ID   TWF1_PONAB              Reviewed;         350 AA.
AC   Q5R7N2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Twinfilin-1;
GN   Name=TWF1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-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 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; CR860082; CAH92228.1; -; mRNA.
DR   RefSeq; NP_001126303.1; NM_001132831.1.
DR   AlphaFoldDB; Q5R7N2; -.
DR   SMR; Q5R7N2; -.
DR   STRING; 9601.ENSPPYP00000005055; -.
DR   PRIDE; Q5R7N2; -.
DR   GeneID; 100173282; -.
DR   KEGG; pon:100173282; -.
DR   CTD; 5756; -.
DR   eggNOG; KOG1747; Eukaryota.
DR   InParanoid; Q5R7N2; -.
DR   OrthoDB; 1578109at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR   GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:InterPro.
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   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_0000232405"
FT   DOMAIN          2..139
FT                   /note="ADF-H 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   DOMAIN          175..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;  40195 MW;  47C2FEBD973D8770 CRC64;
     MSHRTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVIG SYSQPSDSWD KDYDSFVLPL
     LEDKQPCYIL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML YAATRATLKK EFGGGHIKDE
     VFGTVKEDVS LHGYKKYLLS QSSPAPLTAA EEELRQIKIN EVQTDVGVDT KHQTLQGVAF
     PISREAFQAL EKLNNRQLNY VQLEIDIKNE IIILANTTDT ELKDLPKRIP KDSARYHFFL
     YKHSHEGDYL ESIVFIYSMP GYTCSIRERM LYSSCKSPLL EIVERQLQMG VIRKIEIDNG
     DELTADFLYE EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAETEATTD