COF1_PIG
ID COF1_PIG Reviewed; 166 AA.
AC P10668; Q29374;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cofilin-1;
DE AltName: Full=Cofilin, non-muscle isoform;
GN Name=CFL1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=3403546; DOI=10.1016/s0021-9258(18)37996-1;
RA Matsuzaki F., Matsumoto S., Yahara I., Yonezawa N., Nishida E., Sakai H.;
RT "Cloning and characterization of porcine brain cofilin cDNA. Cofilin
RT contains the nuclear transport signal sequence.";
RL J. Biol. Chem. 263:11564-11568(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-104.
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
RN [3]
RP FUNCTION, AND ACTIN-BINDING.
RX PubMed=6509022; DOI=10.1021/bi00317a032;
RA Nishida E., Maekawa S., Sakai H.;
RT "Cofilin, a protein in porcine brain that binds to actin filaments and
RT inhibits their interactions with myosin and tropomyosin.";
RL Biochemistry 23:5307-5313(1984).
RN [4]
RP FUNCTION, ACTIN-BINDING, AND PHOSPHORYLATION AT SER-3.
RX PubMed=9078368; DOI=10.1046/j.1365-2443.1996.05005.x;
RA Moriyama K., Iida K., Yahara I.;
RT "Phosphorylation of Ser-3 of cofilin regulates its essential function on
RT actin.";
RL Genes Cells 1:73-86(1996).
CC -!- FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin
CC depolymerizing activity (PubMed:6509022, PubMed:9078368). In
CC conjunction with the subcortical maternal complex (SCMC), plays an
CC essential role for zygotes to progress beyond the first embryonic cell
CC divisions via regulation of actin dynamics (PubMed:9078368). Required
CC for the centralization of the mitotic spindle and symmetric division of
CC zygotes (By similarity). Plays a role in the regulation of cell
CC morphology and cytoskeletal organization in epithelial cells (By
CC similarity). Required for the up-regulation of atypical chemokine
CC receptor ACKR2 from endosomal compartment to cell membrane, increasing
CC its efficiency in chemokine uptake and degradation (By similarity).
CC Required for neural tube morphogenesis and neural crest cell migration
CC (By similarity). {ECO:0000250|UniProtKB:P18760,
CC ECO:0000250|UniProtKB:P23528, ECO:0000269|PubMed:6509022,
CC ECO:0000269|PubMed:9078368}.
CC -!- SUBUNIT: Can bind G- and F-actin in a 1:1 ratio of cofilin to actin
CC (PubMed:6509022, PubMed:9078368). It is a major component of
CC intranuclear and cytoplasmic actin rods (PubMed:9078368). Interacts
CC with the subcortical maternal complex (SCMC) via interaction with TLE6
CC and NLRP5 (By similarity). Interacts with C9orf72 (By similarity).
CC {ECO:0000250|UniProtKB:P18760, ECO:0000269|PubMed:6509022,
CC ECO:0000269|PubMed:9078368}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:P23528}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P23528}. Cell
CC projection, ruffle membrane {ECO:0000250|UniProtKB:P23528}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P23528}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P23528}. Cell projection, lamellipodium membrane
CC {ECO:0000250|UniProtKB:P23528}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P23528}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P23528}. 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:P23528}.
CC -!- TISSUE SPECIFICITY: Widely distributed in various tissues.
CC -!- PTM: Inactivated by phosphorylation on Ser-3 (PubMed:9078368).
CC Phosphorylated on Ser-3 in resting cells (By similarity).
CC Dephosphorylated by PDXP/chronophin; this restores its activity in
CC promoting actin filament depolymerization. The phosphorylation of Ser-
CC 24 may prevent recognition of the nuclear localization signal (By
CC similarity). Phosphorylated via a ARRB1-RAC1-LIMK1-PAK1 cascade upon
CC active ligand stimulation of atypical chemokine receptor ACKR2 (By
CC similarity). {ECO:0000250|UniProtKB:P45695,
CC ECO:0000269|PubMed:9078368}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; M20866; AAA31020.1; -; mRNA.
DR EMBL; F14577; CAA23134.1; -; mRNA.
DR PIR; A29240; A29240.
DR RefSeq; NP_001004043.1; NM_001004043.1.
DR AlphaFoldDB; P10668; -.
DR BMRB; P10668; -.
DR SMR; P10668; -.
DR STRING; 9823.ENSSSCP00000030314; -.
DR iPTMnet; P10668; -.
DR PaxDb; P10668; -.
DR PeptideAtlas; P10668; -.
DR PRIDE; P10668; -.
DR Ensembl; ENSSSCT00000043957; ENSSSCP00000031883; ENSSSCG00000012974.
DR Ensembl; ENSSSCT00025107024; ENSSSCP00025048171; ENSSSCG00025077099.
DR Ensembl; ENSSSCT00030026834; ENSSSCP00030011961; ENSSSCG00030019417.
DR Ensembl; ENSSSCT00035096287; ENSSSCP00035040515; ENSSSCG00035071147.
DR Ensembl; ENSSSCT00040091304; ENSSSCP00040040241; ENSSSCG00040066748.
DR Ensembl; ENSSSCT00045044723; ENSSSCP00045031025; ENSSSCG00045026140.
DR Ensembl; ENSSSCT00060095546; ENSSSCP00060041328; ENSSSCG00060069854.
DR Ensembl; ENSSSCT00065057958; ENSSSCP00065025141; ENSSSCG00065042384.
DR Ensembl; ENSSSCT00070034488; ENSSSCP00070028806; ENSSSCG00070017422.
DR GeneID; 445532; -.
DR KEGG; ssc:445532; -.
DR CTD; 1072; -.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR InParanoid; P10668; -.
DR OMA; QEDIEWE; -.
DR OrthoDB; 1370477at2759; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Chromosome 2.
DR Bgee; ENSSSCG00000012974; Expressed in prefrontal cortex and 43 other tissues.
DR ExpressionAtlas; P10668; 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: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; IDA: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:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
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:0000250|UniProtKB:P23528"
FT CHAIN 2..166
FT /note="Cofilin-1"
FT /id="PRO_0000214901"
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
