ID   TWF1_XENTR              Reviewed;         350 AA.
AC   Q5I082;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Twinfilin-1;
GN   Name=twf1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC088597; AAH88597.1; -; mRNA.
DR   RefSeq; NP_001011469.1; NM_001011469.1.
DR   AlphaFoldDB; Q5I082; -.
DR   SMR; Q5I082; -.
DR   STRING; 8364.ENSXETP00000060892; -.
DR   PaxDb; Q5I082; -.
DR   Ensembl; ENSXETT00000014895; ENSXETP00000014895; ENSXETG00000026830.
DR   GeneID; 496960; -.
DR   KEGG; xtr:496960; -.
DR   CTD; 5756; -.
DR   Xenbase; XB-GENE-489056; twf1.
DR   eggNOG; KOG1747; Eukaryota.
DR   HOGENOM; CLU_031995_1_0_1; -.
DR   InParanoid; Q5I082; -.
DR   OrthoDB; 1578109at2759; -.
DR   PhylomeDB; Q5I082; -.
DR   Reactome; R-XTR-9013418; RHOBTB2 GTPase cycle.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000026830; Expressed in ovary and 15 other tissues.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome; Repeat.
FT   CHAIN           1..350
FT                   /note="Twinfilin-1"
FT                   /id="PRO_0000232408"
FT   DOMAIN          4..139
FT                   /note="ADF-H 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   DOMAIN          177..313
FT                   /note="ADF-H 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   REGION          316..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   350 AA;  40350 MW;  14DB0BF4821C7AD5 CRC64;
     MSHQTGIQAS EDVLEMFARA RNGKYRLLKL DIEDEQLTVT ACEKPASSWE QEYDSLILPL
     LEDKQPCYIM YRLDSQNAQG FEWIFIAWSP DHSHVRQKML YAATRATVKK EFGGGHIKEE
     LFGTVKDDIS LKGYYKYLAC QSSPAPLTMA EEELRQIKIK ETQVDIGVDT KHQTLQGIAF
     PIEKAAFQAL EQLREKRLNY VQLKIDIKNE TIILADTTNT EVRDLPKRIP KDAARYHFFL
     YKHSHEGDYL DSFVFIYSMP GYTCSIRERM LYSSCKSPLL DVIENRLLME IARKIEIDNG
     DELTPDFLYE EVHPKQHAHK QNFAKPKGPA GKRGIRRLIR GPAEAETAND