ID   TWF_ANOGA               Reviewed;         343 AA.
AC   Q7QG28;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Twinfilin;
GN   Name=twf; ORFNames=AGAP003716;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
CC   -!- FUNCTION: Actin-binding protein involved in motile and morphological
CC       processes. Inhibits actin polymerization, likely by sequestering G-
CC       actin (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with G-actin; ADP-actin form. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC       cell cortex {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. Twinfilin
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAAB01008844; EAA06058.2; -; Genomic_DNA.
DR   RefSeq; XP_310246.2; XM_310246.6.
DR   AlphaFoldDB; Q7QG28; -.
DR   SMR; Q7QG28; -.
DR   STRING; 7165.AGAP003716-PA; -.
DR   PaxDb; Q7QG28; -.
DR   GeneID; 3290886; -.
DR   KEGG; aga:AgaP_AGAP003716; -.
DR   CTD; 3290886; -.
DR   VEuPathDB; VectorBase:AGAP003716; -.
DR   eggNOG; KOG1747; Eukaryota.
DR   HOGENOM; CLU_031995_0_1_1; -.
DR   InParanoid; Q7QG28; -.
DR   OMA; VKKDWER; -.
DR   OrthoDB; 1578109at2759; -.
DR   PhylomeDB; Q7QG28; -.
DR   Proteomes; UP000007062; Chromosome 2R.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR   GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR   GO; GO:0010591; P:regulation of lamellipodium assembly; IBA:GO_Central.
DR   GO; GO:0042989; P:sequestering of actin monomers; IBA:GO_Central.
DR   Gene3D; 3.40.20.10; -; 2.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR028458; Twinfilin.
DR   PANTHER; PTHR13759; PTHR13759; 1.
DR   Pfam; PF00241; Cofilin_ADF; 2.
DR   SMART; SM00102; ADF; 2.
DR   PROSITE; PS51263; ADF_H; 2.
PE   3: Inferred from homology;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome; Repeat.
FT   CHAIN           1..343
FT                   /note="Twinfilin"
FT                   /id="PRO_0000308811"
FT   DOMAIN          4..139
FT                   /note="ADF-H 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   DOMAIN          177..312
FT                   /note="ADF-H 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   REGION          314..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   343 AA;  39282 MW;  1E0D9778D730353B CRC64;
     MSHQTGIKAN AELLKFFGKC KDGKTRVLKV SIENEELRLV SHSDVKRDWE KDYDTLVRPL
     IEESTPCYIL YRLDYKIPTG YAWLLMSWVP ESATVRQKML YASTKATLKL EFGSGHIKEE
     LNATSKEETT LQGYQKHKVD FNTPAPLTSR EEELAELRKT EVKTDFGIDT KQQTLGGINC
     PIADAVAQAL HDMRRGGYNY LQFRIDLEEE KIHLVKADNI ELTGLPAQIP TDHARYHLYI
     FKHHHEGNYL ESVVFVYSMP GYSCSIRERM MYSSCKGPFS ATIEKHGIQV AKKLEIDNGA
     ELTEEFLHEE LHPRKLNLRP QFSKPKGPPS RGAKRLTKPQ AVE