COF2_MOUSE
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 03-AUG-2022, entry version 167.
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, Pancreas,
RC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 iPTMnet; P45591; -.
DR PhosphoSitePlus; P45591; -.
DR SwissPalm; P45591; -.
DR REPRODUCTION-2DPAGE; P45591; -.
DR EPD; P45591; -.
DR jPOST; P45591; -.
DR PaxDb; P45591; -.
DR PeptideAtlas; P45591; -.
DR PRIDE; P45591; -.
DR ProteomicsDB; 283419; -.
DR Antibodypedia; 9589; 352 antibodies from 38 providers.
DR DNASU; 12632; -.
DR Ensembl; ENSMUST00000078124; ENSMUSP00000077262; ENSMUSG00000062929.
DR GeneID; 12632; -.
DR KEGG; mmu:12632; -.
DR UCSC; uc007nnx.1; mouse.
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; ECKYAIY; -.
DR OrthoDB; 1370477at2759; -.
DR PhylomeDB; P45591; -.
DR TreeFam; TF328601; -.
DR BioGRID-ORCS; 12632; 2 hits in 74 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 254 other tissues.
DR ExpressionAtlas; P45591; baseline and differential.
DR Genevisible; P45591; MM.
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; -; 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 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
