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Protein

Advillin

Gene

Avil

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ca2+-regulated actin-binding protein. 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.2 Publications

GO - Molecular functioni

GO - Biological processi

  • actin filament capping Source: UniProtKB-KW
  • actin filament organization Source: MGI
  • cilium morphogenesis Source: UniProtKB
  • positive regulation of neuron projection development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Advillin
Alternative name(s):
Actin-binding protein DOC6
p92
Gene namesi
Name:Avil
Synonyms:Advil
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1333798. Avil.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 819819AdvillinPRO_0000218737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei85 – 851PhosphotyrosineCombined sources
Modified residuei748 – 7481PhosphotyrosineCombined sources
Modified residuei758 – 7581PhosphotyrosineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO88398.
PaxDbiO88398.
PRIDEiO88398.

PTM databases

iPTMnetiO88398.
PhosphoSiteiO88398.

Expressioni

Tissue specificityi

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.3 Publications

Developmental stagei

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.2 Publications

Gene expression databases

BgeeiO88398.
CleanExiMM_AVIL.
ExpressionAtlasiO88398. baseline and differential.
GenevisibleiO88398. MM.

Interactioni

Subunit structurei

Associates (via C-terminus) with actin. 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.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198012. 2 interactions.
IntActiO88398. 1 interaction.
STRINGi10090.ENSMUSP00000026500.

Structurei

3D structure databases

ProteinModelPortaliO88398.
SMRiO88398. Positions 7-819.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati24 – 7350Gelsolin-like 1Add
BLAST
Repeati145 – 18541Gelsolin-like 2Add
BLAST
Repeati262 – 30645Gelsolin-like 3Add
BLAST
Repeati403 – 45452Gelsolin-like 4Add
BLAST
Repeati525 – 56541Gelsolin-like 5Add
BLAST
Repeati628 – 66942Gelsolin-like 6Add
BLAST
Domaini753 – 81967HPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 731731CoreBy similarityAdd
BLAST
Regioni109 – 1168Polyphosphoinositide bindingBy similarity
Regioni135 – 1439Polyphosphoinositide bindingBy similarity
Regioni732 – 81988HeadpieceBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated
Contains 6 gelsolin-like repeats.Curated
Contains 1 HP (headpiece) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiO88398.
KOiK08017.
OMAiPRHFMAM.
OrthoDBiEOG7288RJ.
TreeFamiTF313468.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR030014. Advillin.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF33. PTHR11977:SF33. 1 hit.
PfamiPF00626. Gelsolin. 6 hits.
PF02209. VHP. 1 hit.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
SM00153. VHP. 1 hit.
[Graphical view]
SUPFAMiSSF47050. SSF47050. 1 hit.
SSF82754. SSF82754. 1 hit.
PROSITEiPS51089. HP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88398-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSSAFRAV SNDPRIITWR IEKMELALVP LSAHGNFYEG DCYIVLSTRR
60 70 80 90 100
VGSLLSQNIH FWIGKDSSQD EQSCAAIYTT QLDDYLGGSP VQHREVQYHE
110 120 130 140 150
SDTFRGYFKQ GIIYKKGGVA SGMKHVETNT YDVKRLLHVK GKRNIQATEV
160 170 180 190 200
EMSWDSFNRG DVFLLDLGMV IIQWNGPESN SGERLKAMLL AKDIRDRERG
210 220 230 240 250
GRAEIGVIEG DKEAASPGLM TVLQDTLGRR SMIKPAVSDE IMDQQQKSSI
260 270 280 290 300
MLYHVSDTAG QLSVTEVATR PLVQDLLNHD DCYILDQSGT KIYVWKGKGA
310 320 330 340 350
TKVEKQAAMS KALDFIKMKG YPSSTNVETV NDGAESAMFK QLFQKWSVKD
360 370 380 390 400
QTTGLGKIFS TGKIAKIFQD KFDVSLLHTK PEVAAQERMV DDGKGQVEVW
410 420 430 440 450
RIENLELVPV EYQWHGFFYG GDCYLVLYTY DVNGKPHYIL YIWQGRHASR
460 470 480 490 500
DELAASAYRA VEVDQQFDGA PVQVRVSMGK EPRHFMAIFK GKLVIYEGGT
510 520 530 540 550
SRKGNEEPDP PVRLFQIHGN DKSNTKAVEV SASASSLNSN DVFLLRTQAE
560 570 580 590 600
HYLWYGKGSS GDERAMAKEL VDLLCDGNAD TVAEGQEPPE FWDLLGGKTA
610 620 630 640 650
YANDKRLQQE TLDVQVRLFE CSNKTGRFLV TEVTDFTQED LSPGDVMLLD
660 670 680 690 700
TWDQVFLWIG AEANATEKKG ALSTAQEYLV THPSGRDPDT PILIIKQGFE
710 720 730 740 750
PPTFTGWFLA WDPHIWSEGK SYEQLKNELG DATAIVRITA DMKNATLYLN
760 770 780 790 800
PSDGEPKYYP VEVLLKGQNQ ELPEDVDPAK KENYLSEQDF VSVFGITRGQ
810
FTALPGWKQL QLKKERGLF
Length:819
Mass (Da):92,032
Last modified:July 27, 2011 - v2
Checksum:i75C13F095A898876
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151R → G in AAC31808 (PubMed:9649432).Curated
Sequence conflicti469 – 4691G → R in AAC25050 (PubMed:9664034).Curated
Sequence conflicti538 – 5381N → I in AAC25050 (PubMed:9664034).Curated
Sequence conflicti809 – 8091Q → R in AAC25050 (PubMed:9664034).Curated
Sequence conflicti814 – 8141K → R in AAC25050 (PubMed:9664034).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041448 mRNA. Translation: AAC25050.1.
AF059486 mRNA. Translation: AAC31808.1.
AK154851 mRNA. Translation: BAE32877.1.
AK155900 mRNA. Translation: BAE33492.1.
CH466578 Genomic DNA. Translation: EDL24458.1.
BC120545 mRNA. Translation: AAI20546.1.
CCDSiCCDS24221.1.
RefSeqiNP_033765.2. NM_009635.3.
UniGeneiMm.10739.

Genome annotation databases

EnsembliENSMUST00000026500; ENSMUSP00000026500; ENSMUSG00000025432.
ENSMUST00000129173; ENSMUSP00000123405; ENSMUSG00000025432.
GeneIDi11567.
KEGGimmu:11567.
UCSCiuc007hhl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041448 mRNA. Translation: AAC25050.1.
AF059486 mRNA. Translation: AAC31808.1.
AK154851 mRNA. Translation: BAE32877.1.
AK155900 mRNA. Translation: BAE33492.1.
CH466578 Genomic DNA. Translation: EDL24458.1.
BC120545 mRNA. Translation: AAI20546.1.
CCDSiCCDS24221.1.
RefSeqiNP_033765.2. NM_009635.3.
UniGeneiMm.10739.

3D structure databases

ProteinModelPortaliO88398.
SMRiO88398. Positions 7-819.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198012. 2 interactions.
IntActiO88398. 1 interaction.
STRINGi10090.ENSMUSP00000026500.

PTM databases

iPTMnetiO88398.
PhosphoSiteiO88398.

Proteomic databases

MaxQBiO88398.
PaxDbiO88398.
PRIDEiO88398.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026500; ENSMUSP00000026500; ENSMUSG00000025432.
ENSMUST00000129173; ENSMUSP00000123405; ENSMUSG00000025432.
GeneIDi11567.
KEGGimmu:11567.
UCSCiuc007hhl.2. mouse.

Organism-specific databases

CTDi10677.
MGIiMGI:1333798. Avil.

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiO88398.
KOiK08017.
OMAiPRHFMAM.
OrthoDBiEOG7288RJ.
TreeFamiTF313468.

Miscellaneous databases

PROiO88398.
SOURCEiSearch...

Gene expression databases

BgeeiO88398.
CleanExiMM_AVIL.
ExpressionAtlasiO88398. baseline and differential.
GenevisibleiO88398. MM.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR030014. Advillin.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF33. PTHR11977:SF33. 1 hit.
PfamiPF00626. Gelsolin. 6 hits.
PF02209. VHP. 1 hit.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
SM00153. VHP. 1 hit.
[Graphical view]
SUPFAMiSSF47050. SSF47050. 1 hit.
SSF82754. SSF82754. 1 hit.
PROSITEiPS51089. HP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Advillin (p92): a new member of the gelsolin/villin family of actin regulatory proteins."
    Marks P.W., Arai M., Bandura J.L., Kwiatkowski D.J.
    J. Cell Sci. 111:2129-2136(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "Identification of novel stress-induced genes downstream of chop."
    Wang X.-Z., Kuroda M., Sok J., Batchvarova N., Kimmel R., Chung P., Zinszner H., Ron D.
    EMBO J. 17:3619-3630(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NIH Swiss.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "Type F scavenger receptor SREC-I interacts with advillin, a member of the gelsolin/villin family, and induces neurite-like outgrowth."
    Shibata M., Ishii J., Koizumi H., Shibata N., Dohmae N., Takio K., Adachi H., Tsujimoto M., Arai H.
    J. Biol. Chem. 279:40084-40090(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SCARF1, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-85; TYR-748 AND TYR-758, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  8. "Analyzing somatosensory axon projections with the sensory neuron-specific Advillin gene."
    Hasegawa H., Abbott S., Han B.X., Qi Y., Wang F.
    J. Neurosci. 27:14404-14414(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiAVIL_MOUSE
AccessioniPrimary (citable) accession number: O88398
Secondary accession number(s): O70466, Q3U1K5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.