ID   COF2_MOUSE              Reviewed;         166 AA.
AC   P45591;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Cofilin-2;
DE   AltName: Full=Cofilin, muscle isoform;
GN   Name=Cfl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/HeJ; TISSUE=Skeletal muscle;
RX   PubMed=8195165; DOI=10.1016/s0021-9258(17)36603-6;
RA   Ono S., Minami N., Abe H., Obinata T.;
RT   "Characterization of a novel cofilin isoform that is predominantly
RT   expressed in mammalian skeletal muscle.";
RL   J. Biol. Chem. 269:15280-15286(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11809832; DOI=10.1091/mbc.01-07-0331;
RA   Vartiainen M.K., Mustonen T., Mattila P.K., Ojala P.J., Thesleff I.,
RA   Partanen J., Lappalainen P.;
RT   "The three mouse actin-depolymerizing factor/cofilins evolved to fulfill
RT   cell-type-specific requirements for actin dynamics.";
RL   Mol. Biol. Cell 13:183-194(2002).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-3 AND THR-6, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP   ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   FUNCTION.
RX   PubMed=22343409; DOI=10.1093/hmg/dds053;
RA   Agrawal P.B., Joshi M., Savic T., Chen Z., Beggs A.H.;
RT   "Normal myofibrillar development followed by progressive sarcomeric
RT   disruption with actin accumulations in a mouse Cfl2 knockout demonstrates
RT   requirement of cofilin-2 for muscle maintenance.";
RL   Hum. Mol. Genet. 21:2341-2356(2012).
RN   [8]
RP   FUNCTION.
RX   PubMed=24598388; DOI=10.1016/j.ejcb.2014.01.007;
RA   Gurniak C.B., Chevessier F., Jokwitz M., Joensson F., Perlas E.,
RA   Richter H., Matern G., Boyl P.P., Chaponnier C., Fuerst D., Schroeder R.,
RA   Witke W.;
RT   "Severe protein aggregate myopathy in a knockout mouse model points to an
RT   essential role of cofilin2 in sarcomeric actin exchange and muscle
RT   maintenance.";
RL   Eur. J. Cell Biol. 93:252-266(2014).
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.
CC       {ECO:0000269|PubMed:11809832, ECO:0000269|PubMed:22343409,
CC       ECO:0000269|PubMed:24598388}.
CC   -!- SUBUNIT: Interacts with CSRP3; possibly two molecules of CFL2 can
CC       interact with one molecule if CSRP3. {ECO:0000250|UniProtKB:Q9Y281}.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm, cytoskeleton.
CC       Note=Colocalizes with CSPR3 in the Z line of sarcomeres.
CC       {ECO:0000250|UniProtKB:Q9Y281}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle.
CC       {ECO:0000269|PubMed:11809832}.
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; L29468; AAA37433.1; -; mRNA.
DR   EMBL; BC007138; AAH07138.1; -; mRNA.
DR   CCDS; CCDS36448.1; -.
DR   PIR; A53812; A53812.
DR   RefSeq; NP_031714.1; NM_007688.2.
DR   AlphaFoldDB; P45591; -.
DR   BMRB; P45591; -.
DR   SMR; P45591; -.
DR   BioGRID; 198685; 9.
DR   IntAct; P45591; 3.
DR   MINT; P45591; -.
DR   STRING; 10090.ENSMUSP00000077262; -.
DR   GlyGen; P45591; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P45591; -.
DR   PhosphoSitePlus; P45591; -.
DR   SwissPalm; P45591; -.
DR   REPRODUCTION-2DPAGE; P45591; -.
DR   EPD; P45591; -.
DR   jPOST; P45591; -.
DR   PaxDb; 10090-ENSMUSP00000077262; -.
DR   PeptideAtlas; P45591; -.
DR   ProteomicsDB; 283419; -.
DR   Pumba; P45591; -.
DR   Antibodypedia; 9589; 369 antibodies from 38 providers.
DR   DNASU; 12632; -.
DR   Ensembl; ENSMUST00000078124.8; ENSMUSP00000077262.8; ENSMUSG00000062929.9.
DR   GeneID; 12632; -.
DR   KEGG; mmu:12632; -.
DR   UCSC; uc007nnx.1; mouse.
DR   AGR; MGI:101763; -.
DR   CTD; 1073; -.
DR   MGI; MGI:101763; Cfl2.
DR   VEuPathDB; HostDB:ENSMUSG00000062929; -.
DR   eggNOG; KOG1735; Eukaryota.
DR   GeneTree; ENSGT00950000183000; -.
DR   HOGENOM; CLU_094004_0_0_1; -.
DR   InParanoid; P45591; -.
DR   OMA; NECKYAI; -.
DR   OrthoDB; 3380386at2759; -.
DR   PhylomeDB; P45591; -.
DR   TreeFam; TF328601; -.
DR   BioGRID-ORCS; 12632; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Cfl2; mouse.
DR   PRO; PR:P45591; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; P45591; Protein.
DR   Bgee; ENSMUSG00000062929; Expressed in intercostal muscle and 257 other cell types or tissues.
DR   ExpressionAtlas; P45591; 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:0031674; C:I band; ISO:MGI.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; ISO:MGI.
DR   GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR   GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
DR   GO; GO:0030043; P:actin filament fragmentation; IDA:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR   GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
DR   GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISO:MGI.
DR   GO; GO:0045214; P:sarcomere organization; IMP:MGI.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:UniProtKB.
DR   CDD; cd11286; ADF_cofilin_like; 1.
DR   Gene3D; 3.40.20.10; Severin; 1.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR017904; ADF/Cofilin.
DR   PANTHER; PTHR11913:SF15; COFILIN-2; 1.
DR   PANTHER; PTHR11913; COFILIN-RELATED; 1.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   PRINTS; PR00006; COFILIN.
DR   SMART; SM00102; ADF; 1.
DR   SUPFAM; SSF55753; Actin depolymerizing proteins; 1.
DR   PROSITE; PS51263; ADF_H; 1.
DR   Genevisible; P45591; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:19131326"
FT   CHAIN           2..166
FT                   /note="Cofilin-2"
FT                   /id="PRO_0000214908"
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:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:19131326"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   MOD_RES         6
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
SQ   SEQUENCE   166 AA;  18710 MW;  48B6D7E5AE9FE1CC CRC64;
     MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI
     GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS
     KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGSVVVS LEGKPL
//