COF1_HUMAN
ID COF1_HUMAN Reviewed; 166 AA.
AC P23528; B3KUQ1; Q53Y87; Q9UCA2;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 238.
DE RecName: Full=Cofilin-1;
DE AltName: Full=18 kDa phosphoprotein;
DE Short=p18;
DE AltName: Full=Cofilin, non-muscle isoform;
GN Name=CFL1; Synonyms=CFL;
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].
RC TISSUE=Placenta;
RX PubMed=2263493; DOI=10.1093/nar/18.23.7169;
RA Ogawa K., Tashima M., Yumoto Y., Okuda T., Sawada H., Okuma M.,
RA Maruyama Y.;
RT "Coding sequence of human placenta cofilin cDNA.";
RL Nucleic Acids Res. 18:7169-7169(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pre-B cell;
RX PubMed=7552146; DOI=10.1159/000472281;
RA van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J.,
RA Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C.,
RA van Ommen G.J.B., Buys C.H.C.M.;
RT "A provisional transcript map of the spinal muscular atrophy (SMA) critical
RT region.";
RL Eur. J. Hum. Genet. 3:87-95(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8800436; DOI=10.1111/j.1469-1809.1996.tb00423.x;
RA Gillett G.T., Fox M.F., Rowe P.S.N., Casimir C.M., Povey S.;
RT "Mapping of human non-muscle type cofilin (CFL1) to chromosome 11q13 and
RT muscle-type cofilin (CFL2) to chromosome 14.";
RL Ann. Hum. Genet. 60:201-211(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Ovary, Placenta, and Uterus;
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 [8]
RP PROTEIN SEQUENCE OF 2-21.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP PROTEIN SEQUENCE OF 2-13 AND 54-73, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Quadroni M., Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 34-45; 54-73; 82-92; 96-112; 133-146 AND 153-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 52-71.
RC TISSUE=Platelet;
RX PubMed=8037689; DOI=10.1042/bj3010041;
RA Davidson M.M., Haslam R.J.;
RT "Dephosphorylation of cofilin in stimulated platelets: roles for a GTP-
RT binding protein and Ca2+.";
RL Biochem. J. 301:41-47(1994).
RN [12]
RP FUNCTION, AND ACTIN BINDING.
RX PubMed=11812157; DOI=10.1006/jmbi.2001.5280;
RA Yeoh S., Pope B., Mannherz H.G., Weeds A.;
RT "Determining the differences in actin binding by human ADF and cofilin.";
RL J. Mol. Biol. 315:911-925(2002).
RN [13]
RP PHOSPHORYLATION AT SER-3 BY NRK.
RX PubMed=12837278; DOI=10.1016/s0014-4827(03)00136-8;
RA Nakano K., Kanai-Azuma M., Kanai Y., Moriyama K., Yazaki K., Hayashi Y.,
RA Kitamura N.;
RT "Cofilin phosphorylation and actin polymerization by NRK/NESK, a member of
RT the germinal center kinase family.";
RL Exp. Cell Res. 287:219-227(2003).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEPHOSPHORYLATION BY PDXP.
RX PubMed=15580268; DOI=10.1038/ncb1201;
RA Gohla A., Birkenfeld J., Bokoch G.M.;
RT "Chronophin, a novel HAD-type serine protein phosphatase, regulates
RT cofilin-dependent actin dynamics.";
RL Nat. Cell Biol. 7:21-29(2005).
RN [17]
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 [18]
RP INDUCTION BY EV71 INFECTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT differential cellular gene expression in response to enterovirus 71
RT infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-156, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
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 [21]
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].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-68 AND SER-156, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-73 AND LYS-144, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3; THR-25 AND SER-156, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [25]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [26]
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 [27]
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].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [28]
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 [29]
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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-41 AND SER-156, AND
RP IDENTIFICATION BY MASS 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 [31]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=23633677; DOI=10.1126/scisignal.2003627;
RA Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B.,
RA Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A., Bonecchi R.,
RA Locati M.;
RT "Beta-arrestin-dependent activation of the cofilin pathway is required for
RT the scavenging activity of the atypical chemokine receptor D6.";
RL Sci. Signal. 6:RA30-RA30(2013).
RN [32]
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 [33]
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=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [34]
RP INTERACTION WITH HRSV MATRIX PROTEIN (MICROBIAL INFECTION).
RX PubMed=25556234; DOI=10.1074/mcp.m114.044107;
RA Kipper S., Hamad S., Caly L., Avrahami D., Bacharach E., Jans D.A.,
RA Gerber D., Bajorek M.;
RT "New host factors important for respiratory syncytial virus (RSV)
RT replication revealed by a novel microfluidics screen for interactors of
RT matrix (M) protein.";
RL Mol. Cell. Proteomics 14:532-543(2015).
RN [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-132, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [36]
RP PHOSPHORYLATION AT SER-3; THR-63; TYR-82; SER-108 AND SER-156, ACETYLATION
RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=30550596; DOI=10.1371/journal.pone.0208979;
RA Prudent R., Demoncheaux N., Diemer H., Collin-Faure V., Kapur R.,
RA Paublant F., Lafanechere L., Cianferani S., Rabilloud T.;
RT "A quantitative proteomic analysis of cofilin phosphorylation in myeloid
RT cells and its modulation using the LIM kinase inhibitor Pyr1.";
RL PLoS ONE 13:E0208979-E0208979(2018).
RN [37]
RP STRUCTURE BY NMR.
RX PubMed=14627701; DOI=10.1074/jbc.m310148200;
RA Pope B.J., Zierler-Gould K.M., Kuhne R., Weeds A.G., Ball L.J.;
RT "Solution structure of human cofilin: actin binding, pH sensitivity, and
RT relationship to actin-depolymerizing factor.";
RL J. Biol. Chem. 279:4840-4848(2004).
CC -!- FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin
CC depolymerizing activity (PubMed:11812157). In conjunction with the
CC subcortical maternal complex (SCMC), plays an essential role for
CC zygotes to progress beyond the first embryonic cell divisions via
CC regulation of actin dynamics (PubMed:15580268). Required for the
CC centralization of the mitotic spindle and symmetric division of zygotes
CC (By similarity). Plays a role in the regulation of cell morphology and
CC cytoskeletal organization in epithelial cells (PubMed:21834987).
CC Required for the up-regulation of atypical chemokine receptor ACKR2
CC from endosomal compartment to cell membrane, increasing its efficiency
CC in chemokine uptake and degradation (PubMed:23633677). Required for
CC neural tube morphogenesis and neural crest cell migration (By
CC similarity). {ECO:0000250|UniProtKB:P18760,
CC ECO:0000269|PubMed:11812157, ECO:0000269|PubMed:15580268,
CC ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:23633677}.
CC -!- SUBUNIT: Can bind G- and F-actin in a 1:1 ratio of cofilin to actin
CC (PubMed:11812157). It is a major component of intranuclear and
CC cytoplasmic actin rods (By similarity). Interacts with the subcortical
CC maternal complex (SCMC) via interaction with TLE6 isoform 1 and NLRP5
CC (By similarity). Interacts with C9orf72 (By similarity).
CC {ECO:0000250|UniProtKB:P10668, ECO:0000250|UniProtKB:P18760,
CC ECO:0000269|PubMed:11812157}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human respiratory
CC syncytial virus (HRSV) matrix protein; this interaction probably
CC facilitates viral replication. {ECO:0000269|PubMed:25556234}.
CC -!- INTERACTION:
CC P23528; P60709: ACTB; NbExp=9; IntAct=EBI-352733, EBI-353944;
CC P23528; P63261: ACTG1; NbExp=9; IntAct=EBI-352733, EBI-351292;
CC P23528; P54253: ATXN1; NbExp=11; IntAct=EBI-352733, EBI-930964;
CC P23528; Q549N0: CFL2; NbExp=3; IntAct=EBI-352733, EBI-10201319;
CC P23528; P00533: EGFR; NbExp=3; IntAct=EBI-352733, EBI-297353;
CC P23528; P57058: HUNK; NbExp=2; IntAct=EBI-352733, EBI-3959804;
CC P23528; P53667: LIMK1; NbExp=3; IntAct=EBI-352733, EBI-444403;
CC P23528; Q96CV9: OPTN; NbExp=3; IntAct=EBI-352733, EBI-748974;
CC P23528; Q13393: PLD1; NbExp=4; IntAct=EBI-352733, EBI-2827556;
CC P23528; O14939: PLD2; NbExp=2; IntAct=EBI-352733, EBI-1053996;
CC P23528; Q1KLZ0: PS1TP5BP1; NbExp=3; IntAct=EBI-352733, EBI-9978131;
CC P23528; Q8WYL5: SSH1; NbExp=2; IntAct=EBI-352733, EBI-1222387;
CC P23528; P63104: YWHAZ; NbExp=3; IntAct=EBI-352733, EBI-347088;
CC P23528; P0DOE7: M; Xeno; NbExp=2; IntAct=EBI-352733, EBI-10042882;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:15580268}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15580268}. Cell projection,
CC ruffle membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane
CC protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side
CC {ECO:0000269|PubMed:15580268}. Cell projection, lamellipodium membrane
CC {ECO:0000269|PubMed:15580268}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15580268}; Cytoplasmic side
CC {ECO:0000269|PubMed:15580268}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P18760}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:P18760}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P18760}. Note=Colocalizes with the actin
CC cytoskeleton in membrane ruffles and lamellipodia. Detected at the
CC cleavage furrow and contractile ring during cytokinesis. Almost
CC completely in nucleus in cells exposed to heat shock or 10% dimethyl
CC sulfoxide.
CC -!- TISSUE SPECIFICITY: Widely distributed in various tissues.
CC -!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71) infection
CC (at protein level). {ECO:0000269|PubMed:16548883}.
CC -!- PTM: Inactivated by phosphorylation on Ser-3. Phosphorylated on Ser-3
CC in resting cells (By similarity). Dephosphorylated by PDXP/chronophin;
CC this restores its activity in promoting actin filament
CC depolymerization. The phosphorylation of Ser-24 may prevent recognition
CC of the nuclear localization signal (By similarity). Phosphorylated via
CC a ARRB1-RAC1-LIMK1-PAK1 cascade upon active ligand stimulation of
CC atypical chemokine receptor ACKR2. {ECO:0000250|UniProtKB:P45695,
CC ECO:0000269|PubMed:12837278, ECO:0000269|PubMed:23633677}.
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; D00682; BAA00589.1; -; mRNA.
DR EMBL; U21909; AAA64501.1; -; mRNA.
DR EMBL; X95404; CAA64685.1; -; mRNA.
DR EMBL; BT006846; AAP35492.1; -; mRNA.
DR EMBL; AK097690; BAG53513.1; -; mRNA.
DR EMBL; CH471076; EAW74449.1; -; Genomic_DNA.
DR EMBL; BC011005; AAH11005.1; -; mRNA.
DR EMBL; BC012265; AAH12265.1; -; mRNA.
DR EMBL; BC012318; AAH12318.1; -; mRNA.
DR EMBL; BC018256; AAH18256.1; -; mRNA.
DR CCDS; CCDS8114.1; -.
DR PIR; S12632; S12632.
DR RefSeq; NP_005498.1; NM_005507.2.
DR PDB; 1Q8G; NMR; -; A=1-166.
DR PDB; 1Q8X; NMR; -; A=1-166.
DR PDB; 3J0S; EM; 9.00 A; M/N/O/P/Q/R/S/T/U/V/W/X=1-166.
DR PDB; 4BEX; X-ray; 2.80 A; 1=1-166.
DR PDB; 5HVK; X-ray; 3.50 A; B/D=2-166.
DR PDB; 5L6W; X-ray; 2.53 A; C=1-166.
DR PDB; 6UBY; EM; 7.50 A; I=1-166.
DR PDB; 6UC0; EM; 7.50 A; I=1-166.
DR PDB; 6UC4; EM; 9.20 A; I/M/N/O/P=1-166.
DR PDB; 6VAO; EM; 3.40 A; F/G/H/I/J=1-166.
DR PDBsum; 1Q8G; -.
DR PDBsum; 1Q8X; -.
DR PDBsum; 3J0S; -.
DR PDBsum; 4BEX; -.
DR PDBsum; 5HVK; -.
DR PDBsum; 5L6W; -.
DR PDBsum; 6UBY; -.
DR PDBsum; 6UC0; -.
DR PDBsum; 6UC4; -.
DR PDBsum; 6VAO; -.
DR AlphaFoldDB; P23528; -.
DR BMRB; P23528; -.
DR SMR; P23528; -.
DR BioGRID; 107499; 284.
DR CORUM; P23528; -.
DR DIP; DIP-33000N; -.
DR IntAct; P23528; 123.
DR MINT; P23528; -.
DR STRING; 9606.ENSP00000432660; -.
DR ChEMBL; CHEMBL1075129; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR CarbonylDB; P23528; -.
DR GlyGen; P23528; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P23528; -.
DR MetOSite; P23528; -.
DR PhosphoSitePlus; P23528; -.
DR SwissPalm; P23528; -.
DR BioMuta; CFL1; -.
DR DMDM; 116848; -.
DR DOSAC-COBS-2DPAGE; P23528; -.
DR OGP; P23528; -.
DR REPRODUCTION-2DPAGE; IPI00012011; -.
DR SWISS-2DPAGE; P23528; -.
DR UCD-2DPAGE; P23528; -.
DR EPD; P23528; -.
DR jPOST; P23528; -.
DR MassIVE; P23528; -.
DR PaxDb; P23528; -.
DR PeptideAtlas; P23528; -.
DR PRIDE; P23528; -.
DR ProteomicsDB; 54128; -.
DR TopDownProteomics; P23528; -.
DR Antibodypedia; 16010; 1070 antibodies from 41 providers.
DR DNASU; 1072; -.
DR Ensembl; ENST00000308162.10; ENSP00000309629.5; ENSG00000172757.13.
DR Ensembl; ENST00000525451.6; ENSP00000432660.1; ENSG00000172757.13.
DR GeneID; 1072; -.
DR KEGG; hsa:1072; -.
DR MANE-Select; ENST00000308162.10; ENSP00000309629.5; NM_005507.3; NP_005498.1.
DR CTD; 1072; -.
DR DisGeNET; 1072; -.
DR GeneCards; CFL1; -.
DR HGNC; HGNC:1874; CFL1.
DR HPA; ENSG00000172757; Low tissue specificity.
DR MIM; 601442; gene.
DR neXtProt; NX_P23528; -.
DR OpenTargets; ENSG00000172757; -.
DR PharmGKB; PA26423; -.
DR VEuPathDB; HostDB:ENSG00000172757; -.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR InParanoid; P23528; -.
DR OMA; ASEICEM; -.
DR OrthoDB; 1370477at2759; -.
DR PhylomeDB; P23528; -.
DR TreeFam; TF328601; -.
DR PathwayCommons; P23528; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR SignaLink; P23528; -.
DR SIGNOR; P23528; -.
DR BioGRID-ORCS; 1072; 404 hits in 1084 CRISPR screens.
DR ChiTaRS; CFL1; human.
DR EvolutionaryTrace; P23528; -.
DR GeneWiki; Cofilin_1; -.
DR GenomeRNAi; 1072; -.
DR Pharos; P23528; Tbio.
DR PRO; PR:P23528; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P23528; protein.
DR Bgee; ENSG00000172757; Expressed in ileal mucosa and 216 other tissues.
DR ExpressionAtlas; P23528; baseline and differential.
DR Genevisible; P23528; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
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:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0051293; P:establishment of spindle localization; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0044794; P:positive regulation by host of viral process; IMP:AgBase.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR CDD; cd11286; ADF_cofilin_like; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR IDEAL; IID00627; -.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR017904; ADF/Cofilin.
DR InterPro; IPR027234; Cofilin_1.
DR PANTHER; PTHR11913; PTHR11913; 1.
DR PANTHER; PTHR11913:SF17; PTHR11913:SF17; 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; Acetylation; Actin-binding; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Host-virus interaction;
KW Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.9,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..166
FT /note="Cofilin-1"
FT /id="PRO_0000214898"
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:0000269|PubMed:30550596, ECO:0000269|Ref.9,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 3
FT /note="Phosphoserine; by NRK"
FT /evidence="ECO:0000269|PubMed:12837278,
FT ECO:0000269|PubMed:30550596, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18760"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:30550596"
FT MOD_RES 68
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 82
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:30550596"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30550596"
FT MOD_RES 140
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30550596,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:5L6W"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:5L6W"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:5L6W"
FT STRAND 44..56
FT /evidence="ECO:0007829|PDB:5L6W"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5L6W"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:5L6W"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:5L6W"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:4BEX"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:5L6W"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:5L6W"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:5L6W"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:5L6W"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:5L6W"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:5L6W"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4BEX"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:5L6W"
SQ SEQUENCE 166 AA; 18502 MW; 589EF8FC1EC13719 CRC64;
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV
GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS
KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL
