COF1_BOVIN
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 03-AUG-2022, entry version 123.
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}.
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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; Q5E9F7; -.
DR PeptideAtlas; Q5E9F7; -.
DR PRIDE; Q5E9F7; -.
DR Ensembl; ENSBTAT00000028602; ENSBTAP00000028602; ENSBTAG00000021455.
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; QEDIEWE; -.
DR OrthoDB; 1370477at2759; -.
DR TreeFam; TF328601; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000021455; Expressed in Ammon's horn and 105 other 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:0030042; P:actin filament depolymerization; IBA:GO_Central.
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; -; 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:SF17; PTHR11913:SF17; 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; 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
