O75366 (AVIL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Advillin

Alternative name(s):
p92

Gene names

Name:

AVIL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	819 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. Cell projection By similarity. Cell projection › axon 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.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Actin-binding Calcium
Molecular function	Actin capping
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament capping Inferred from electronic annotation. Source: UniProtKB-KW cilium morphogenesis Inferred from mutant phenotype Ref.7. Source: UniProtKB cytoskeleton organization Inferred from electronic annotation. Source: InterPro positive regulation of neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB response to stress Inferred from electronic annotation. Source: Compara
Cellular_component	actin cytoskeleton Traceable author statement Ref.1. Source: ProtInc axon Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW neuron projection Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	actin binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 819

819

Advillin

PRO_0000218736

Regions

Repeat

24 – 73

50

Gelsolin-like 1

Repeat

145 – 185

41

Gelsolin-like 2

Repeat

262 – 306

45

Gelsolin-like 3

Repeat

403 – 454

52

Gelsolin-like 4

Repeat

525 – 565

41

Gelsolin-like 5

Repeat

628 – 669

42

Gelsolin-like 6

Domain

753 – 819

67

HP

Region

1 – 731

731

Core By similarity

Region

109 – 116

8

Polyphosphoinositide binding By similarity

Region

135 – 143

9

Polyphosphoinositide binding By similarity

Region

731 – 819

89

Headpiece By similarity

Amino acid modifications

Modified residue

85

1

Phosphotyrosine By similarity

Modified residue

758

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

1 – 21

21

MPLTS…IVWRI → MSSTGHPGSYKIWG in isoform 2.

VSP_036961

Natural variant

204

1

K → E. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs2172521 [ dbSNP | Ensembl ].

VAR_054974

Experimental info

Mutagenesis

62

1

W → A: Reduces interaction with F-actin. Ref.8

Sequence conflict

445

1

G → D in AAC25051. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

819

Helix Strand Turn

Details...

Helix

787 – 794

8

Helix

798 – 803

6

Helix

806 – 817

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 30, 2010. Version 3. Checksum: F5EF3A94BA61E647	FASTA	819	92,027
	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
	Isoform 2 [UniParc]. Checksum: CAACCD7994F2D989	FASTA	812	91,163
	10 20 30 40 50 60 MSSTGHPGSY KIWGEKMELA LVPVSAHGNF YEGDCYVILS TRRVASLLSQ DIHFWIGKDS 70 80 90 100 110 120 SQDEQSCAAI YTTQLDDYLG GSPVQHREVQ YHESDTFRGY FKQGIIYKQG GVASGMKHVE 130 140 150 160 170 180 TNTYDVKRLL HVKGKRNIRA TEVEMSWDSF NRGDVFLLDL GKVIIQWNGP ESNSGERLKA 190 200 210 220 230 240 MLLAKDIRDR ERGGRAKIGV IEGDKEAASP ELMKVLQDTL GRRSIIKPTV PDEIIDQKQK 250 260 270 280 290 300 STIMLYHISD SAGQLAVTEV ATRPLVQDLL NHDDCYILDQ SGTKIYVWKG KGATKAEKQA 310 320 330 340 350 360 AMSKALGFIK MKSYPSSTNV ETVNDGAESA MFKQLFQKWS VKDQTMGLGK TFSIGKIAKV 370 380 390 400 410 420 FQDKFDVTLL HTKPEVAAQE RMVDDGNGKV EVWRIENLEL VPVEYQWYGF FYGGDCYLVL 430 440 450 460 470 480 YTYEVNGKPH HILYIWQGRH ASQDELAASA YQAVEVDRQF DGAAVQVRVR MGTEPRHFMA 490 500 510 520 530 540 IFKGKLVIFE GGTSRKGNAE PDPPVRLFQI HGNDKSNTKA VEVPAFASSL NSNDVFLLRT 550 560 570 580 590 600 QAEHYLWYGK GSSGDERAMA KELASLLCDG SENTVAEGQE PAEFWDLLGG KTPYANDKRL 610 620 630 640 650 660 QQEILDVQSR LFECSNKTGQ FVVTEITDFT QDDLNPTDVM LLDTWDQVFL WIGAEANATE 670 680 690 700 710 720 KESALATAQQ YLHTHPSGRD PDTPILIIKQ GFEPPIFTGW FLAWDPNIWS AGKTYEQLKE 730 740 750 760 770 780 ELGDAAAIMR ITADMKNATL SLNSNDSEPK YYPIAVLLKN QNQELPEDVN PAKKENYLSE 790 800 810 QDFVSVFGIT RGQFAALPGW KQLQMKKEKG LF

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

IPI

IPI00289330.
IPI00791035.

RefSeq

NP_006567.3. NM_006576.3.

UniGene

Hs.584854.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UND	NMR	-	A	784-819	[»]

ProteinModelPortal

O75366.

SMR

O75366. Positions 7-722, 759-819.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000257861.

PTM databases

PhosphoSite

O75366.

Proteomic databases

PaxDb

O75366.

PRIDE

O75366.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000257861; ENSP00000257861; ENSG00000135407.
ENST00000537081; ENSP00000443207; ENSG00000135407.

GeneID

10677.

KEGG

hsa:10677.

UCSC

uc001sqj.2. human.
uc009zqe.2. human.

Organism-specific databases

CTD

10677.

GeneCards

GC12M058191.

H-InvDB

HIX0023233.

HGNC

HGNC:14188. AVIL.

MIM

613397. gene.

neXtProt

NX_O75366.

PharmGKB

PA38380.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG304849.

HOGENOM

HOG000233630.

HOVERGEN

HBG004183.

InParanoid

O75366.

KO

K08017.

OMA

QLQMKKE.

OrthoDB

EOG45X7VG.

PhylomeDB

O75366.

Gene expression databases

ArrayExpress

O75366.

Bgee

O75366.

CleanEx

HS_AVIL.

Genevestigator

O75366.

GermOnline

ENSG00000135407. Homo sapiens.

Family and domain databases

Gene3D

1.10.950.10. 1 hit.

InterPro

IPR007123. Gelsolin_dom.
IPR015627. Villin.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]

PANTHER

PTHR11977. PTHR11977. 1 hit.
PTHR11977:SF15. PTHR11977:SF15. 1 hit.

Pfam

PF00626. Gelsolin. 6 hits.
PF02209. VHP. 1 hit.
[Graphical view]

PRINTS

PR00597. GELSOLIN.

SMART

SM00262. GEL. 6 hits.
SM00153. VHP. 1 hit.
[Graphical view]

SUPFAM

SSF47050. VHP. 1 hit.

PROSITE

PS51089. HP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O75366.

GenomeRNAi

10677.

NextBio

40597.

SOURCE

Search...

Entry information

Entry name

AVIL_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.