ID   COF2_BOVIN              Reviewed;         166 AA.
AC   Q148F1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cofilin-2;
DE   AltName: Full=Cofilin, muscle isoform;
GN   Name=CFL2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Controls reversibly actin polymerization and depolymerization
CC       in a pH-sensitive manner. It has the ability to bind G- and F-actin in
CC       a 1:1 ratio of cofilin to actin. It is the major component of
CC       intranuclear and cytoplasmic actin rods (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}.
CC   -!- PTM: The phosphorylation of Ser-24 may prevent recognition of the
CC       nuclear localization signal.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC       {ECO:0000305}.
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DR   EMBL; BC118390; AAI18391.1; -; mRNA.
DR   RefSeq; NP_001069622.1; NM_001076154.2.
DR   AlphaFoldDB; Q148F1; -.
DR   BMRB; Q148F1; -.
DR   SMR; Q148F1; -.
DR   STRING; 9913.ENSBTAP00000020036; -.
DR   PaxDb; Q148F1; -.
DR   PeptideAtlas; Q148F1; -.
DR   PRIDE; Q148F1; -.
DR   Ensembl; ENSBTAT00000020036; ENSBTAP00000020036; ENSBTAG00000015053.
DR   GeneID; 539332; -.
DR   KEGG; bta:539332; -.
DR   CTD; 1073; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015053; -.
DR   VGNC; VGNC:27254; CFL2.
DR   eggNOG; KOG1735; Eukaryota.
DR   GeneTree; ENSGT00950000183000; -.
DR   HOGENOM; CLU_094004_0_0_1; -.
DR   InParanoid; Q148F1; -.
DR   OMA; ECKYAIY; -.
DR   OrthoDB; 1370477at2759; -.
DR   TreeFam; TF328601; -.
DR   Proteomes; UP000009136; Chromosome 21.
DR   Bgee; ENSBTAG00000015053; Expressed in gluteus medius and 105 other tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
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:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0030836; P:positive regulation of actin filament depolymerization; IEA:Ensembl.
DR   GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
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   PANTHER; PTHR11913; PTHR11913; 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; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y281"
FT   CHAIN           2..166
FT                   /note="Cofilin-2"
FT                   /id="PRO_0000260255"
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|UniProtKB:Q9Y281"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y281"
FT   MOD_RES         6
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P45591"
SQ   SEQUENCE   166 AA;  18737 MW;  48B6CDCCAE9FE1CC CRC64;
     MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI
     GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS
     KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGNVVVS LEGKPL