ID TWF2_CHICK Reviewed; 349 AA. AC Q5ZM35; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 24-JAN-2024, entry version 96. DE RecName: Full=Twinfilin-2; GN Name=TWF2; ORFNames=RCJMB04_3e19; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., RA Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:R6.1-R6.9(2005). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cochlea; RX PubMed=19955359; DOI=10.1523/jneurosci.2782-09.2009; RA Peng A.W., Belyantseva I.A., Hsu P.D., Friedman T.B., Heller S.; RT "Twinfilin 2 regulates actin filament lengths in cochlear stereocilia."; RL J. Neurosci. 29:15083-15088(2009). 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"; 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; AJ719549; CAG31208.1; -; mRNA. DR RefSeq; NP_001025760.1; NM_001030589.1. DR AlphaFoldDB; Q5ZM35; -. DR SMR; Q5ZM35; -. DR STRING; 9031.ENSGALP00000052343; -. DR PaxDb; 9031-ENSGALP00000006326; -. DR GeneID; 415940; -. DR KEGG; gga:415940; -. DR CTD; 11344; -. DR VEuPathDB; HostDB:geneid_415940; -. DR eggNOG; KOG1747; Eukaryota. DR InParanoid; Q5ZM35; -. DR PhylomeDB; Q5ZM35; -. DR PRO; PR:Q5ZM35; -. DR Proteomes; UP000000539; Unassembled WGS sequence. 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 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:SF9; TWINFILIN-2; 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 1: Evidence at protein level; KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome; Repeat. FT CHAIN 1..349 FT /note="Twinfilin-2" FT /id="PRO_0000233139" 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 324..349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 349 AA; 39835 MW; 8F4EFDBA0453BD97 CRC64; MTHQTGIHAT TELRDFFAKA RNGSVRLIKV IIEEEQLVLG AHKELARRWD VDYDAFVLPL LDEQQPCYVL YRLDSQNAQG YEWLFISWSP DNSPVRLKML YAATRATVKK EFGGGHIKDE MFGTVKEDVS LSGYQKHVSS CSAPAPLTAA EQELQQIRIN EVKTEISVES KHQTLQGLAF PLQLDAQQAI QTLKQKKINY IQLKLDLERE TIDLVHTSPT DISDLPKRIP QDSARYHFFL YKHSHEGDYL ESVVFIYSMP GYKCSIKERM LYSSCKSRLL DTVEQEFCLE IAKKIEIDDG AELTAEFLYD EVHPKQHAFK QAFAKPKGPV GKRGQKRLIK GPGENGEDS //