ID   TWF1_BOVIN              Reviewed;         350 AA.
AC   Q56JV6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 103.
DE   RecName: Full=Twinfilin-1;
GN   Name=TWF1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymphoid epithelium;
RA   Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT   "Analysis of sequences obtained from constructed full-length bovine cDNA
RT   libraries.";
RL   Submitted (JAN-2005) 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 capping the barbed ends of filaments, it also regulates
CC       motility. Seems to play an important role in clathrin-mediated
CC       endocytosis and distribution of endocytic organelles (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with G-actin; ADP-actin form and capping protein
CC       (CP). May also be able to interact with TWF2 and phosphoinositides,
CC       PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated. Interacts
CC       with ACTG1. {ECO:0000250|UniProtKB:Q12792,
CC       ECO:0000250|UniProtKB:Q91YR1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}.
CC       Note=Diffuse cytoplasmic localization with perinuclear and G-actin-rich
CC       cortical actin structures sublocalization. Also found at membrane
CC       ruffles and cell-cell contacts (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated on serine and threonine residues. {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";
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DR   EMBL; AY911376; AAW82139.1; -; mRNA.
DR   RefSeq; NP_001020491.1; NM_001025320.2.
DR   AlphaFoldDB; Q56JV6; -.
DR   SMR; Q56JV6; -.
DR   STRING; 9913.ENSBTAP00000070174; -.
DR   PaxDb; 9913-ENSBTAP00000027889; -.
DR   GeneID; 506683; -.
DR   KEGG; bta:506683; -.
DR   CTD; 5756; -.
DR   eggNOG; KOG1747; Eukaryota.
DR   HOGENOM; CLU_031995_1_0_1; -.
DR   InParanoid; Q56JV6; -.
DR   OrthoDB; 5360875at2759; -.
DR   TreeFam; TF352598; -.
DR   Proteomes; UP000009136; Unplaced.
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:0003779; F:actin binding; ISS: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; 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   CDD; cd11284; ADF_Twf-C_like; 1.
DR   CDD; cd11285; ADF_Twf-N_like; 1.
DR   Gene3D; 3.40.20.10; Severin; 2.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR028458; Twinfilin.
DR   PANTHER; PTHR13759; TWINFILIN; 1.
DR   PANTHER; PTHR13759:SF8; TWINFILIN-1; 1.
DR   Pfam; PF00241; Cofilin_ADF; 2.
DR   SMART; SM00102; ADF; 2.
DR   SUPFAM; SSF55753; Actin depolymerizing proteins; 2.
DR   PROSITE; PS51263; ADF_H; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q12792"
FT   CHAIN           2..350
FT                   /note="Twinfilin-1"
FT                   /id="PRO_0000232404"
FT   DOMAIN          2..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"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12792"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12792"
FT   MOD_RES         277
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJR2"
FT   MOD_RES         309
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12792"
FT   MOD_RES         349
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12792"
SQ   SEQUENCE   350 AA;  40249 MW;  EFEFC1E0DC21E7A3 CRC64;
     MSHQTGIQAS EDVKDIFARA RNGKYRLLKI SIENEKLVIG SCRKPSDSWD QDYDSFVLPL
     LEDKQPCYVL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML YAATRATLKK EFGGGHIKDE
     MFGTVKEDVS LHGYKKYLLS QSSPAPLTAA EEELRQIKIN EVQTDVSVDA KHQTLQGVAF
     PISQEAFQAL EKLNNRQLNY VQLEIDIKNE IIILANTINT ELKDLPKRIP KDAARYHFFL
     YKHSHEGDYL ESIVFIYSMP GYTCSIRERM LYSSCKSPLL EIVERQLQMD IIRKIEIDNG
     DELTADFLYE EVHPKQHAHK QSFAKPKGPS GKRGIRRIIR GPAETEATTE
//