O88398 · AVIL_MOUSE
- ProteinAdvillin
- GeneAvil
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids819 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ca2+-regulated actin-binding protein which plays an important role in actin bundling. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis (PubMed:15247299, PubMed:18160648).
In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (By similarity).
In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (By similarity).
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | actin filament | |
Cellular Component | axon | |
Cellular Component | cell projection | |
Cellular Component | cytoplasm | |
Cellular Component | focal adhesion | |
Cellular Component | lamellipodium | |
Cellular Component | neuron projection | |
Molecular Function | actin binding | |
Molecular Function | actin filament binding | |
Molecular Function | Arp2/3 complex binding | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate binding | |
Biological Process | actin filament organization | |
Biological Process | actin filament severing | |
Biological Process | actin polymerization or depolymerization | |
Biological Process | barbed-end actin filament capping | |
Biological Process | cilium assembly | |
Biological Process | nervous system development | |
Biological Process | positive regulation of lamellipodium assembly | |
Biological Process | positive regulation of neuron projection development | |
Biological Process | regulation of diacylglycerol biosynthetic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameAdvillin
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO88398
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In podocytes, present in the F-actin-enriched cell periphery that generates lamellipodia and focal adhesions.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Half of the homozygous mice die during embryogenesis, the other 50% do not show any noticeable abnormality in development, growth or behavior and are fertile.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 53 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000218737 | 1-819 | Advillin | |||
Sequence: MSLSSAFRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGSLLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQYHESDTFRGYFKQGIIYKKGGVASGMKHVETNTYDVKRLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAASPGLMTVLQDTLGRRSMIKPAVSDEIMDQQQKSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTNVETVNDGAESAMFKQLFQKWSVKDQTTGLGKIFSTGKIAKIFQDKFDVSLLHTKPEVAAQERMVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVRVSMGKEPRHFMAIFKGKLVIYEGGTSRKGNEEPDPPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDGNADTVAEGQEPPEFWDLLGGKTAYANDKRLQQETLDVQVRLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRDPDTPILIIKQGFEPPTFTGWFLAWDPHIWSEGKSYEQLKNELGDATAIVRITADMKNATLYLNPSDGEPKYYPVEVLLKGQNQELPEDVDPAKKENYLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF | ||||||
Modified residue | 85 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 748 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 758 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Most highly expressed in the endometrium of the uterus, the intestinal villi and the testes. Weaker expression also detected in the brain, dorsal root ganglions and on the surface of the tongue.
Developmental stage
Expressed almost exclusively in peripheral sensory neurons (craniofacial and dorsal root ganglia (DRG) sensory neurons), but also in trigeminal ganglia (TG) Me5 proprioceptive neurons and Mo5 motoneurons.
Gene expression databases
Interaction
Subunit
Associates (via C-terminus) with actin (By similarity).
Interacts with F-actin (By similarity).
Interacts with SCARF1; the interaction occurs in embryonic dorsal root ganglions at 18 dpc and induces neurite-like outgrowth (PubMed:15247299).
Interacts with PLCE1. Interacts with ACTR2 and ACTR3; associates with the ARP2/3 complex (By similarity).
Interacts with F-actin (By similarity).
Interacts with SCARF1; the interaction occurs in embryonic dorsal root ganglions at 18 dpc and induces neurite-like outgrowth (PubMed:15247299).
Interacts with PLCE1. Interacts with ACTR2 and ACTR3; associates with the ARP2/3 complex (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-731 | Core | ||||
Sequence: MSLSSAFRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGSLLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQYHESDTFRGYFKQGIIYKKGGVASGMKHVETNTYDVKRLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAASPGLMTVLQDTLGRRSMIKPAVSDEIMDQQQKSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTNVETVNDGAESAMFKQLFQKWSVKDQTTGLGKIFSTGKIAKIFQDKFDVSLLHTKPEVAAQERMVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVRVSMGKEPRHFMAIFKGKLVIYEGGTSRKGNEEPDPPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDGNADTVAEGQEPPEFWDLLGGKTAYANDKRLQQETLDVQVRLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRDPDTPILIIKQGFEPPTFTGWFLAWDPHIWSEGKSYEQLKNELGD | ||||||
Repeat | 24-73 | Gelsolin-like 1 | ||||
Sequence: MELALVPLSAHGNFYEGDCYIVLSTRRVGSLLSQNIHFWIGKDSSQDEQS | ||||||
Repeat | 145-185 | Gelsolin-like 2 | ||||
Sequence: IQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERL | ||||||
Repeat | 262-306 | Gelsolin-like 3 | ||||
Sequence: LSVTEVATRPLVQDLLNHDDCYILDQSGTKIYVWKGKGATKVEKQ | ||||||
Repeat | 403-454 | Gelsolin-like 4 | ||||
Sequence: ENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELA | ||||||
Repeat | 525-565 | Gelsolin-like 5 | ||||
Sequence: TKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERA | ||||||
Repeat | 628-669 | Gelsolin-like 6 | ||||
Sequence: FLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKK | ||||||
Region | 628-819 | Required for interaction with F-actin | ||||
Sequence: FLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRDPDTPILIIKQGFEPPTFTGWFLAWDPHIWSEGKSYEQLKNELGDATAIVRITADMKNATLYLNPSDGEPKYYPVEVLLKGQNQELPEDVDPAKKENYLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF | ||||||
Region | 732-819 | Headpiece | ||||
Sequence: ATAIVRITADMKNATLYLNPSDGEPKYYPVEVLLKGQNQELPEDVDPAKKENYLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF | ||||||
Domain | 753-819 | HP | ||||
Sequence: DGEPKYYPVEVLLKGQNQELPEDVDPAKKENYLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF |
Sequence similarities
Belongs to the villin/gelsolin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length819
- Mass (Da)92,032
- Last updated2011-07-27 v2
- Checksum75C13F095A898876
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 15 | in Ref. 2; AAC31808 | ||||
Sequence: R → G | ||||||
Sequence conflict | 469 | in Ref. 1; AAC25050 | ||||
Sequence: G → R | ||||||
Sequence conflict | 538 | in Ref. 1; AAC25050 | ||||
Sequence: N → I | ||||||
Sequence conflict | 809 | in Ref. 1; AAC25050 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 814 | in Ref. 1; AAC25050 | ||||
Sequence: K → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF041448 EMBL· GenBank· DDBJ | AAC25050.1 EMBL· GenBank· DDBJ | mRNA | ||
AF059486 EMBL· GenBank· DDBJ | AAC31808.1 EMBL· GenBank· DDBJ | mRNA | ||
AK154851 EMBL· GenBank· DDBJ | BAE32877.1 EMBL· GenBank· DDBJ | mRNA | ||
AK155900 EMBL· GenBank· DDBJ | BAE33492.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466578 EMBL· GenBank· DDBJ | EDL24458.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC120545 EMBL· GenBank· DDBJ | AAI20546.1 EMBL· GenBank· DDBJ | mRNA |