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Cofilin-1 (Cofilin, non-muscle isoform)

 COF1_PIG                Reviewed;         166 AA.
P10668; Q29374;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 132.
RecName: Full=Cofilin-1;
AltName: Full=Cofilin, non-muscle isoform;
Name=CFL1;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Brain;
PubMed=3403546;
Matsuzaki F., Matsumoto S., Yahara I., Yonezawa N., Nishida E.,
Sakai H.;
"Cloning and characterization of porcine brain cofilin cDNA. Cofilin
contains the nuclear transport signal sequence.";
J. Biol. Chem. 263:11564-11568(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-104.
TISSUE=Small intestine;
PubMed=8672129; DOI=10.1007/s003359900153;
Winteroe A.K., Fredholm M., Davies W.;
"Evaluation and characterization of a porcine small intestine cDNA
library: analysis of 839 clones.";
Mamm. Genome 7:509-517(1996).
[3]
ACTIN-BINDING.
PubMed=6509022; DOI=10.1021/bi00317a032;
Nishida E., Maekawa S., Sakai H.;
"Cofilin, a protein in porcine brain that binds to actin filaments and
inhibits their interactions with myosin and tropomyosin.";
Biochemistry 23:5307-5313(1984).
[4]
ACTIN-BINDING, AND PHOSPHORYLATION AT SER-3.
PubMed=9078368; DOI=10.1046/j.1365-2443.1996.05005.x;
Moriyama K., Iida K., Yahara I.;
"Phosphorylation of Ser-3 of cofilin regulates its essential function
on actin.";
Genes Cells 1:73-86(1996).
-!- FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin
depolymerizing activity. Regulates actin cytoskeleton dynamics
(PubMed:6509022, PubMed:9078368). Important for normal progress
through mitosis and normal cytokinesis. Plays a role in the
regulation of cell morphology and cytoskeletal organization.
Required for the up-regulation of atypical chemokine receptor
ACKR2 from endosomal compartment to cell membrane, increasing its
efficiency in chemokine uptake and degradation. Required for
neural tube morphogenesis and neural crest cell migration (By
similarity). {ECO:0000250|UniProtKB:P10668,
ECO:0000250|UniProtKB:P18760, ECO:0000269|PubMed:6509022,
ECO:0000269|PubMed:9078368}.
-!- SUBUNIT: Can bind G- and F-actin in a 1:1 ratio of cofilin to
actin. It is a major component of intranuclear and cytoplasmic
actin rods (By similarity). {ECO:0000250|UniProtKB:P10668}.
-!- SUBCELLULAR LOCATION: Nucleus matrix
{ECO:0000250|UniProtKB:P10668}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P10668}. Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:P10668}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P10668}; Cytoplasmic side
{ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium
membrane {ECO:0000250|UniProtKB:P10668}; Peripheral membrane
protein {ECO:0000250|UniProtKB:P10668}; Cytoplasmic side
{ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:P18760}. Note=Colocalizes with the actin
cytoskeleton in membrane ruffles and lamellipodia. Detected at the
cleavage furrow and contractile ring during cytokinesis. Almost
completely in nucleus in cells exposed to heat shock (By
similarity). {ECO:0000250|UniProtKB:P10668}.
-!- TISSUE SPECIFICITY: Widely distributed in various tissues.
-!- PTM: Inactivated by phosphorylation on Ser-3 (PubMed:9078368).
Phosphorylated on Ser-3 in resting cells (By similarity).
Dephosphorylated by PDXP/chronophin; this restores its activity in
promoting actin filament depolymerization. The phosphorylation of
Ser-24 may prevent recognition of the nuclear localization signal
(By similarity). Phosphorylated via a ARRB1-RAC1-LIMK1-PAK1
cascade upon active ligand stimulation of atypical chemokine
receptor ACKR2 (By similarity). {ECO:0000250|UniProtKB:P45695,
ECO:0000269|PubMed:9078368}.
-!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
{ECO:0000305}.
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EMBL; M20866; AAA31020.1; -; mRNA.
EMBL; F14577; CAA23134.1; -; mRNA.
PIR; A29240; A29240.
RefSeq; NP_001004043.1; NM_001004043.1.
UniGene; Ssc.716; -.
ProteinModelPortal; P10668; -.
STRING; 9823.ENSSSCP00000030314; -.
iPTMnet; P10668; -.
PaxDb; P10668; -.
PeptideAtlas; P10668; -.
PRIDE; P10668; -.
Ensembl; ENSSSCT00000043957; ENSSSCP00000031883; ENSSSCG00000012974.
GeneID; 445532; -.
KEGG; ssc:445532; -.
CTD; 1072; -.
GeneTree; ENSGT00440000033289; -.
HOGENOM; HOG000039697; -.
HOVERGEN; HBG000381; -.
InParanoid; P10668; -.
KO; K05765; -.
Proteomes; UP000008227; Chromosome 2.
ExpressionAtlas; P10668; baseline and differential.
GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0030042; P:actin filament depolymerization; IEA:InterPro.
GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
CDD; cd11286; ADF_cofilin_like; 1.
Gene3D; 3.40.20.10; -; 1.
InterPro; IPR002108; ADF-H.
InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
InterPro; IPR017904; ADF/Cofilin.
InterPro; IPR027234; Cofilin_1.
PANTHER; PTHR11913; PTHR11913; 1.
PANTHER; PTHR11913:SF17; PTHR11913:SF17; 1.
Pfam; PF00241; Cofilin_ADF; 1.
PRINTS; PR00006; COFILIN.
SMART; SM00102; ADF; 1.
PROSITE; PS51263; ADF_H; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P23528}.
CHAIN 2 166 Cofilin-1.
/FTId=PRO_0000214901.
DOMAIN 4 153 ADF-H. {ECO:0000255|PROSITE-
ProRule:PRU00599}.
MOTIF 30 34 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P23528}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:P23528}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:P18760}.
MOD_RES 13 13 N6-acetyllysine.
{ECO:0000250|UniProtKB:P23528}.
MOD_RES 25 25 Phosphothreonine.
{ECO:0000250|UniProtKB:P23528}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000250|UniProtKB:P23528}.
MOD_RES 68 68 Phosphotyrosine.
{ECO:0000250|UniProtKB:P23528}.
MOD_RES 73 73 N6-acetyllysine.
{ECO:0000250|UniProtKB:P23528}.
MOD_RES 140 140 Phosphotyrosine.
{ECO:0000250|UniProtKB:P23528}.
MOD_RES 144 144 N6-acetyllysine.
{ECO:0000250|UniProtKB:P23528}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000250|UniProtKB:P23528}.
CROSSLNK 132 132 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P23528}.
MUTAGEN 112 112 K->Q: Slight modification of activity.
Abolishes ability to depolymerize or bind
F-actin; when associated with Q-114.
MUTAGEN 114 114 K->Q: Impairs interaction with actin.
Abolishes ability to depolymerize or bind
F-actin; when associated with Q-112.
SEQUENCE 166 AA; 18519 MW; 589EE8EC1ED12719 CRC64;
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV
GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPECAP LKSKMIYASS
KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL


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