COF2_HUMAN
ID COF2_HUMAN Reviewed; 166 AA.
AC Q9Y281; G3V5P4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Cofilin-2;
DE AltName: Full=Cofilin, muscle isoform;
GN Name=CFL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CFL2A AND CFL2B).
RA Jin J., Li G., Hu S., Li W., Yuan J., Qiang B.;
RT "Isolation of two isoforms of human cofilin cDNA.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11422377; DOI=10.1046/j.1432-1327.2001.02247.x;
RA Thirion C., Stucka R., Mendel B., Gruhler A., Jaksch M., Nowak K.J.,
RA Binz N., Laing N.G., Lochmuller H.;
RT "Characterization of human muscle type cofilin (CFL2) in normal and
RT regenerating muscle.";
RL Eur. J. Biochem. 268:3473-3482(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS CFL2A AND CFL2B).
RC TISSUE=Bone marrow, Placenta, and Skeletal muscle;
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 [6]
RP PROTEIN SEQUENCE OF 2-21; 35-92; 96-112; 115-125 AND 153-166, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
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].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CSRP3.
RX PubMed=19752190; DOI=10.1128/mcb.00654-09;
RA Papalouka V., Arvanitis D.A., Vafiadaki E., Mavroidis M., Papadodima S.A.,
RA Spiliopoulou C.A., Kremastinos D.T., Kranias E.G., Sanoudou D.;
RT "Muscle LIM protein interacts with cofilin 2 and regulates F-actin dynamics
RT in cardiac and skeletal muscle.";
RL Mol. Cell. Biol. 29:6046-6058(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
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].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
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].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] MET-47.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [17]
RP VARIANT NEM7 THR-35, AND CHARACTERIZATION OF VARIANT NEM7 THR-35.
RX PubMed=17160903; DOI=10.1086/510402;
RA Agrawal P.B., Greenleaf R.S., Tomczak K.K., Lehtokari V.-L.,
RA Wallgren-Pettersson C., Wallefeld W., Laing N.G., Darras B.T.,
RA Maciver S.K., Dormitzer P.R., Beggs A.H.;
RT "Nemaline myopathy with minicores caused by mutation of the CFL2 gene
RT encoding the skeletal muscle actin-binding protein, cofilin-2.";
RL Am. J. Hum. Genet. 80:162-167(2007).
RN [18]
RP VARIANT NEM7 MET-7.
RX PubMed=22560515; DOI=10.1016/j.nmd.2012.03.008;
RA Ockeloen C.W., Gilhuis H.J., Pfundt R., Kamsteeg E.J., Agrawal P.B.,
RA Beggs A.H., Dara Hama-Amin A., Diekstra A., Knoers N.V., Lammens M.,
RA van Alfen N.;
RT "Congenital myopathy caused by a novel missense mutation in the CFL2
RT gene.";
RL Neuromuscul. Disord. 22:632-639(2012).
CC -!- FUNCTION: Controls reversibly actin polymerization and depolymerization
CC in a pH-sensitive manner. Its F-actin depolymerization activity is
CC regulated by association with CSPR3 (PubMed:19752190). It has the
CC ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It
CC is the major component of intranuclear and cytoplasmic actin rods.
CC Required for muscle maintenance. May play a role during the exchange of
CC alpha-actin forms during the early postnatal remodeling of the
CC sarcomere (By similarity). {ECO:0000250|UniProtKB:P45591,
CC ECO:0000269|PubMed:19752190}.
CC -!- SUBUNIT: Interacts with CSRP3; possibly two molecules of CFL2 can
CC interact with one molecule if CSRP3. {ECO:0000269|PubMed:19752190}.
CC -!- INTERACTION:
CC Q9Y281; P60709: ACTB; NbExp=10; IntAct=EBI-351218, EBI-353944;
CC Q9Y281; P63261: ACTG1; NbExp=9; IntAct=EBI-351218, EBI-351292;
CC Q9Y281; P50461: CSRP3; NbExp=2; IntAct=EBI-351218, EBI-5658719;
CC Q9Y281; P60981: DSTN; NbExp=3; IntAct=EBI-351218, EBI-745191;
CC Q9Y281; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-351218, EBI-356015;
CC Q9Y281; Q08426: EHHADH; NbExp=3; IntAct=EBI-351218, EBI-2339219;
CC Q9Y281; Q92876: KLK6; NbExp=3; IntAct=EBI-351218, EBI-2432309;
CC Q9Y281; Q9NUX5: POT1; NbExp=3; IntAct=EBI-351218, EBI-752420;
CC Q9Y281; P61019: RAB2A; NbExp=3; IntAct=EBI-351218, EBI-752037;
CC Q9Y281; P78317: RNF4; NbExp=3; IntAct=EBI-351218, EBI-2340927;
CC Q9Y281; Q9C029: TRIM7; NbExp=3; IntAct=EBI-351218, EBI-2813981;
CC Q9Y281; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-351218, EBI-10180829;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Note=Colocalizes with CSPR3 in the Z line
CC of sarcomeres. {ECO:0000269|PubMed:19752190}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Isoforms are identical at the level of the protein sequence.;
CC Name=CFL2b;
CC IsoId=Q9Y281-1; Sequence=Displayed;
CC Name=CFL2a;
CC IsoId=Q9Y281-2; Sequence=Not described;
CC Name=3;
CC IsoId=Q9Y281-3; Sequence=VSP_046831;
CC -!- TISSUE SPECIFICITY: Isoform CFL2b is expressed predominantly in
CC skeletal muscle and heart. Isoform CFL2a is expressed in various
CC tissues.
CC -!- PTM: The phosphorylation of Ser-24 may prevent recognition of the
CC nuclear localization signal.
CC -!- DISEASE: Nemaline myopathy 7 (NEM7) [MIM:610687]: A form of nemaline
CC myopathy. Nemaline myopathies are muscular disorders characterized by
CC muscle weakness of varying severity and onset, and abnormal thread-like
CC or rod-shaped structures in muscle fibers on histologic examination.
CC Nemaline myopathy type 7 presents at birth with hypotonia and
CC generalized weakness. Major motor milestones are delayed, but
CC independent ambulation is achieved. {ECO:0000269|PubMed:17160903,
CC ECO:0000269|PubMed:22560515}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Cofilin entry;
CC URL="https://en.wikipedia.org/wiki/Cofilin";
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DR EMBL; AF134802; AAD31280.1; -; mRNA.
DR EMBL; AF134803; AAD31281.1; -; mRNA.
DR EMBL; AF283513; AAF97934.1; -; Genomic_DNA.
DR EMBL; AF242299; AAF64498.1; -; Genomic_DNA.
DR EMBL; AL355885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65912.1; -; Genomic_DNA.
DR EMBL; BC011444; AAH11444.1; -; mRNA.
DR EMBL; BC022364; AAH22364.1; -; mRNA.
DR EMBL; BC022876; AAH22876.1; -; mRNA.
DR CCDS; CCDS58311.1; -. [Q9Y281-3]
DR CCDS; CCDS9649.1; -. [Q9Y281-1]
DR CCDS; CCDS9650.1; -. [Q9Y281-1]
DR RefSeq; NP_001230574.1; NM_001243645.1. [Q9Y281-3]
DR RefSeq; NP_068733.1; NM_021914.7. [Q9Y281-1]
DR RefSeq; NP_619579.1; NM_138638.4. [Q9Y281-1]
DR RefSeq; XP_011534665.1; XM_011536363.2. [Q9Y281-3]
DR AlphaFoldDB; Q9Y281; -.
DR BMRB; Q9Y281; -.
DR SMR; Q9Y281; -.
DR BioGRID; 107500; 101.
DR DIP; DIP-33178N; -.
DR IntAct; Q9Y281; 45.
DR MINT; Q9Y281; -.
DR STRING; 9606.ENSP00000298159; -.
DR iPTMnet; Q9Y281; -.
DR PhosphoSitePlus; Q9Y281; -.
DR SwissPalm; Q9Y281; -.
DR BioMuta; CFL2; -.
DR DMDM; 6831517; -.
DR EPD; Q9Y281; -.
DR jPOST; Q9Y281; -.
DR MassIVE; Q9Y281; -.
DR MaxQB; Q9Y281; -.
DR PaxDb; Q9Y281; -.
DR PeptideAtlas; Q9Y281; -.
DR PRIDE; Q9Y281; -.
DR ProteomicsDB; 33582; -.
DR ProteomicsDB; 85686; -. [Q9Y281-1]
DR TopDownProteomics; Q9Y281-1; -. [Q9Y281-1]
DR Antibodypedia; 9589; 352 antibodies from 38 providers.
DR DNASU; 1073; -.
DR Ensembl; ENST00000298159.11; ENSP00000298159.6; ENSG00000165410.15. [Q9Y281-1]
DR Ensembl; ENST00000341223.8; ENSP00000340635.3; ENSG00000165410.15. [Q9Y281-1]
DR Ensembl; ENST00000555765.5; ENSP00000452451.1; ENSG00000165410.15. [Q9Y281-3]
DR Ensembl; ENST00000556161.1; ENSP00000452188.1; ENSG00000165410.15. [Q9Y281-3]
DR Ensembl; ENST00000672163.1; ENSP00000500375.1; ENSG00000165410.15. [Q9Y281-1]
DR Ensembl; ENST00000672517.1; ENSP00000500532.1; ENSG00000165410.15. [Q9Y281-1]
DR Ensembl; ENST00000673315.1; ENSP00000500002.1; ENSG00000165410.15. [Q9Y281-3]
DR GeneID; 1073; -.
DR KEGG; hsa:1073; -.
DR MANE-Select; ENST00000298159.11; ENSP00000298159.6; NM_138638.5; NP_619579.1.
DR UCSC; uc001wsg.4; human. [Q9Y281-1]
DR CTD; 1073; -.
DR DisGeNET; 1073; -.
DR GeneCards; CFL2; -.
DR HGNC; HGNC:1875; CFL2.
DR HPA; ENSG00000165410; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; CFL2; -.
DR MIM; 601443; gene.
DR MIM; 610687; phenotype.
DR neXtProt; NX_Q9Y281; -.
DR OpenTargets; ENSG00000165410; -.
DR Orphanet; 171436; Typical nemaline myopathy.
DR PharmGKB; PA26424; -.
DR VEuPathDB; HostDB:ENSG00000165410; -.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR HOGENOM; CLU_094004_0_0_1; -.
DR InParanoid; Q9Y281; -.
DR OMA; ECKYAIY; -.
DR PhylomeDB; Q9Y281; -.
DR TreeFam; TF328601; -.
DR PathwayCommons; Q9Y281; -.
DR SignaLink; Q9Y281; -.
DR SIGNOR; Q9Y281; -.
DR BioGRID-ORCS; 1073; 5 hits in 1041 CRISPR screens.
DR ChiTaRS; CFL2; human.
DR GeneWiki; CFL2_(gene); -.
DR GenomeRNAi; 1073; -.
DR Pharos; Q9Y281; Tbio.
DR PRO; PR:Q9Y281; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9Y281; protein.
DR Bgee; ENSG00000165410; Expressed in cardiac muscle of right atrium and 189 other tissues.
DR ExpressionAtlas; Q9Y281; baseline and differential.
DR Genevisible; Q9Y281; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0031674; C:I band; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; IDA: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; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Nemaline myopathy; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..166
FT /note="Cofilin-2"
FT /id="PRO_0000214907"
FT DOMAIN 4..153
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REGION 2..55
FT /note="Interaction with CSRP3"
FT /evidence="ECO:0000269|PubMed:19752190"
FT REGION 55..105
FT /note="Interaction with CSRP3"
FT /evidence="ECO:0000269|PubMed:19752190"
FT MOTIF 30..34
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P45591"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046831"
FT VARIANT 7
FT /note="V -> M (in NEM7; unknown pathological significance;
FT dbSNP:rs397515451)"
FT /evidence="ECO:0000269|PubMed:22560515"
FT /id="VAR_075983"
FT VARIANT 35
FT /note="A -> T (in NEM7; protein is less soluble when
FT expressed in Escherichia coli; dbSNP:rs80358250)"
FT /evidence="ECO:0000269|PubMed:17160903"
FT /id="VAR_031989"
FT VARIANT 47
FT /note="I -> M (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036458"
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
