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TWF_DROME
ID   TWF_DROME               Reviewed;         343 AA.
AC   Q9VFM9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Twinfilin;
GN   Name=twf; ORFNames=CG3172;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ACTIN, SUBCELLULAR
RP   LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=11724820; DOI=10.1083/jcb.200108022;
RA   Wahlstroem G., Vartiainen M., Yamamoto L., Mattila P.K., Lappalainen P.,
RA   Heino T.I.;
RT   "Twinfilin is required for actin-dependent developmental processes in
RT   Drosophila.";
RL   J. Cell Biol. 155:787-795(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Actin-binding protein involved in motile and morphological
CC       processes. Inhibits actin polymerization, likely by sequestering G-
CC       actin. {ECO:0000269|PubMed:11724820}.
CC   -!- SUBUNIT: Interacts with G-actin; ADP-actin form.
CC       {ECO:0000269|PubMed:11724820}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:11724820}. Cytoplasm, cell cortex
CC       {ECO:0000269|PubMed:11724820}.
CC   -!- DEVELOPMENTAL STAGE: Maternally expressed. Ubiquitously expressed in
CC       embryos and throughout development. {ECO:0000269|PubMed:11724820}.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. Twinfilin
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ430055; CAD22537.1; -; mRNA.
DR   EMBL; AE014297; AAF55022.1; -; Genomic_DNA.
DR   EMBL; AY069613; AAL39758.1; -; mRNA.
DR   RefSeq; NP_650338.1; NM_142081.4.
DR   AlphaFoldDB; Q9VFM9; -.
DR   SMR; Q9VFM9; -.
DR   BioGRID; 66796; 2.
DR   STRING; 7227.FBpp0082352; -.
DR   PaxDb; Q9VFM9; -.
DR   PRIDE; Q9VFM9; -.
DR   DNASU; 41719; -.
DR   EnsemblMetazoa; FBtr0082891; FBpp0082352; FBgn0038206.
DR   GeneID; 41719; -.
DR   KEGG; dme:Dmel_CG3172; -.
DR   UCSC; CG3172-RA; d. melanogaster.
DR   CTD; 41719; -.
DR   FlyBase; FBgn0038206; twf.
DR   VEuPathDB; VectorBase:FBgn0038206; -.
DR   eggNOG; KOG1747; Eukaryota.
DR   GeneTree; ENSGT00530000063868; -.
DR   HOGENOM; CLU_031995_0_1_1; -.
DR   InParanoid; Q9VFM9; -.
DR   OMA; VKKDWER; -.
DR   OrthoDB; 1578109at2759; -.
DR   PhylomeDB; Q9VFM9; -.
DR   Reactome; R-DME-9013418; RHOBTB2 GTPase cycle.
DR   BioGRID-ORCS; 41719; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 41719; -.
DR   PRO; PR:Q9VFM9; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0038206; Expressed in embryonic/larval hemocyte (Drosophila) and 25 other tissues.
DR   Genevisible; Q9VFM9; DM.
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; IDA:UniProtKB.
DR   GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0003779; F:actin binding; IMP:UniProtKB.
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; IDA:FlyBase.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR   GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR   GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
DR   GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR   GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:CACAO.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IMP:UniProtKB.
DR   GO; GO:0010591; P:regulation of lamellipodium assembly; IMP:FlyBase.
DR   GO; GO:0042989; P:sequestering of actin monomers; IBA:GO_Central.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:FlyBase.
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   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome; Repeat.
FT   CHAIN           1..343
FT                   /note="Twinfilin"
FT                   /id="PRO_0000308812"
FT   DOMAIN          11..135
FT                   /note="ADF-H 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   DOMAIN          184..312
FT                   /note="ADF-H 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   REGION          319..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   343 AA;  39070 MW;  A6B7046EA5BC4A86 CRC64;
     MSHQTGIRAN EQLAKVFGKA KNGKFRVIKV SIENEQLSCG ATAETKKDWE RDYDKLIGPL
     LEKDVPCYIL YRLDAKIPLG YSWLLISWTP DTASIRQKMV YASTKATLKT EFGSAYITEE
     LHATTLDECT LEGYRRHKQD FAAPAPLTSR EEELKELRKT EVHTEINTNT RHQTLGGINC
     PLSEATVAAV QDLVRGKHDY LQFRIDLEEE QIHVSRAAKV ELADLPKQVP EDHARYHLFL
     FRHTHEGDYF ESYVFVYSMP GYSCSVRERM MYSSCKAPFL DELAALGVEV VKKLEIDSGS
     ELTEAFLQDE LHPKKILHRP AFAKPKGPPN RGAKRLTRPT AED
 
 
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