COF2_CHICK
ID COF2_CHICK Reviewed; 166 AA.
AC P21566;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cofilin-2;
DE AltName: Full=Cofilin, muscle isoform;
GN Name=CFL2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=1699599; DOI=10.1021/bi00484a010;
RA Abe H., Endo T., Yamamoto K., Obinata T.;
RT "Sequence of cDNAs encoding actin depolymerizing factor and cofilin of
RT embryonic chicken skeletal muscle: two functionally distinct actin-
RT regulatory proteins exhibit high structural homology.";
RL Biochemistry 29:7420-7425(1990).
RN [2]
RP STRUCTURE BY NMR, AND SEQUENCE REVISION TO 53-54.
RX PubMed=11885570; DOI=10.1023/a:1014227808686;
RA Bains N.P.S., Gorbatyuk V.Y., Nosworthy N.J., Robson S.A.,
RA Maciejewski M.W., dos Remedios C.G., King G.F.;
RT "Backbone and side-chain 1H, 15N, and 13C assignments for chick cofilin.";
RL J. Biomol. NMR 22:193-194(2002).
CC -!- FUNCTION: Controls reversibly actin polymerization and depolymerization
CC in a pH-sensitive manner. It has the ability to bind G- and F-actin in
CC a 1:1 ratio of cofilin to actin. It is the major component of
CC intranuclear and cytoplasmic actin rods.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely distributed in various tissues.
CC -!- PTM: The phosphorylation of Ser-24 may prevent recognition of the
CC nuclear localization signal.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; M55659; AAA62732.1; -; mRNA.
DR PIR; B35703; B35703.
DR RefSeq; NP_001004406.1; NM_001004406.1.
DR PDB; 1TVJ; NMR; -; A=1-166.
DR PDB; 5YU8; EM; 3.80 A; H/I/J=1-166.
DR PDBsum; 1TVJ; -.
DR PDBsum; 5YU8; -.
DR AlphaFoldDB; P21566; -.
DR BMRB; P21566; -.
DR SMR; P21566; -.
DR STRING; 9031.ENSGALP00000016266; -.
DR PaxDb; P21566; -.
DR Ensembl; ENSGALT00000081155; ENSGALP00000045503; ENSGALG00000010027.
DR GeneID; 423320; -.
DR KEGG; gga:423320; -.
DR CTD; 1073; -.
DR VEuPathDB; HostDB:geneid_423320; -.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR HOGENOM; CLU_094004_0_0_1; -.
DR InParanoid; P21566; -.
DR OMA; ECKYAIY; -.
DR OrthoDB; 1370477at2759; -.
DR PhylomeDB; P21566; -.
DR TreeFam; TF328601; -.
DR EvolutionaryTrace; P21566; -.
DR PRO; PR:P21566; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000010027; Expressed in skeletal muscle tissue and 12 other tissues.
DR ExpressionAtlas; P21566; 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:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:AgBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
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:0051014; P:actin filament severing; IBA:GO_Central.
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 PANTHER; PTHR11913; PTHR11913; 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 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..166
FT /note="Cofilin-2"
FT /id="PRO_0000214910"
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 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:1TVJ"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1TVJ"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1TVJ"
FT STRAND 44..56
FT /evidence="ECO:0007829|PDB:1TVJ"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1TVJ"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1TVJ"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1TVJ"
FT STRAND 81..93
FT /evidence="ECO:0007829|PDB:1TVJ"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:1TVJ"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:1TVJ"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:1TVJ"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1TVJ"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1TVJ"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:1TVJ"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1TVJ"
SQ SEQUENCE 166 AA; 18662 MW; 514685E940786EF0 CRC64;
MASGVTVNDE VIKVFNDMKV RKSSTPEEIK KRKKAVLFCL SDDKKQIIVE EAKQILVGDI
GDTVEDPYTA FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS
KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGNVVVS LEGKPL
