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0AVIL_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameAVIL
DescriptionAdvillin (p92).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0015629 actin cytoskeleton (TAS)
0007399 neurogenesis (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Gelsolin is a cytoplasmic.alcium-regulated.ctin-modulating protein that bindsto the barbed ends of actin filaments.reventing monomer exchange (end-blocking orcapping) . It can promote nucleation (the assembly ofmonomers into filaments).s well as sever existing filaments. In addition.his proteinbinds with high affinity to fibronectin. Plasma gelsolin and cytoplasmic gelsolin arederived from a single gene by alternate initiation sites and differential splicing.Sequence comparisons indicate an evolutionary relationship between gelsolin.illin.ragmin and severin . Six large repeating segmentsoccur in gelsolin and villin.nd 3 similar segments in severin and fragmin. While themultiple repeats have yet to be related to any known function of the actin-severingproteins.he superfamily appears to have evolved from an ancestral sequence of 120to 130 amino acid residues .
  IPR007123:Gelsolin region
Villin is an F-actin bundling protein involved in themaintenance of the microvilli of the absorptive epithelia. The villin-type "headpiece" domain is a modular motif found at the extreme C-terminus of larger "core" domains in over 25 cytoskeletal proteins in plants and animals.ften in assocation with the Gelsolin repeat. Although the headpiece is classified as an F-actin-binding domain.t has been shown that not all headpiece domains are intrinsically F-actin-binding motifs.urface charge distribution may be an important element for F-actin recognition . An autonomously folding.5 residue.hermostable subdomain (HP36) of the full-length 76 amino acid residue villinheadpiece.s the smallest known example of a cooperatively folded domain of a naturally occurring protein. The structure of HP36.s determined by NMRspectroscopy.onsists of three short helices surrounding a tightly packed hydrophobic core .
  IPR003128:Villin headpiece
Gelsolin is a cytoplasmic.alcium-regulated.ctin-modulating protein that binds to the barbed ends of actin filaments.reventing monomer exchange (end-blocking or capping) . It can promote nucleation (the assembly of monomers into filaments).s well as sever existing filaments. In addition.his protein binds with high affinity to fibronectin. Plasma gelsolin and cytoplasmic gelsolin are derived from a single gene by alternate initiation sites and differential splicing.Sequence comparisons indicate an evolutionary relationship between gelsolin.illin.ragmin and severin . Six large repeating segments occur in gelsolin and villin.nd 3 similar segments in severin and fragmin. While the multiple repeats have yet to be related to any known function of the actin-severing proteins.he superfamily appears to have evolved from an ancestral sequence of 120 to 130 amino acid residues .
  IPR007122:Gelsolin
IPR007122:GEL 
Evalue:-29.4559319556497 
Location:617-711IPR007122:GEL 
Evalue:-28.8239087409443 
Location:512-598IPR007122:GEL 
Evalue:-28.1249387366083 
Location:253-346IPR007122:GEL 
Evalue:-23.8860566476932 
Location:395-492IPR007122:GEL 
Evalue:-23.537602002101 
Location:14-111IPR007122:GEL 
Evalue:-22.0315170514461 
Location:132-226IPR003128:VHP 
Evalue:-19.8538722991943 
Location:784-819
SequencesProtein: AVIL_HUMAN (819 aa)
mRNA: BC111730 NM_006576
Local Annotation
Synapse Ontology
actin exists in two states within the cell: as polymerized two-stranded helical filaments (F-actin) or as monomers (Gactin), which provide the building blocks for filament assembly.
sdb:0283 G-actin  (Evidence:keywords)
KO assignmentK08017
  Level 3 annotation:
    advillin
  Level 2 annotation:
    Membrane and intracellular structural molecules
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 113 residues, 56477709-56478045Exon2: 44 residues, 56479844-56479970Exon3: 25 residues, 56481193-56481262Exon4: 65 residues, 56482209-56482398Exon5: 50 residues, 56483296-56483441Exon6: 50 residues, 56483573-56483719Exon7: 62 residues, 56486409-56486589Exon8: 55 residues, 56487380-56487539Exon9: 48 residues, 56487639-56487777Exon10: 35 residues, 56488243-56488344Exon11: 53 residues, 56488444-56488598Exon12: 35 residues, 56489646-56489745Exon13: 28 residues, 56489861-56489940Exon14: 69 residues, 56490398-56490601Exon15: 39 residues, 56490865-56490976Exon16: 38 residues, 56491068-56491177Exon17: 67 residues, 56493276-56493473Exon18: 27 residues, 56494201-56494276Exon19: 33 residues, 56496024-56496119Exon20: 2 residues, -Jump to AVIL_HUMANExon1: 86 residues, 56477789-56478045Exon2: 44 residues, 56479844-56479970Exon3: 25 residues, 56481193-56481262Exon4: 65 residues, 56482209-56482398Exon5: 50 residues, 56483296-56483441Exon6: 50 residues, 56483573-56483719Exon7: 62 residues, 56486409-56486589Exon8: 55 residues, 56487380-56487539Exon9: 48 residues, 56487639-56487777Exon10: 35 residues, 56488243-56488344Exon11: 53 residues, 56488444-56488598Exon12: 35 residues, 56489646-56489745Exon13: 28 residues, 56489861-56489940Exon14: 69 residues, 56490398-56490601Exon15: 39 residues, 56490865-56490976Exon16: 38 residues, 56491068-56491177Exon17: 67 residues, 56493276-56493473Exon18: 27 residues, 56494201-56494276Exon19: 40 residues, 56495627-56495742Exon20: 30 residues, 56496024-56496108Exon21: 2 residues, -Jump to AVIL_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2768 56462825-56476784 ~-14K 9198(TSFM)(+)Loci: 4058 56477709-56496119 ~-18K 9200(AVIL)(-)Loci: 4057 56210360-56227245 ~-17K 9162(DCTN2)(-)Link out to UCSC