COF2_PIG
ID COF2_PIG Reviewed; 166 AA.
AC Q5G6V9;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 4.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cofilin-2;
DE AltName: Full=Cofilin, muscle isoform;
GN Name=CFL2;
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].
RC TISSUE=Skeletal muscle;
RA Su Y., Song H., Zeng R., Liu D., Zhu B., Ba C.;
RT "Characterization of cofilin 2 (CFL2) in pig skeletal muscle.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Su Y., Zeng R., Liu D., Song H., Zhu B., Ba C.;
RT "Cloning and sequencing of gene cofilin 2 in pig.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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. Required for muscle
CC maintenance. May play a role during the exchange of alpha-actin forms
CC during the early postnatal remodeling of the sarcomere (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y281}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Note=Colocalizes with CSPR3 in the Z line
CC of sarcomeres. {ECO:0000250|UniProtKB:Q9Y281}.
CC -!- PTM: The phosphorylation of Ser-24 may prevent recognition of the
CC nuclear localization signal. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; DQ058293; AAY78932.1; -; mRNA.
DR EMBL; AY830126; AAW66489.4; -; Genomic_DNA.
DR RefSeq; NP_001020386.1; NM_001025215.1.
DR RefSeq; XP_005656356.1; XM_005656299.2.
DR AlphaFoldDB; Q5G6V9; -.
DR BMRB; Q5G6V9; -.
DR SMR; Q5G6V9; -.
DR STRING; 9823.ENSSSCP00000002141; -.
DR PaxDb; Q5G6V9; -.
DR PeptideAtlas; Q5G6V9; -.
DR PRIDE; Q5G6V9; -.
DR Ensembl; ENSSSCT00000002192; ENSSSCP00000002141; ENSSSCG00000001959.
DR Ensembl; ENSSSCT00000064495; ENSSSCP00000045533; ENSSSCG00000001959.
DR Ensembl; ENSSSCT00015081329; ENSSSCP00015032906; ENSSSCG00015060726.
DR Ensembl; ENSSSCT00025097662; ENSSSCP00025042895; ENSSSCG00025071059.
DR Ensembl; ENSSSCT00025097775; ENSSSCP00025042960; ENSSSCG00025071059.
DR Ensembl; ENSSSCT00030084024; ENSSSCP00030038627; ENSSSCG00030060165.
DR Ensembl; ENSSSCT00030084061; ENSSSCP00030038644; ENSSSCG00030060165.
DR Ensembl; ENSSSCT00035058921; ENSSSCP00035023692; ENSSSCG00035044355.
DR Ensembl; ENSSSCT00035058928; ENSSSCP00035023697; ENSSSCG00035044355.
DR Ensembl; ENSSSCT00040014372; ENSSSCP00040005591; ENSSSCG00040010975.
DR Ensembl; ENSSSCT00040014403; ENSSSCP00040005610; ENSSSCG00040010975.
DR Ensembl; ENSSSCT00045015210; ENSSSCP00045010566; ENSSSCG00045008975.
DR Ensembl; ENSSSCT00045015248; ENSSSCP00045010588; ENSSSCG00045008975.
DR Ensembl; ENSSSCT00050007891; ENSSSCP00050003343; ENSSSCG00050005802.
DR Ensembl; ENSSSCT00050007910; ENSSSCP00050003354; ENSSSCG00050005802.
DR Ensembl; ENSSSCT00055035195; ENSSSCP00055027950; ENSSSCG00055017925.
DR Ensembl; ENSSSCT00055035425; ENSSSCP00055028135; ENSSSCG00055017925.
DR Ensembl; ENSSSCT00060103565; ENSSSCP00060045254; ENSSSCG00060075576.
DR Ensembl; ENSSSCT00060103642; ENSSSCP00060045316; ENSSSCG00060075576.
DR Ensembl; ENSSSCT00065087321; ENSSSCP00065038177; ENSSSCG00065063654.
DR Ensembl; ENSSSCT00065087327; ENSSSCP00065038179; ENSSSCG00065063654.
DR Ensembl; ENSSSCT00070013566; ENSSSCP00070011187; ENSSSCG00070007061.
DR Ensembl; ENSSSCT00070013575; ENSSSCP00070011194; ENSSSCG00070007061.
DR GeneID; 497233; -.
DR KEGG; ssc:497233; -.
DR CTD; 1073; -.
DR VGNC; VGNC:86611; CFL2.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR HOGENOM; CLU_094004_0_0_1; -.
DR InParanoid; Q5G6V9; -.
DR OMA; ECKYAIY; -.
DR OrthoDB; 1370477at2759; -.
DR TreeFam; TF328601; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Proteomes; UP000314985; Chromosome 7.
DR Bgee; ENSSSCG00000001959; Expressed in muscle tissue and 44 other tissues.
DR ExpressionAtlas; Q5G6V9; baseline and differential.
DR Genevisible; Q5G6V9; SS.
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:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0030043; P:actin filament fragmentation; IBA:GO_Central.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; 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 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 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y281"
FT CHAIN 2..166
FT /note="Cofilin-2"
FT /id="PRO_0000214909"
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:Q9Y281"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y281"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P45591"
SQ SEQUENCE 166 AA; 18737 MW; 48B6CDCCAE9FE1CC CRC64;
MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI
GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS
KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGNVVVS LEGKPL
