TWF2_CHICK
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 03-AUG-2022, entry version 91.
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";
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DR EMBL; AJ719549; CAG31208.1; -; mRNA.
DR RefSeq; NP_001025760.1; NM_001030589.1.
DR AlphaFoldDB; Q5ZM35; -.
DR SMR; Q5ZM35; -.
DR STRING; 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 OrthoDB; 1578109at2759; -.
DR PhylomeDB; Q5ZM35; -.
DR PRO; PR:Q5ZM35; -.
DR Proteomes; UP000000539; 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: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 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
