AVIL_RAT
ID AVIL_RAT Reviewed; 819 AA.
AC Q9WU06; M0RCA6;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Advillin {ECO:0000305};
DE AltName: Full=Peripheral nervous system villin-like protein;
DE Short=Pervin {ECO:0000303|PubMed:11849295};
GN Name=Avil {ECO:0000312|RGD:620301};
GN Synonyms=Advil, Pervin {ECO:0000303|PubMed:11849295};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ASSOCIATION WITH ACTIN, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral nerve;
RX PubMed=11849295; DOI=10.1046/j.0953-816x.2001.01862.x;
RA Ravenall S.J., Gavazzi I., Wood J.N., Akopian A.N.;
RT "A peripheral nervous system actin-binding protein regulates neurite
RT outgrowth.";
RL Eur. J. Neurosci. 15:281-290(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=29058690; DOI=10.1172/jci94138;
RA Rao J., Ashraf S., Tan W., van der Ven A.T., Gee H.Y., Braun D.A.,
RA Feher K., George S.P., Esmaeilniakooshkghazi A., Choi W.I.,
RA Jobst-Schwan T., Schneider R., Schmidt J.M., Widmeier E., Warejko J.K.,
RA Hermle T., Schapiro D., Lovric S., Shril S., Daga A., Nayir A., Shenoy M.,
RA Tse Y., Bald M., Helmchen U., Mir S., Berdeli A., Kari J.A., El Desoky S.,
RA Soliman N.A., Bagga A., Mane S., Jairajpuri M.A., Lifton R.P., Khurana S.,
RA Martins J.C., Hildebrandt F.;
RT "Advillin acts upstream of phospholipase C 1 in steroid-resistant nephrotic
RT syndrome.";
RL J. Clin. Invest. 127:4257-4269(2017).
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 (PubMed:11849295). Involved in the
CC formation of long fine actin-containing filopodia-like structures in
CC fibroblast. Plays a role in ciliogenesis. In podocytes, controls
CC 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:11849295}.
CC -!- SUBUNIT: Associates (via C-terminus) with actin (PubMed:11849295).
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 (By similarity). 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:O88398, ECO:0000269|PubMed:11849295}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11849295}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:11849295}. Cell projection, axon
CC {ECO:0000269|PubMed:11849295}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:O75366}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:O75366}. 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: Expressed in dorsal root ganglion (DRG) neurons and
CC superior cervical ganglia (SCG) (PubMed:11849295). Expressed in
CC podocytes (PubMed:29058690). {ECO:0000269|PubMed:11849295,
CC ECO:0000269|PubMed:29058690}.
CC -!- DOMAIN: The C-terminal domain is necessary for the induction of long
CC fine actin-containing filopodia-like structures in fibroblast and
CC neurite-like outgrowth.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; AF099929; AAD22523.1; -; mRNA.
DR EMBL; AABR07057421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473950; EDM16510.1; -; Genomic_DNA.
DR RefSeq; NP_077377.2; NM_024401.2.
DR AlphaFoldDB; Q9WU06; -.
DR SMR; Q9WU06; -.
DR STRING; 10116.ENSRNOP00000067218; -.
DR PaxDb; Q9WU06; -.
DR PRIDE; Q9WU06; -.
DR Ensembl; ENSRNOT00000073237; ENSRNOP00000067218; ENSRNOG00000050419.
DR GeneID; 79253; -.
DR KEGG; rno:79253; -.
DR CTD; 10677; -.
DR RGD; 620301; Avil.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000159587; -.
DR HOGENOM; CLU_002568_3_1_1; -.
DR InParanoid; Q9WU06; -.
DR OMA; DPNIWSA; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; Q9WU06; -.
DR PRO; PR:Q9WU06; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000050419; Expressed in duodenum and 19 other tissues.
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; IDA: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; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA: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; IDA:RGD.
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; 2.
DR PROSITE; PS51089; HP; 1.
PE 2: Evidence at transcript 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_0000407313"
FT REPEAT 24..105
FT /note="Gelsolin-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 144..215
FT /note="Gelsolin-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 265..339
FT /note="Gelsolin-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 407..486
FT /note="Gelsolin-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 524..592
FT /note="Gelsolin-like 5"
FT /evidence="ECO:0000255"
FT REPEAT 631..704
FT /note="Gelsolin-like 6"
FT /evidence="ECO:0000255"
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 731..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:0000250|UniProtKB:O88398"
FT MOD_RES 758
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88398"
FT CONFLICT 129..130
FT /note="NT -> FS (in Ref. 1; AAD22523)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="R -> G (in Ref. 1; AAD22523)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="D -> S (in Ref. 1; AAD22523)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="G -> R (in Ref. 1; AAD22523)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="G -> P (in Ref. 1; AAD22523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 819 AA; 91894 MW; CA0285657B4D6A64 CRC64;
MSLSSAFRTV TNDPGIITWR IEKMELVLVP LSAHGNFYEG DCYIILSTRR VGSLLSQNIH
FWIGKDSSQD EQSCAAIYTT QLDDYLGGSP VQHREVQYHE SDTFRGYFKR GIIYKKGGVA
SGMKHVETNT YDVKRLLHVK GKRNIRATEV EMSWDSFNQG DVFLLDLGMV IIQWNGPESN
SGERLKAMLL AKDIRDRERG GRAEIGVIEG DKEAASPELM TVLQNTLGRR SIIKPAVPDE
VTDQQQKSTI MLYHVSDTTG QLSVTEVATR PLVQELLNHD DCYILDQSGT KIYVWKGKGA
TKVEKQAAMS KALDFIKMKG YPSSTNVETV NDGAESAMFK QLFQKWSVKD QTTGLGKTFS
IGKIAKIFQD KFDVTLLHTK PEVAAQERMV DDGNGKVEVW RIENLELVPV EYQWHGFFYG
GDCYLVLYTY DVNGKPCYIL YIWQGRHASQ DELAASAYQA VEVDQQFGGA PVQVRVSMGK
EPRHFMAIFK GKLVIYEGGT SRKGNVEPDP PVRLFQIHGN DKSNTKAVEV SASASSLNSN
DVFLLWTQAE HYLWYGKGSS GDERAMAKEL AELLCDGDAD TVAEGQEPPE FWDLLGGKAP
YANDKRLQQE TLDIQVRLFE CSNKTGRFLV TEVTDFTQDD LSPGDVMLLD TWDQVFLWIG
AEANATEKEG ALSTAQEYLV THPSGRDPDT PILIIKQGFE PPTFTGWFLA WDPHIWSEGK
SYEQLKNELG DATAIVRITT DMKNATLSLN SSESGPKYYP VEVLLKSQDQ ELPEDVDPTK
KENYLSERDF VSVFGITRGQ FVSLPGWKQL QLKKEAGLF
