ID   TWF2_PONAB              Reviewed;         341 AA.
AC   Q5RFH1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Twinfilin-2;
DE   Flags: Fragment;
GN   Name=TWF2;
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=Heart;
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. May play a role
CC       in regulating the mature length of the middle and short rows of
CC       stereocilia (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with G-actin; ADP-actin form and capping protein
CC       (CP). May also be able to interact with TWF1 and phosphoinositides,
CC       PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated. Interacts
CC       with MYO7A (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC       perinuclear region {ECO:0000250}. Cell projection, stereocilium
CC       {ECO:0000250}. Note=Perinuclear and G-actin-rich cortical actin
CC       structure sublocalization. {ECO:0000250}.
CC   -!- PTM: Phosphorylated on both serine and threonine residues.
CC       {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; CR857187; CAH89486.1; -; Transcribed_RNA.
DR   AlphaFoldDB; Q5RFH1; -.
DR   SMR; Q5RFH1; -.
DR   STRING; 9601.ENSPPYP00000015459; -.
DR   eggNOG; KOG1747; Eukaryota.
DR   InParanoid; Q5RFH1; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Acetylation; Actin-binding; Cell projection; Cilium biogenesis/degradation;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           <1..341
FT                   /note="Twinfilin-2"
FT                   /id="PRO_0000233138"
FT   DOMAIN          <1..131
FT                   /note="ADF-H 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   DOMAIN          169..305
FT                   /note="ADF-H 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   REGION          314..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IBS0"
FT   MOD_RES         301
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IBS0"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IBS0"
FT   NON_TER         1
SQ   SEQUENCE   341 AA;  38707 MW;  98C5E459EB3413A5 CRC64;
     ATEELKEFFA KARAGSVRLI KVVIEDEQLV LGASQEPVGR WDRDYDRAVL PLLDAQQPCY
     LLYRLDSQNA QGFEWLFLAW SPDNSPVRLK MLYAATRATV KKEFGGGHIK DELFGTVKDD
     LSFAGYQKHL SSCAAPAPLT SAERELQQIR INEVKTEISV ESKHQTLQGL AFPLQPEAQR
     ALQQLKQKMV NYIQMKLDLE RETIELVHTE STDVAQLPSR VPRDAARYHF FLYKHTHEGD
     LLESVVFIYS MPGYKCSIEE RMLYSSCKSR LLDSVEQDFH LEIAKKIEIG DGAELTAEFL
     YDEVHPKQHA FKQAFAKPKG PGGKRGHKRL IRGPGENGDD S