AVIL_MOUSE
ID AVIL_MOUSE Reviewed; 819 AA.
AC O88398; O70466; Q3U1K5;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Advillin {ECO:0000305};
DE AltName: Full=Actin-binding protein DOC6;
DE AltName: Full=p92;
GN Name=Avil {ECO:0000312|MGI:MGI:1333798}; Synonyms=Advil;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9664034; DOI=10.1242/jcs.111.15.2129;
RA Marks P.W., Arai M., Bandura J.L., Kwiatkowski D.J.;
RT "Advillin (p92): a new member of the gelsolin/villin family of actin
RT regulatory proteins.";
RL J. Cell Sci. 111:2129-2136(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NIH Swiss;
RX PubMed=9649432; DOI=10.1093/emboj/17.13.3619;
RA Wang X.-Z., Kuroda M., Sok J., Batchvarova N., Kimmel R., Chung P.,
RA Zinszner H., Ron D.;
RT "Identification of novel stress-induced genes downstream of chop.";
RL EMBO J. 17:3619-3630(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, INTERACTION WITH SCARF1, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15247299; DOI=10.1074/jbc.m403844200;
RA Shibata M., Ishii J., Koizumi H., Shibata N., Dohmae N., Takio K.,
RA Adachi H., Tsujimoto M., Arai H.;
RT "Type F scavenger receptor SREC-I interacts with advillin, a member of the
RT gelsolin/villin family, and induces neurite-like outgrowth.";
RL J. Biol. Chem. 279:40084-40090(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-85; TYR-748 AND TYR-758, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18160648; DOI=10.1523/jneurosci.4908-07.2007;
RA Hasegawa H., Abbott S., Han B.X., Qi Y., Wang F.;
RT "Analyzing somatosensory axon projections with the sensory neuron-specific
RT Advillin gene.";
RL J. Neurosci. 27:14404-14414(2007).
CC -!- FUNCTION: Ca(2+)-regulated actin-binding protein which plays an
CC important role in actin bundling. May have a unique function in the
CC morphogenesis of neuronal cells which form ganglia. Required for SREC1-
CC mediated regulation of neurite-like outgrowth. Plays a role in
CC regenerative sensory axon outgrowth and remodeling processes after
CC peripheral injury in neonates. Involved in the formation of long fine
CC actin-containing filopodia-like structures in fibroblast. Plays a role
CC in ciliogenesis (PubMed:15247299, PubMed:18160648). In podocytes,
CC controls lamellipodia formation through the regulation of EGF-induced
CC diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (By
CC similarity). {ECO:0000250|UniProtKB:O75366,
CC ECO:0000269|PubMed:15247299, ECO:0000269|PubMed:18160648}.
CC -!- SUBUNIT: Associates (via C-terminus) with actin (By similarity).
CC Interacts with F-actin (By similarity). Interacts with SCARF1; the
CC interaction occurs in embryonic dorsal root ganglions at 18 dpc and
CC induces neurite-like outgrowth (PubMed:15247299). Interacts with PLCE1.
CC Interacts with ACTR2 and ACTR3; associates with the ARP2/3 complex (By
CC similarity). {ECO:0000250|UniProtKB:O75366,
CC ECO:0000250|UniProtKB:Q9WU06, ECO:0000269|PubMed:15247299}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O75366}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:O75366}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:O75366}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q9WU06}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9WU06}. Note=In podocytes, present in the F-
CC actin-enriched cell periphery that generates lamellipodia and focal
CC adhesions. {ECO:0000250|UniProtKB:O75366}.
CC -!- TISSUE SPECIFICITY: Most highly expressed in the endometrium of the
CC uterus, the intestinal villi and the testes. Weaker expression also
CC detected in the brain, dorsal root ganglions and on the surface of the
CC tongue. {ECO:0000269|PubMed:15247299, ECO:0000269|PubMed:18160648,
CC ECO:0000269|PubMed:9664034}.
CC -!- DEVELOPMENTAL STAGE: Expressed almost exclusively in peripheral sensory
CC neurons (craniofacial and dorsal root ganglia (DRG) sensory neurons),
CC but also in trigeminal ganglia (TG) Me5 proprioceptive neurons and Mo5
CC motoneurons. {ECO:0000269|PubMed:15247299,
CC ECO:0000269|PubMed:18160648}.
CC -!- DISRUPTION PHENOTYPE: Half of the homozygous mice die during
CC embryogenesis, the other 50% do not show any noticeable abnormality in
CC development, growth or behavior and are fertile.
CC {ECO:0000269|PubMed:18160648}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; AF041448; AAC25050.1; -; mRNA.
DR EMBL; AF059486; AAC31808.1; -; mRNA.
DR EMBL; AK154851; BAE32877.1; -; mRNA.
DR EMBL; AK155900; BAE33492.1; -; mRNA.
DR EMBL; CH466578; EDL24458.1; -; Genomic_DNA.
DR EMBL; BC120545; AAI20546.1; -; mRNA.
DR CCDS; CCDS24221.1; -.
DR RefSeq; NP_033765.2; NM_009635.3.
DR AlphaFoldDB; O88398; -.
DR SMR; O88398; -.
DR BioGRID; 198012; 5.
DR IntAct; O88398; 1.
DR STRING; 10090.ENSMUSP00000026500; -.
DR iPTMnet; O88398; -.
DR PhosphoSitePlus; O88398; -.
DR MaxQB; O88398; -.
DR PaxDb; O88398; -.
DR PeptideAtlas; O88398; -.
DR PRIDE; O88398; -.
DR ProteomicsDB; 277233; -.
DR Antibodypedia; 28969; 145 antibodies from 21 providers.
DR DNASU; 11567; -.
DR Ensembl; ENSMUST00000026500; ENSMUSP00000026500; ENSMUSG00000025432.
DR Ensembl; ENSMUST00000129173; ENSMUSP00000123405; ENSMUSG00000025432.
DR GeneID; 11567; -.
DR KEGG; mmu:11567; -.
DR UCSC; uc007hhl.2; mouse.
DR CTD; 10677; -.
DR MGI; MGI:1333798; Avil.
DR VEuPathDB; HostDB:ENSMUSG00000025432; -.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000159587; -.
DR HOGENOM; CLU_002568_3_1_1; -.
DR InParanoid; O88398; -.
DR OMA; DPNIWSA; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; O88398; -.
DR TreeFam; TF313468; -.
DR BioGRID-ORCS; 11567; 1 hit in 71 CRISPR screens.
DR PRO; PR:O88398; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O88398; protein.
DR Bgee; ENSMUSG00000025432; Expressed in pyloric antrum and 104 other tissues.
DR ExpressionAtlas; O88398; baseline and differential.
DR Genevisible; O88398; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0071933; F:Arp2/3 complex binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:1900480; P:regulation of diacylglycerol biosynthetic process; ISS:UniProtKB.
DR Gene3D; 1.10.950.10; -; 1.
DR Gene3D; 3.40.20.10; -; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR007122; Villin/Gelsolin.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR Pfam; PF02209; VHP; 1.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF47050; SSF47050; 1.
DR SUPFAM; SSF82754; SSF82754; 1.
DR PROSITE; PS51089; HP; 1.
PE 1: Evidence at protein level;
KW Actin capping; Actin-binding; Calcium; Cell junction; Cell projection;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..819
FT /note="Advillin"
FT /id="PRO_0000218737"
FT REPEAT 24..73
FT /note="Gelsolin-like 1"
FT REPEAT 145..185
FT /note="Gelsolin-like 2"
FT REPEAT 262..306
FT /note="Gelsolin-like 3"
FT REPEAT 403..454
FT /note="Gelsolin-like 4"
FT REPEAT 525..565
FT /note="Gelsolin-like 5"
FT REPEAT 628..669
FT /note="Gelsolin-like 6"
FT DOMAIN 753..819
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 1..731
FT /note="Core"
FT /evidence="ECO:0000250"
FT REGION 628..819
FT /note="Required for interaction with F-actin"
FT /evidence="ECO:0000250|UniProtKB:O75366"
FT REGION 732..819
FT /note="Headpiece"
FT /evidence="ECO:0000250"
FT BINDING 109..116
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 135..143
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 748
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 758
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT CONFLICT 15
FT /note="R -> G (in Ref. 2; AAC31808)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="G -> R (in Ref. 1; AAC25050)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="N -> I (in Ref. 1; AAC25050)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="Q -> R (in Ref. 1; AAC25050)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="K -> R (in Ref. 1; AAC25050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 819 AA; 92032 MW; 75C13F095A898876 CRC64;
MSLSSAFRAV SNDPRIITWR IEKMELALVP LSAHGNFYEG DCYIVLSTRR VGSLLSQNIH
FWIGKDSSQD EQSCAAIYTT QLDDYLGGSP VQHREVQYHE SDTFRGYFKQ GIIYKKGGVA
SGMKHVETNT YDVKRLLHVK GKRNIQATEV EMSWDSFNRG DVFLLDLGMV IIQWNGPESN
SGERLKAMLL AKDIRDRERG GRAEIGVIEG DKEAASPGLM TVLQDTLGRR SMIKPAVSDE
IMDQQQKSSI MLYHVSDTAG QLSVTEVATR PLVQDLLNHD DCYILDQSGT KIYVWKGKGA
TKVEKQAAMS KALDFIKMKG YPSSTNVETV NDGAESAMFK QLFQKWSVKD QTTGLGKIFS
TGKIAKIFQD KFDVSLLHTK PEVAAQERMV DDGKGQVEVW RIENLELVPV EYQWHGFFYG
GDCYLVLYTY DVNGKPHYIL YIWQGRHASR DELAASAYRA VEVDQQFDGA PVQVRVSMGK
EPRHFMAIFK GKLVIYEGGT SRKGNEEPDP PVRLFQIHGN DKSNTKAVEV SASASSLNSN
DVFLLRTQAE HYLWYGKGSS GDERAMAKEL VDLLCDGNAD TVAEGQEPPE FWDLLGGKTA
YANDKRLQQE TLDVQVRLFE CSNKTGRFLV TEVTDFTQED LSPGDVMLLD TWDQVFLWIG
AEANATEKKG ALSTAQEYLV THPSGRDPDT PILIIKQGFE PPTFTGWFLA WDPHIWSEGK
SYEQLKNELG DATAIVRITA DMKNATLYLN PSDGEPKYYP VEVLLKGQNQ ELPEDVDPAK
KENYLSEQDF VSVFGITRGQ FTALPGWKQL QLKKERGLF
