ID   TWF2B_XENLA             Reviewed;         349 AA.
AC   Q640W2;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Twinfilin-2-B;
GN   Name=twf2-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-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; BC082477; AAH82477.1; -; mRNA.
DR   RefSeq; NP_001087921.1; NM_001094452.1.
DR   AlphaFoldDB; Q640W2; -.
DR   SMR; Q640W2; -.
DR   DNASU; 447782; -.
DR   GeneID; 447782; -.
DR   KEGG; xla:447782; -.
DR   CTD; 447782; -.
DR   Xenbase; XB-GENE-6253382; twf2.S.
DR   OMA; RWDTDYD; -.
DR   OrthoDB; 1578109at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 447782; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; 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   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome; Repeat.
FT   CHAIN           1..349
FT                   /note="Twinfilin-2-B"
FT                   /id="PRO_0000233142"
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          321..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   349 AA;  39847 MW;  E3EAC8545371ED22 CRC64;
     MAHQTGIHAT PELKEFFAKA RNGSVRLIKV IIEEEQLVLG SHKELKHAWD QDYDAFVLQL
     LDESQPCYIL YRLDSQNAQG YEWIFLSWSP DHSPVRLKML YAATRATVKK EFGGGHIKDE
     IFGTLKEDVA LSGYKKHVSS CAAPAPLTAA ERELQAIKIN EVKTEISVES KQQTLQGLSF
     PLRPQAEEAI LLLKQKKINY IQLRLDLEKE TVDLVHTKHT EIQDLPGRIP QDTARYHFFL
     YKHSHEGDHL ESVVFIYSMP GYKCSIKERM LYSSCKNRLL DSVEQDFLME IAKKIEIEDG
     AELTDEFLYD EVHPKQHAFK QAFAKPKGPA GKRGQKRLIK GPGENGEDS