TWF1_YEAST
ID TWF1_YEAST Reviewed; 332 AA.
AC P53250; D6VUL2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Twinfilin-1;
DE AltName: Full=Twinfilin-A;
GN Name=TWF1; OrderedLocusNames=YGR080W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9700161; DOI=10.1083/jcb.142.3.723;
RA Goode B.L., Drubin D.G., Lappalainen P.;
RT "Regulation of the cortical actin cytoskeleton in budding yeast by
RT twinfilin, a ubiquitous actin monomer-sequestering protein.";
RL J. Cell Biol. 142:723-733(1998).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND SER-172, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Actin-binding protein involved in motile and morphological
CC processes. Inhibits actin polymerization, likely by sequestering G-
CC actin. Prevents actin filament assembly by forming a 1:1 complex with
CC actin monomers, and inhibits the nucleotide exchange reaction of actin
CC monomers (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with G-actin; ADP-actin form. {ECO:0000250}.
CC -!- INTERACTION:
CC P53250; P17555: SRV2; NbExp=3; IntAct=EBI-19663, EBI-4024;
CC P53250; P68135: ACTA1; Xeno; NbExp=5; IntAct=EBI-19663, EBI-367540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 1470 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. Twinfilin
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular embrace - Issue 73
CC of August 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/073";
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DR EMBL; Z72865; CAA97082.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08173.1; -; Genomic_DNA.
DR PIR; S64375; S64375.
DR RefSeq; NP_011594.3; NM_001181209.3.
DR AlphaFoldDB; P53250; -.
DR SMR; P53250; -.
DR BioGRID; 33322; 81.
DR DIP; DIP-2202N; -.
DR IntAct; P53250; 8.
DR MINT; P53250; -.
DR STRING; 4932.YGR080W; -.
DR iPTMnet; P53250; -.
DR MaxQB; P53250; -.
DR PaxDb; P53250; -.
DR PRIDE; P53250; -.
DR EnsemblFungi; YGR080W_mRNA; YGR080W; YGR080W.
DR GeneID; 852971; -.
DR KEGG; sce:YGR080W; -.
DR SGD; S000003312; TWF1.
DR VEuPathDB; FungiDB:YGR080W; -.
DR eggNOG; KOG1747; Eukaryota.
DR GeneTree; ENSGT00530000063868; -.
DR HOGENOM; CLU_031995_0_2_1; -.
DR InParanoid; P53250; -.
DR OMA; VKKDWER; -.
DR BioCyc; YEAST:G3O-30792-MON; -.
DR PRO; PR:P53250; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53250; protein.
DR GO; GO:0005884; C:actin filament; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0003785; F:actin monomer binding; IDA:SGD.
DR GO; GO:0044396; P:actin cortical patch organization; IMP:SGD.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:SGD.
DR GO; GO:0007015; P:actin filament organization; IDA:SGD.
DR GO; GO:0051014; P:actin filament severing; IDA:SGD.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IDA:SGD.
DR GO; GO:0042989; P:sequestering of actin monomers; IDA:SGD.
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; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..332
FT /note="Twinfilin-1"
FT /id="PRO_0000214953"
FT DOMAIN 5..132
FT /note="ADF-H 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 173..300
FT /note="ADF-H 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REGION 301..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 332 AA; 37071 MW; D9213BBB2D953DBD CRC64;
MSTQSGIVAE QALLHSLNEN LSADGIVIII AKISPDSTSV HQTQVARSFE ELVQLASQER
EPLYIFYKPE GLDKYFFVSF IPDGSPVRSR MLYASTKNTL ARQVGSNSLS TEQPLITDAQ
DLVDLKNFDS ARPAGQNKPL THDEEMQIEI NKQQALLRKN TSVKLVSQDS ASPLSLTFRV
NSEKPINEIL DSEGKNLIIF QIDPSNETIQ IVQSDTCPSV DELYIDLPGP SYTIFRQGDS
SFFIYSCPSG SKVKDRMIYA SNKNGFINYL KNDQKIAFSK VVEIGDFVEL DKSLLMATNK
EDSLDHGSNP DLPNKSNLKF NKPKGPLRKR RT
