ID COF1_BOVIN Reviewed; 166 AA. AC Q5E9F7; Q3SZ74; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 129. DE RecName: Full=Cofilin-1; DE AltName: Full=Cofilin, non-muscle isoform; GN Name=CFL1; 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]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin CC depolymerizing activity (By similarity). Important for normal progress CC through mitosis and normal cytokinesis (By similarity). In conjunction CC with the subcortical maternal complex (SCMC), plays an essential role CC for zygotes to progress beyond the first embryonic cell divisions via CC regulation of actin dynamics (By similarity). Required for the CC centralization of the mitotic spindle and symmetric division of zygotes CC (By similarity). Plays a role in the regulation of cell morphology and CC cytoskeletal organization in epithelial cells (By similarity). Required CC for the up-regulation of atypical chemokine receptor ACKR2 from CC endosomal compartment to cell membrane, increasing its efficiency in CC chemokine uptake and degradation (By similarity). Required for neural CC tube morphogenesis and neural crest cell migration (By similarity). CC {ECO:0000250|UniProtKB:P18760, ECO:0000250|UniProtKB:P23528}. CC -!- SUBUNIT: Can bind G- and F-actin in a 1:1 ratio of cofilin to actin (By CC similarity). It is a major component of intranuclear and cytoplasmic CC actin rods (By similarity). Interacts with the subcortical maternal CC complex (SCMC) via interaction with TLE6 and NLRP5 (By similarity). CC Interacts with C9orf72 (By similarity). {ECO:0000250|UniProtKB:P10668, CC ECO:0000250|UniProtKB:P18760}. CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:P10668}. CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P10668}. Cell CC projection, ruffle membrane {ECO:0000250|UniProtKB:P10668}; Peripheral CC membrane protein {ECO:0000250|UniProtKB:P10668}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium membrane CC {ECO:0000250|UniProtKB:P10668}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P10668}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium CC {ECO:0000250|UniProtKB:P18760}. Cell projection, growth cone CC {ECO:0000250|UniProtKB:P18760}. Cell projection, axon CC {ECO:0000250|UniProtKB:P18760}. Note=Colocalizes with the actin CC cytoskeleton in membrane ruffles and lamellipodia. Detected at the CC cleavage furrow and contractile ring during cytokinesis. Almost CC completely in nucleus in cells exposed to heat shock or 10% dimethyl CC sulfoxide. {ECO:0000250|UniProtKB:P10668, CC ECO:0000250|UniProtKB:P23528}. CC -!- PTM: Inactivated by phosphorylation on Ser-3. Phosphorylated on Ser-3 CC in resting cells (By similarity). Dephosphorylated by PDXP/chronophin; CC this restores its activity in promoting actin filament CC depolymerization. The phosphorylation of Ser-24 may prevent recognition CC of the nuclear localization signal (By similarity). Phosphorylated via CC a ARRB1-RAC1-LIMK1-PAK1 cascade upon active ligand stimulation of CC atypical chemokine receptor ACKR2 (By similarity). CC {ECO:0000250|UniProtKB:P45695}. 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; BT020963; AAX08980.1; -; mRNA. DR EMBL; BC103077; AAI03078.1; -; mRNA. DR RefSeq; NP_001015655.1; NM_001015655.1. DR AlphaFoldDB; Q5E9F7; -. DR SMR; Q5E9F7; -. DR STRING; 9913.ENSBTAP00000028602; -. DR PaxDb; 9913-ENSBTAP00000028602; -. DR PeptideAtlas; Q5E9F7; -. DR Ensembl; ENSBTAT00000028602.6; ENSBTAP00000028602.5; ENSBTAG00000021455.6. DR GeneID; 534553; -. DR KEGG; bta:534553; -. DR CTD; 1072; -. DR VEuPathDB; HostDB:ENSBTAG00000021455; -. DR VGNC; VGNC:27253; CFL1. DR eggNOG; KOG1735; Eukaryota. DR GeneTree; ENSGT00950000183000; -. DR HOGENOM; CLU_094004_0_0_1; -. DR InParanoid; Q5E9F7; -. DR OMA; WSMIYAT; -. DR OrthoDB; 3380386at2759; -. DR TreeFam; TF328601; -. DR Proteomes; UP000009136; Chromosome 29. DR Bgee; ENSBTAG00000021455; Expressed in Ammon's horn and 105 other cell types or tissues. DR ExpressionAtlas; Q5E9F7; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl. DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB. DR GO; GO:0030043; P:actin filament fragmentation; IBA:GO_Central. DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB. DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central. DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0051293; P:establishment of spindle localization; ISS:UniProtKB. DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central. DR GO; GO:0044794; P:positive regulation by host of viral process; IEA:Ensembl. DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB. DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB. DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IEA:Ensembl. DR GO; GO:0009615; P:response to virus; IEA:Ensembl. DR CDD; cd11286; ADF_cofilin_like; 1. DR Gene3D; 3.40.20.10; Severin; 1. DR InterPro; IPR002108; ADF-H. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf. DR InterPro; IPR017904; ADF/Cofilin. DR PANTHER; PTHR11913:SF17; COFILIN-1; 1. DR PANTHER; PTHR11913; COFILIN-RELATED; 1. DR Pfam; PF00241; Cofilin_ADF; 1. DR PRINTS; PR00006; COFILIN. DR SMART; SM00102; ADF; 1. DR SUPFAM; SSF55753; Actin depolymerizing proteins; 1. DR PROSITE; PS51263; ADF_H; 1. PE 2: Evidence at transcript level; KW Acetylation; Actin-binding; Cell membrane; Cell projection; Cytoplasm; KW Cytoskeleton; Isopeptide bond; Membrane; Nucleus; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P23528" FT CHAIN 2..166 FT /note="Cofilin-1" FT /id="PRO_0000214897" 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:P23528" FT MOD_RES 3 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P23528" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P18760" FT MOD_RES 13 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P23528" FT MOD_RES 25 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P23528" FT MOD_RES 41 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P23528" FT MOD_RES 68 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P23528" FT MOD_RES 73 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P23528" FT MOD_RES 140 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P23528" FT MOD_RES 144 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P23528" FT MOD_RES 156 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P23528" FT CROSSLNK 132 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P23528" SQ SEQUENCE 166 AA; 18519 MW; 589EE8EC1ED12719 CRC64; MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPECAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL //