COF1_RAT
ID COF1_RAT Reviewed; 166 AA.
AC P45592;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Cofilin-1;
DE AltName: Full=Cofilin, non-muscle isoform;
GN Name=Cfl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RA Shirasawa T., Takahashi H., Sakamoto K., Kawashima A., Akashi T.;
RL Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-166, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-3,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Parotid gland;
RX PubMed=9877327; DOI=10.1016/s0003-9969(98)00083-1;
RA Kanamori T., Suzuki M., Titani K.;
RT "Complete amino acid sequences and phosphorylation sites, determined by
RT Edman degradation and mass spectrometry, of rat parotid destrin- and
RT cofilin-like proteins.";
RL Arch. Oral Biol. 43:955-967(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 35-73; 82-92; 96-112; 133-146 AND 153-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
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 -!- INTERACTION:
CC P45592; Q66HL2: Cttn; NbExp=4; IntAct=EBI-917556, EBI-6273816;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:P10668}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P10668}. Cell
CC projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein
CC {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. Dephosphorylated by PDXP/chronophin; this restores
CC its activity in promoting actin filament depolymerization. The
CC phosphorylation of Ser-24 may prevent recognition of the nuclear
CC localization signal (By similarity). Phosphorylated via a ARRB1-RAC1-
CC LIMK1-PAK1 cascade upon active ligand stimulation of atypical chemokine
CC receptor ACKR2 (By similarity). {ECO:0000250|UniProtKB:P45695}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; X62908; CAA44694.1; -; mRNA.
DR EMBL; BC059143; AAH59143.1; -; mRNA.
DR EMBL; BC086533; AAH86533.1; -; mRNA.
DR PIR; S49101; S49101.
DR RefSeq; NP_058843.1; NM_017147.2.
DR AlphaFoldDB; P45592; -.
DR BMRB; P45592; -.
DR SMR; P45592; -.
DR BioGRID; 247942; 10.
DR IntAct; P45592; 6.
DR MINT; P45592; -.
DR STRING; 10116.ENSRNOP00000059624; -.
DR iPTMnet; P45592; -.
DR PhosphoSitePlus; P45592; -.
DR World-2DPAGE; 0004:P45592; -.
DR jPOST; P45592; -.
DR PaxDb; P45592; -.
DR PRIDE; P45592; -.
DR Ensembl; ENSRNOT00000117088; ENSRNOP00000093902; ENSRNOG00000020660.
DR GeneID; 29271; -.
DR KEGG; rno:29271; -.
DR UCSC; RGD:69285; rat.
DR CTD; 1072; -.
DR RGD; 69285; Cfl1.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR HOGENOM; CLU_094004_0_0_1; -.
DR InParanoid; P45592; -.
DR OMA; QEDIEWE; -.
DR OrthoDB; 1370477at2759; -.
DR PhylomeDB; P45592; -.
DR PRO; PR:P45592; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020660; Expressed in cerebellum and 19 other tissues.
DR Genevisible; P45592; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0031252; C:cell leading edge; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0090732; C:cofilin-actin rod; IDA:RGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0030175; C:filopodium; IDA:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IMP:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:RGD.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IPI:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0030042; P:actin filament depolymerization; ISO:RGD.
DR GO; GO:0030043; P:actin filament fragmentation; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0030030; P:cell projection organization; IDA:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IMP:RGD.
DR GO; GO:0071362; P:cellular response to ether; IEP:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:RGD.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IDA:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IDA:RGD.
DR GO; GO:0071354; P:cellular response to interleukin-6; IDA:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:RGD.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:RGD.
DR GO; GO:0051293; P:establishment of spindle localization; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; IMP:RGD.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IMP:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IMP:RGD.
DR GO; GO:2000146; P:negative regulation of cell motility; IMP:RGD.
DR GO; GO:0045792; P:negative regulation of cell size; IDA:MGI.
DR GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IMP:RGD.
DR GO; GO:0010593; P:negative regulation of lamellipodium assembly; IMP:RGD.
DR GO; GO:1905875; P:negative regulation of postsynaptic density organization; IMP:RGD.
DR GO; GO:0051511; P:negative regulation of unidimensional cell growth; IMP:RGD.
DR GO; GO:0001755; P:neural crest cell migration; ISO:RGD.
DR GO; GO:0001842; P:neural fold formation; ISO:RGD.
DR GO; GO:0044794; P:positive regulation by host of viral process; ISO:RGD.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISO:RGD.
DR GO; GO:2000814; P:positive regulation of barbed-end actin filament capping; IMP:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
DR GO; GO:2000147; P:positive regulation of cell motility; IMP:RGD.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:2000784; P:positive regulation of establishment of cell polarity regulating cell shape; IMP:RGD.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:RGD.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:RGD.
DR GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; IMP:RGD.
DR GO; GO:1905873; P:positive regulation of protein localization to cell leading edge; IMP:RGD.
DR GO; GO:0045862; P:positive regulation of proteolysis; IMP:RGD.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; IMP:RGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0043200; P:response to amino acid; ISO:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009615; P:response to virus; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Isopeptide bond; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9877327, ECO:0000269|Ref.5"
FT CHAIN 2..166
FT /note="Cofilin-1"
FT /id="PRO_0000214902"
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:0000269|PubMed:9877327, ECO:0000269|Ref.5"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9877327, ECO:0000269|Ref.5"
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; 18533 MW; 19835391A81A5AB2 CRC64;
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV
GQTVDDPYTT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS
KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL
