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O75366 (AVIL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Advillin
Alternative name(s):
p92
Gene names
Name:AVIL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length819 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

Associates (via C-terminus) with actin. Interacts with SCARF1 By similarity. Interacts with F-actin. Ref.8

Subcellular location

Cytoplasmcytoskeleton. Cell projection By similarity. Cell projectionaxon By similarity.

Tissue specificity

Most highly expressed in the small intestine and colonic lining. Weaker expression also detected in the thymus, prostate, testes and uterus. Ref.6

Sequence similarities

Belongs to the villin/gelsolin family.

Contains 6 gelsolin-like repeats.

Contains 1 HP (headpiece) domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75366-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O75366-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MPLTSAFRAVDNDPGIIVWRI → MSSTGHPGSYKIWG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 819819Advillin
PRO_0000218736

Regions

Repeat24 – 7350Gelsolin-like 1
Repeat145 – 18541Gelsolin-like 2
Repeat262 – 30645Gelsolin-like 3
Repeat403 – 45452Gelsolin-like 4
Repeat525 – 56541Gelsolin-like 5
Repeat628 – 66942Gelsolin-like 6
Domain753 – 81967HP
Region1 – 731731Core By similarity
Region109 – 1168Polyphosphoinositide binding By similarity
Region135 – 1439Polyphosphoinositide binding By similarity
Region731 – 81989Headpiece By similarity

Amino acid modifications

Modified residue851Phosphotyrosine By similarity
Modified residue7581Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 2121MPLTS…IVWRI → MSSTGHPGSYKIWG in isoform 2.
VSP_036961
Natural variant2041K → E. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs2172521 [ dbSNP | Ensembl ].
VAR_054974

Experimental info

Mutagenesis621W → A: Reduces interaction with F-actin. Ref.8
Sequence conflict4451G → D in AAC25051. Ref.1

Secondary structure

....... 819
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: F5EF3A94BA61E647

FASTA81992,027
        10         20         30         40         50         60 
MPLTSAFRAV DNDPGIIVWR IEKMELALVP VSAHGNFYEG DCYVILSTRR VASLLSQDIH 

        70         80         90        100        110        120 
FWIGKDSSQD EQSCAAIYTT QLDDYLGGSP VQHREVQYHE SDTFRGYFKQ GIIYKQGGVA 

       130        140        150        160        170        180 
SGMKHVETNT YDVKRLLHVK GKRNIRATEV EMSWDSFNRG DVFLLDLGKV IIQWNGPESN 

       190        200        210        220        230        240 
SGERLKAMLL AKDIRDRERG GRAKIGVIEG DKEAASPELM KVLQDTLGRR SIIKPTVPDE 

       250        260        270        280        290        300 
IIDQKQKSTI MLYHISDSAG QLAVTEVATR PLVQDLLNHD DCYILDQSGT KIYVWKGKGA 

       310        320        330        340        350        360 
TKAEKQAAMS KALGFIKMKS YPSSTNVETV NDGAESAMFK QLFQKWSVKD QTMGLGKTFS 

       370        380        390        400        410        420 
IGKIAKVFQD KFDVTLLHTK PEVAAQERMV DDGNGKVEVW RIENLELVPV EYQWYGFFYG 

       430        440        450        460        470        480 
GDCYLVLYTY EVNGKPHHIL YIWQGRHASQ DELAASAYQA VEVDRQFDGA AVQVRVRMGT 

       490        500        510        520        530        540 
EPRHFMAIFK GKLVIFEGGT SRKGNAEPDP PVRLFQIHGN DKSNTKAVEV PAFASSLNSN 

       550        560        570        580        590        600 
DVFLLRTQAE HYLWYGKGSS GDERAMAKEL ASLLCDGSEN TVAEGQEPAE FWDLLGGKTP 

       610        620        630        640        650        660 
YANDKRLQQE ILDVQSRLFE CSNKTGQFVV TEITDFTQDD LNPTDVMLLD TWDQVFLWIG 

       670        680        690        700        710        720 
AEANATEKES ALATAQQYLH THPSGRDPDT PILIIKQGFE PPIFTGWFLA WDPNIWSAGK 

       730        740        750        760        770        780 
TYEQLKEELG DAAAIMRITA DMKNATLSLN SNDSEPKYYP IAVLLKNQNQ ELPEDVNPAK 

       790        800        810 
KENYLSEQDF VSVFGITRGQ FAALPGWKQL QMKKEKGLF 

« Hide

Isoform 2 [UniParc].

Checksum: CAACCD7994F2D989
Show »

FASTA81291,163

References

« Hide 'large scale' references
[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] (ISOFORM 1), VARIANT GLU-204.
Tissue: Uterus.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-204.
Tissue: Brain.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-204.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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] (ISOFORM 2), VARIANT GLU-204.
[6]"Genomic structure, chromosome mapping and expression analysis of the human AVIL gene, and its exclusion as a candidate for locus for inflammatory bowel disease at 12q13-14 (IBD2)."
Tumer Z., Croucher P.J., Jensen L.R., Hampe J., Hansen C., Kalscheuer V., Ropers H.H., Tommerup N., Schreiber S.
Gene 288:179-185(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Functional genomic screen for modulators of ciliogenesis and cilium length."
Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements."
Vermeulen W., Vanhaesebrouck P., Van Troys M., Verschueren M., Fant F., Goethals M., Ampe C., Martins J.C., Borremans F.A.
Protein Sci. 13:1276-1287(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 784-819, INTERACTION WITH F-ACTIN, MUTAGENESIS OF TRP-62.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041449 mRNA. Translation: AAC25051.1.
AK314362 mRNA. Translation: BAG36994.1.
AC025165 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97080.1.
BC111730 mRNA. Translation: AAI11731.1.
RefSeqNP_006567.3. NM_006576.3.
UniGeneHs.584854.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UNDNMR-A784-819[»]
ProteinModelPortalO75366.
SMRO75366. Positions 7-722, 759-819.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115918. 3 interactions.
MINTMINT-4990440.
STRING9606.ENSP00000257861.

PTM databases

PhosphoSiteO75366.

Proteomic databases

PaxDbO75366.
PRIDEO75366.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257861; ENSP00000257861; ENSG00000135407. [O75366-1]
ENST00000537081; ENSP00000443207; ENSG00000135407. [O75366-2]
GeneID10677.
KEGGhsa:10677.
UCSCuc001sqj.2. human. [O75366-1]
uc009zqe.2. human. [O75366-2]

Organism-specific databases

CTD10677.
GeneCardsGC12M058191.
H-InvDBHIX0023233.
HGNCHGNC:14188. AVIL.
HPAHPA058864.
MIM613397. gene.
neXtProtNX_O75366.
PharmGKBPA38380.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304849.
HOGENOMHOG000233630.
HOVERGENHBG004183.
InParanoidO75366.
KOK08017.
OMACYVILST.
OrthoDBEOG7288RJ.
PhylomeDBO75366.
TreeFamTF313468.

Gene expression databases

ArrayExpressO75366.
BgeeO75366.
CleanExHS_AVIL.
GenevestigatorO75366.

Family and domain databases

Gene3D1.10.950.10. 1 hit.
InterProIPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERPTHR11977. PTHR11977. 1 hit.
PfamPF00626. Gelsolin. 6 hits.
PF02209. VHP. 1 hit.
[Graphical view]
PRINTSPR00597. GELSOLIN.
SMARTSM00262. GEL. 6 hits.
SM00153. VHP. 1 hit.
[Graphical view]
SUPFAMSSF47050. SSF47050. 1 hit.
PROSITEPS51089. HP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75366.
GenomeRNAi10677.
NextBio40597.
PROO75366.
SOURCESearch...

Entry information

Entry nameAVIL_HUMAN
AccessionPrimary (citable) accession number: O75366
Secondary accession number(s): B2RAU7, Q2NKM9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM