ID   COF1_XENTR              Reviewed;         168 AA.
AC   Q6NX11; Q0VGY0; Q28IR0;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Cofilin-1;
DE   AltName: Full=ADF/cofilin;
GN   Name=cfl1; ORFNames=TNeu055g03.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tail bud;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in the regulation of cell morphology and
CC       cytoskeletal organization (By similarity). Binds to F-actin and
CC       exhibits pH-sensitive F-actin depolymerizing activity. Required for
CC       formation of the cleavage furrow during cytokinesis. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}.
CC       Membrane {ECO:0000250}. Note=Cellular localization varies throughout
CC       development and may be related to phosphorylation levels. Shows diffuse
CC       cortical cytoplasm localization in oocytes, with membrane-association
CC       increasing after fertilization, particularly in the vegetal hemisphere
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Inactive when phosphorylated. Phosphorylation levels vary during
CC       development. Dephosphorylated by pdxp (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC       {ECO:0000305}.
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; CR760270; CAJ82443.1; -; mRNA.
DR   EMBL; BC067328; AAH67328.1; -; mRNA.
DR   EMBL; BC080356; AAH80356.1; -; mRNA.
DR   RefSeq; NP_998878.1; NM_213713.1.
DR   AlphaFoldDB; Q6NX11; -.
DR   SMR; Q6NX11; -.
DR   STRING; 8364.ENSXETP00000055308; -.
DR   PaxDb; Q6NX11; -.
DR   DNASU; 407855; -.
DR   Ensembl; ENSXETT00000080789; ENSXETP00000091251; ENSXETG00000026161.
DR   GeneID; 407855; -.
DR   KEGG; xtr:407855; -.
DR   CTD; 1072; -.
DR   Xenbase; XB-GENE-1016481; cfl1.
DR   eggNOG; KOG1735; Eukaryota.
DR   HOGENOM; CLU_094004_0_0_1; -.
DR   InParanoid; Q6NX11; -.
DR   OMA; QEDIEWE; -.
DR   OrthoDB; 1370477at2759; -.
DR   PhylomeDB; Q6NX11; -.
DR   TreeFam; TF328601; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000026161; Expressed in female reproductive system and 36 other tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR   GO; GO:0030042; P:actin filament depolymerization; ISS:UniProtKB.
DR   GO; GO:0030043; P:actin filament fragmentation; IBA:GO_Central.
DR   GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR   GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; ISS:UniProtKB.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR   CDD; cd11286; ADF_cofilin_like; 1.
DR   Gene3D; 3.40.20.10; -; 1.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR017904; ADF/Cofilin.
DR   InterPro; IPR027234; Cofilin_1.
DR   PANTHER; PTHR11913; PTHR11913; 1.
DR   PANTHER; PTHR11913:SF53; PTHR11913:SF53; 1.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   PRINTS; PR00006; COFILIN.
DR   SMART; SM00102; ADF; 1.
DR   PROSITE; PS51263; ADF_H; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..168
FT                   /note="Cofilin-1"
FT                   /id="PRO_0000214906"
FT   DOMAIN          4..153
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   MOTIF           30..34
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   168 AA;  19073 MW;  14AB09FF9616496A CRC64;
     MASGVMVSDD VIKVFNDMKV RHQLSPEEAK KRKKAVVFCL SEDKKMIILE PGKEILQGDV
     GCNVDDPYKA FVKMLPRNDC RYALYDALYE TKETKKEDLV FVFWAPEEAS LKSKMIYASS
     KDAIKKRFPG IKHEWQTNTF EDINDPCNLA EKLGGSTVIS LEGKTLKS