TWF1_SCHPO
ID TWF1_SCHPO Reviewed; 328 AA.
AC O94399;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Twinfilin;
GN Name=twf1; ORFNames=SPCC126.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. Twinfilin
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAA22475.1; -; Genomic_DNA.
DR PIR; T40910; T40910.
DR RefSeq; NP_588449.1; NM_001023440.2.
DR AlphaFoldDB; O94399; -.
DR SMR; O94399; -.
DR BioGRID; 275636; 15.
DR STRING; 4896.SPCC126.06.1; -.
DR iPTMnet; O94399; -.
DR MaxQB; O94399; -.
DR PaxDb; O94399; -.
DR PRIDE; O94399; -.
DR EnsemblFungi; SPCC126.06.1; SPCC126.06.1:pep; SPCC126.06.
DR GeneID; 2539064; -.
DR KEGG; spo:SPCC126.06; -.
DR PomBase; SPCC126.06; twf1.
DR VEuPathDB; FungiDB:SPCC126.06; -.
DR eggNOG; KOG1747; Eukaryota.
DR HOGENOM; CLU_031995_0_1_1; -.
DR InParanoid; O94399; -.
DR OMA; VKKDWER; -.
DR PhylomeDB; O94399; -.
DR PRO; PR:O94399; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; ISO:PomBase.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:1904600; P:actin fusion focus assembly; IMP:PomBase.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0042989; P:sequestering of actin monomers; ISO:PomBase.
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..328
FT /note="Twinfilin"
FT /id="PRO_0000214952"
FT DOMAIN 1..137
FT /note="ADF-H 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 173..304
FT /note="ADF-H 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REGION 302..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 328 AA; 36781 MW; D07F7566404DE5FA CRC64;
MSASVELKPT EKFSKFLEEY SSVPVRAAII SISNENSFDV KTMVEKSESI ESDFKKVREC
LLGSEEPAFV LVYDDSKKNL LQLISYVPEN ANVRRKMLYA SSRAAFVRCV TLAKLDESYF
ASTPEELDYQ QIMKSLSKQE DQSPLRQDEL ERKEYNESMQ SSVTHKRPLV TRGVAMSIDD
KALKALSDLK SSTENNLVIL SIDKEVISLS QEKQNIPPSD VKSFFSSTEP NFAFYSLPKD
GSSKILFIYI CPMQATVKHR MVYSSSKLGL LDSIKAELGI VIDGKIESND AADITEKEIL
HAAGISSPQA ETSTTKTGFS RPRPPRRR
