domains found in proteins involved in cell recognition and adhesion. For example.everal viral and bacterial toxins carry Con A-like domains. Examples include the Clostridium neurotoxins responsible for the neuroparalytic effects of botulism and tetanus . The Pseudomonas exotoxin A. virulence factor which is highly toxic to eukaryotic cells.ausing the arrest of protein synthesis.ontains a Con A-like domain involved in receptor binding . Cholerae neuraminidase can bind to cell surfaces.ossibly through their Con A-like domains.here they function as part of a mucinase complex to degrade the mucin layer of the gastrointestinal tract . The rotaviral outer capsid protein.P4.as a Con A-like sialic acid binding domain.hich functions in cell attachment and membrane penetration . Con A-like domains also play a role in cell recognition in eukaryotes. Proteins containing a Con A-like domain include the sex hormone-binding globulins which transport sex steroids in blood and regulate their access to target tissues .aminins which are large heterotrimeric glycoproteins involved in basement membrane architecture and function .eurexins which are expressed in hundreds of isoforms on the neuronal cell surface.here they may function as cell recognition molecules and sialidases that are found in both microorganisms and animals.nd function in cell adhesion and signal transduction . Other proteins containing a Con A-like domain include pentraxins and calnexins. The pentraxin PTX3 is a TNFalpha-induced.ecreted protein of adipose cells produced during inflammation . The calnexin family of molecular chaperones is conserved among plants.ungi.nd animals. Family members include Calnexin. type-I integral membrane protein in the endoplasmic reticulum which coordinates the processing of newly synthesized N-linked glycoproteins with their productive folding.almegin. type-I membrane protein expressed mainly in the spermatids of the testis.nd calreticulin. soluble ER lumenal paralog .
  IPR008985:Concanavalin A-like lectin/glucanase
This SSF signature was designed to identify serine proteases inhibitors belonging to the grasshopper PMP inhibitor family .nd to the desert locust SGCI/SGTI family .oth of which belong to MEROPS inhibitor family I19.lan IW. The PMP inhibitors have a conserved array of six cysteine residues (Cys-Xaa(9-12)-Cys-Asn-Xaa-Cys-Xaa-Cys-Xaa(2-3)-Gly-Xaa(3-4)-Cys-Thr-Xaa(3)-Cys).hich are involved in an identical disulfide bridge pattern (Cys(1)-Cys(4).ys(2)-Cys(6).ys(3)-Cys(5)) . Some of the PMP inhibitors are fucosylated.he function of the fucose moiety being unknown.The signature also matches many proteins which are not known to be proteinase inhibitors.nd which are annotated as mucin.CO-spondin.ollagen alpha 1.agged1.agged2 or von Willebrand factor.ype D and type C.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009041:Proteinase inhibitor, PMP and SGCI
Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain.hich consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse.nd include the lectins: legume lectins.ereal lectins.iral lectins.nd animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds.he binding of nitrogen-fixing bacteria to root hairs.he inhibition of fungal growth or insect feeding.nd in hormonally regulated plant growth . Protein members include concanavalin A (Con A).avin.solectin I.ectin IV.oybean agglutinin and lentil lectin. Animal lectins include the galectins.hich are S-type lactose-binding and IgE-binding proteins such as S-lectin.LC protein.alectin1.alectin2.alectin3 CRD.nd Congerin I . Other members with a Con A-like domain include the glucanases. Bacterial and fungal beta-glucanases.uch as Bacillus 1-3.-4-beta-glucanse.arry out the acid catalysis of beta-glucans found in microorganisms and plants . Similarly.appa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls . This entry differs from () by omitting the xylanases and glycosyl hydrolases.
  IPR013320:Concanavalin A-like lectin/glucanase, subgroup
Epidermal growth factors and transforming growth factors belong to a general class of proteins that share a repeat pattern involving a number of conserved Cys residues. Growth factors are involved in cell recognition and division . The repeating pattern.specially of cysteines (the so-called EGF repeat).s thought to be important to the 3D structure of the proteins.nd hence its recognition by receptors and other molecules. The type 1 EGF signature includes six conserved cysteines believed to be involved in disulphide bond formation. The EGF motif is found frequently in nature.articularly in extracellular proteins.
  IPR006210:EGF
IPR003129:TSPN 
Evalue:-77.431798275933 
Location:29-213IPR001007:VWC 
Evalue:-13.8538722991943 
Location:273-331IPR001007:VWC 
Evalue:-12.8860569000244 
Location:694-749IPR001881:EGF_CA 
Evalue:-9.85387196432176 
Location:549-595IPR013091:EGF_CA 
Evalue:-9.61978912353516 
Location:434-474IPR013091:EGF_CA 
Evalue:-6.58502674102783 
Location:596-634IPR013091:EGF_CA 
Evalue:-6.22184896469116 
Location:478-515IPR013111:EGF_2 
Evalue:-4.25181198120117 
Location:519-546IPR001007:VWC 
Evalue:-0.0315170514460649 
Location:335-389IPR008985:ConA_like_lec_gl 
Evalue:0 
Location:3-15IPR006210:EGF 
Evalue:0.146128035678238 
Location:394-433
SequencesProtein: NELL1_HUMAN (810 aa)
mRNA: AK127805 NM_006157
Local Annotation
Synapse Ontology
A neuromuscular junction is the junction of the axon terminal of a motoneuron with the motor end plate, the highly-excitable region of muscle fiber plasma membrane responsible for initiation of action potentials across the muscle's surface.
sdb:0024 neuromuscular junction  (Evidence:keywords,domains)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 70 residues, 20647692-20647900Exon2: 30 residues, 20652610-20652694Exon3: 45 residues, 20656053-20656182Exon4: 52 residues, 20761801-20761952Exon5: 59 residues, 20825704-20825875Exon6: 34 residues, 20863565-20863662Exon7: 26 residues, 20896303-20896376Exon8: 29 residues, 20897373-20897456Exon9: 47 residues, 20905429-20905564Exon10: 36 residues, 20906498-20906601Exon11: 26 residues, 20915907-20915981Exon12: 35 residues, 20925457-20925557Exon13: 45 residues, 20938553-20938682Exon14: 44 residues, 21091710-21091836Exon15: 43 residues, 21207453-21207576Exon16: 34 residues, 21348974-21349070Exon17: 49 residues, 21512495-21512636Exon18: 66 residues, 21538310-21538504Exon19: 61 residues, 21548885-21549062Exon20: 77 residues, 21551306-21551531Exon21: 238 residues, 21553093-21553803Exon22: 2 residues, -Jump to NELL1_HUMANExon1: 64 residues, 20647711-20647900Exon2: 45 residues, 20656053-20656182Exon3: 52 residues, 20761801-20761952Exon4: 59 residues, 20825704-20825875Exon5: 34 residues, 20863565-20863662Exon6: 26 residues, 20896303-20896376Exon7: 29 residues, 20897373-20897456Exon8: 47 residues, 20905429-20905564Exon9: 36 residues, 20906498-20906601Exon10: 26 residues, 20915907-20915981Exon11: 35 residues, 20925457-20925557Exon12: 45 residues, 20938553-20938682Exon13: 44 residues, 21091710-21091836Exon14: 43 residues, 21207453-21207576Exon15: 34 residues, 21348974-21349070Exon16: 49 residues, 21512495-21512636Exon17: 66 residues, 21538310-21538504Exon18: 61 residues, 21548885-21549062Exon19: 77 residues, 21551306-21551531Exon20: 163 residues, 21553093-21553576Exon21: 2 residues, -Jump to NELL1_HUMAN  
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