TWF2_DANRE
ID TWF2_DANRE Reviewed; 347 AA.
AC Q6GMH3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Twinfilin-2;
DE AltName: Full=Twinfilin-1-like protein;
GN Name=twf2; Synonyms=ptk9l, twf1l; ORFNames=zgc:91817;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-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 and capping protein
CC (CP). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Note=Perinuclear and G-actin-rich
CC cortical actin structure sublocalization. {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; BC074077; AAH74077.1; -; mRNA.
DR RefSeq; NP_001009897.1; NM_001009897.2.
DR AlphaFoldDB; Q6GMH3; -.
DR SMR; Q6GMH3; -.
DR STRING; 7955.ENSDARP00000024168; -.
DR PaxDb; Q6GMH3; -.
DR Ensembl; ENSDART00000065006; ENSDARP00000065005; ENSDARG00000094792.
DR GeneID; 100310784; -.
DR KEGG; dre:100310784; -.
DR CTD; 11344; -.
DR ZFIN; ZDB-GENE-030131-7638; twf2a.
DR GeneTree; ENSGT00530000063868; -.
DR HOGENOM; CLU_031995_1_0_1; -.
DR InParanoid; Q6GMH3; -.
DR PhylomeDB; Q6GMH3; -.
DR TreeFam; TF352598; -.
DR PRO; PR:Q6GMH3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000094792; Expressed in muscle tissue and 14 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:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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..347
FT /note="Twinfilin-2"
FT /id="PRO_0000233140"
FT DOMAIN 3..137
FT /note="ADF-H 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 175..311
FT /note="ADF-H 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REGION 314..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 39859 MW; 948D3BCD3A0D7B21 CRC64;
MFLVLVVTEE LREFLARARN GTGRLIQVLI RDEQLVLGAY REPRHSWDKD YDPVLLPLLD
PLEPCYILYR LDSKNAQGYE WLFISWSPDQ SPVRQKMLYA ATRATVKKEF GGGHVKDEMF
GTVEEDICLQ GYLRHITSCS APAPLTVAEQ ELQRIKITEV KAEISVDPKH QTLQGLAFPL
QAEAKRALKQ LAERRINYIQ LKLDTEKETI DLVHTSPTDI RDLPCRIPLD TPRYHFFLYK
HSHEGDYLES VVFIYSMPGY SCSIKERMLY SSCKSRLLDE VERDFHLEVA KKLEIDSGEE
LTEEYLYDEV HPKQHAHKQA FAKPRGPAGK RGNKRLIKGG GENGGNS