ID   COR1C_MOUSE             Reviewed;         474 AA.
AC   Q9WUM4; Q499X7; Q8VCQ5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Coronin-1C;
DE   AltName: Full=Coronin-3 {ECO:0000303|PubMed:9778037};
GN   Name=Coro1c;
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], AND TISSUE SPECIFICITY.
RX   PubMed=9778037; DOI=10.1089/dna.1998.17.779;
RA   Okumura M., Kung C., Wong S., Rodgers M., Thomas M.L.;
RT   "Definition of family of coronin-related proteins conserved between humans
RT   and mice: close genetic linkage between coronin-2 and CD45-associated
RT   protein.";
RL   DNA Cell Biol. 17:779-787(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Spinal cord, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Salivary gland;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19651142; DOI=10.1016/j.jmb.2009.07.079;
RA   Xavier C.P., Rastetter R.H., Stumpf M., Rosentreter A., Muller R.,
RA   Reimann J., Cornfine S., Linder S., van Vliet V., Hofmann A., Morgan R.O.,
RA   Fernandez M.P., Schroder R., Noegel A.A., Clemen C.S.;
RT   "Structural and functional diversity of novel coronin 1C (CRN2) isoforms in
RT   muscle.";
RL   J. Mol. Biol. 393:287-299(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, 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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [9]
RP   ACTIN BINDING, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-28;
RP   418-LYS-LYS-419 AND 427-LYS-LYS-429.
RX   PubMed=22364218; DOI=10.1042/bj20120209;
RA   Chan K.T., Roadcap D.W., Holoweckyj N., Bear J.E.;
RT   "Coronin 1C harbours a second actin-binding site that confers co-operative
RT   binding to F-actin.";
RL   Biochem. J. 444:89-96(2012).
RN   [10]
RP   FUNCTION, INTERACTION WITH RCC2 AND RAC1, AND SUBCELLULAR LOCATION.
RX   PubMed=25074804; DOI=10.1242/jcs.154864;
RA   Williamson R.C., Cowell C.A., Hammond C.L., Bergen D.J., Roper J.A.,
RA   Feng Y., Rendall T.C., Race P.R., Bass M.D.;
RT   "Coronin-1C and RCC2 guide mesenchymal migration by trafficking Rac1 and
RT   controlling GEF exposure.";
RL   J. Cell Sci. 127:4292-4307(2014).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=25925950; DOI=10.1074/jbc.m115.640367;
RA   Williamson R.C., Cowell C.A., Reville T., Roper J.A., Rendall T.C.,
RA   Bass M.D.;
RT   "Coronin-1C Protein and Caveolin Protein Provide Constitutive and Inducible
RT   Mechanisms of Rac1 Protein Trafficking.";
RL   J. Biol. Chem. 290:15437-15449(2015).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH VIM.
RX   PubMed=27178841; DOI=10.1016/j.ejcb.2016.04.004;
RA   Behrens J., Solga R., Ziemann A., Rastetter R.H., Berwanger C.,
RA   Herrmann H., Noegel A.A., Clemen C.S.;
RT   "Coronin 1C-free primary mouse fibroblasts exhibit robust rearrangements in
RT   the orientation of actin filaments, microtubules and intermediate
RT   filaments.";
RL   Eur. J. Cell Biol. 95:239-251(2016).
CC   -!- FUNCTION: Plays a role in directed cell migration by regulating the
CC       activation and subcellular location of RAC1 (PubMed:25074804,
CC       PubMed:25925950). Increases the presence of activated RAC1 at the
CC       leading edge of migrating cells (PubMed:25074804, PubMed:25925950).
CC       Required for normal organization of the cytoskeleton, including the
CC       actin cytoskeleton, microtubules and the vimentin intermediate
CC       filaments (PubMed:27178841). Required for normal cell proliferation,
CC       cell migration, and normal formation of lamellipodia (PubMed:27178841).
CC       Plays a role in endoplasmic reticulum-associated endosome fission:
CC       localizes to endosome membrane tubules and promotes recruitment of
CC       TMCC1, leading to recruitment of the endoplasmic reticulum to endosome
CC       tubules for fission. Endosome membrane fission of early and late
CC       endosomes is essential to separate regions destined for lysosomal
CC       degradation from carriers to be recycled to the plasma membrane (By
CC       similarity). Required for normal distribution of mitochondria within
CC       cells (PubMed:27178841). {ECO:0000250|UniProtKB:Q9ULV4,
CC       ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:25925950,
CC       ECO:0000269|PubMed:27178841}.
CC   -!- SUBUNIT: Homotrimer (By similarity). Binds F-actin (PubMed:22364218).
CC       Interacts with RCC2 (PubMed:25074804). Interacts preferentially with
CC       nucleotide-free and GDP-bound RAC1 (PubMed:25074804). Interacts with
CC       VIM (via head domain) (PubMed:27178841). Interacts with MICAL2; this
CC       interaction recruits MICAL2 to the actin filaments (By similarity).
CC       {ECO:0000250|UniProtKB:Q9ULV4, ECO:0000269|PubMed:22364218,
CC       ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:27178841}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19651142,
CC       ECO:0000269|PubMed:22364218, ECO:0000269|PubMed:25074804,
CC       ECO:0000269|PubMed:25925950}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:22364218,
CC       ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:25925950}; Cytoplasmic
CC       side {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:22364218,
CC       ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:25925950}. Cell
CC       projection, lamellipodium {ECO:0000269|PubMed:22364218,
CC       ECO:0000269|PubMed:27178841}. Cell projection, ruffle membrane
CC       {ECO:0000269|PubMed:25074804}. Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:22364218,
CC       ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:27178841}. Cytoplasm,
CC       cell cortex {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:22364218}.
CC       Endosome membrane {ECO:0000250|UniProtKB:Q9ULV4}. Note=Colocalizes with
CC       the actin cytoskeleton in the cytosol, and especially in the cell
CC       cortex (PubMed:19651142, PubMed:22364218, PubMed:25074804,
CC       PubMed:27178841). Colocalizes with F-actin at the leading edge of
CC       lamellipodia (PubMed:22364218). Partially colocalizes with microtubules
CC       and vimentin intermediate filaments (PubMed:27178841). Localizes to
CC       endosome membrane tubules/buds (By similarity).
CC       {ECO:0000250|UniProtKB:Q9ULV4, ECO:0000269|PubMed:19651142,
CC       ECO:0000269|PubMed:22364218, ECO:0000269|PubMed:25074804,
CC       ECO:0000269|PubMed:27178841}.
CC   -!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level)
CC       (PubMed:19651142). Detected in fibroblasts (at protein level)
CC       (PubMed:27178841). Ubiquitous (PubMed:9778037).
CC       {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:27178841,
CC       ECO:0000269|PubMed:9778037}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is essential for cortical
CC       membrane localization and oligomerization. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:27178841).
CC       Fibroblasts from mutant mice display a disordered actin cytoskeleton
CC       with a reduced width of the actin stress fibers. Likewise, these cells
CC       have several microtubule-organizing centers (MTOCs) and a disordered
CC       microbutule network (PubMed:27178841). {ECO:0000269|PubMed:27178841}.
CC   -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
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DR   EMBL; AF143957; AAD32705.1; -; mRNA.
DR   EMBL; AK079327; BAC37609.1; -; mRNA.
DR   EMBL; AK082986; BAC38722.1; -; mRNA.
DR   EMBL; AK088101; BAC40144.1; -; mRNA.
DR   EMBL; AK151017; BAE30036.1; -; mRNA.
DR   EMBL; AK151749; BAE30659.1; -; mRNA.
DR   EMBL; AK167089; BAE39246.1; -; mRNA.
DR   EMBL; AK159506; BAE35139.1; -; mRNA.
DR   EMBL; CH466529; EDL19932.1; -; Genomic_DNA.
DR   EMBL; BC019444; AAH19444.1; -; mRNA.
DR   EMBL; BC085498; AAH85498.1; -; mRNA.
DR   EMBL; BC099671; AAH99671.1; -; mRNA.
DR   CCDS; CCDS19555.1; -.
DR   RefSeq; NP_035909.2; NM_011779.3.
DR   AlphaFoldDB; Q9WUM4; -.
DR   SMR; Q9WUM4; -.
DR   BioGRID; 204714; 169.
DR   IntAct; Q9WUM4; 151.
DR   MINT; Q9WUM4; -.
DR   STRING; 10090.ENSMUSP00000004646; -.
DR   GlyGen; Q9WUM4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9WUM4; -.
DR   PhosphoSitePlus; Q9WUM4; -.
DR   SwissPalm; Q9WUM4; -.
DR   CPTAC; non-CPTAC-3699; -.
DR   CPTAC; non-CPTAC-3780; -.
DR   EPD; Q9WUM4; -.
DR   jPOST; Q9WUM4; -.
DR   MaxQB; Q9WUM4; -.
DR   PaxDb; 10090-ENSMUSP00000004646; -.
DR   ProteomicsDB; 277994; -.
DR   Pumba; Q9WUM4; -.
DR   Antibodypedia; 30774; 320 antibodies from 33 providers.
DR   DNASU; 23790; -.
DR   Ensembl; ENSMUST00000004646.13; ENSMUSP00000004646.7; ENSMUSG00000004530.13.
DR   GeneID; 23790; -.
DR   KEGG; mmu:23790; -.
DR   UCSC; uc008yyu.1; mouse.
DR   AGR; MGI:1345964; -.
DR   CTD; 23603; -.
DR   MGI; MGI:1345964; Coro1c.
DR   VEuPathDB; HostDB:ENSMUSG00000004530; -.
DR   eggNOG; KOG0303; Eukaryota.
DR   GeneTree; ENSGT00940000156488; -.
DR   HOGENOM; CLU_026859_0_1_1; -.
DR   InParanoid; Q9WUM4; -.
DR   OMA; NFQDDIY; -.
DR   OrthoDB; 5474889at2759; -.
DR   PhylomeDB; Q9WUM4; -.
DR   TreeFam; TF314280; -.
DR   BioGRID-ORCS; 23790; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Coro1c; mouse.
DR   PRO; PR:Q9WUM4; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9WUM4; Protein.
DR   Bgee; ENSMUSG00000004530; Expressed in stroma of bone marrow and 258 other cell types or tissues.
DR   ExpressionAtlas; Q9WUM4; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR   GO; GO:0016600; C:flotillin complex; IDA:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR   GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR   GO; GO:0000147; P:actin cortical patch assembly; TAS:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; TAS:MGI.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
DR   GO; GO:0022038; P:corpus callosum development; IMP:MGI.
DR   GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR   GO; GO:0140285; P:endosome fission; ISS:UniProtKB.
DR   GO; GO:0097750; P:endosome membrane tubulation; ISS:UniProtKB.
DR   GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR   GO; GO:0090148; P:membrane fission; ISS:UniProtKB.
DR   GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:MGI.
DR   GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR   GO; GO:0001755; P:neural crest cell migration; ISO:MGI.
DR   GO; GO:0006909; P:phagocytosis; TAS:MGI.
DR   GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; ISO:MGI.
DR   GO; GO:0010632; P:regulation of epithelial cell migration; ISO:MGI.
DR   GO; GO:0010762; P:regulation of fibroblast migration; IMP:UniProtKB.
DR   GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:1900027; P:regulation of ruffle assembly; IGI:UniProtKB.
DR   GO; GO:1900024; P:regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR   GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015048; DUF1899.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR10856; CORONIN; 1.
DR   PANTHER; PTHR10856:SF10; CORONIN-1C; 1.
DR   Pfam; PF08953; DUF1899; 1.
DR   Pfam; PF00400; WD40; 3.
DR   Pfam; PF16300; WD40_4; 1.
DR   SMART; SM01166; DUF1899; 1.
DR   SMART; SM01167; DUF1900; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   Genevisible; Q9WUM4; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cell membrane; Cell projection; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Endosome; Membrane; Reference proteome; Repeat;
KW   WD repeat.
FT   CHAIN           1..474
FT                   /note="Coronin-1C"
FT                   /id="PRO_0000050927"
FT   REPEAT          78..118
FT                   /note="WD 1"
FT   REPEAT          128..168
FT                   /note="WD 2"
FT   REPEAT          172..202
FT                   /note="WD 3"
FT   REPEAT          215..249
FT                   /note="WD 4"
FT   REPEAT          263..303
FT                   /note="WD 5"
FT   COILED          435..474
FT                   /evidence="ECO:0000250"
FT   MOD_RES         446
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULV4"
FT   MUTAGEN         28
FT                   /note="R->D: Decreased actin-binding. Loss of actin
FT                   binding; when associated with 418-E-E-419 and 427-E-E-428."
FT                   /evidence="ECO:0000269|PubMed:22364218"
FT   MUTAGEN         418..419
FT                   /note="KK->EE: Decreased actin-binding. Loss of actin
FT                   binding; when associated with D-28 and 427-E-E-428."
FT                   /evidence="ECO:0000269|PubMed:22364218"
FT   MUTAGEN         427..428
FT                   /note="KK->EE: Decreased actin-binding. Loss of actin
FT                   binding; when associated with D-28 and 418-E-E-419."
FT                   /evidence="ECO:0000269|PubMed:22364218"
FT   CONFLICT        66
FT                   /note="T -> S (in Ref. 1; AAD32705)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        422
FT                   /note="L -> F (in Ref. 1; AAD32705)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   474 AA;  53121 MW;  4B1C41E1BB59AFCF CRC64;
     MRRVVRQSKF RHVFGQAVKN DQCYDDIRVS RVTWDSSFCA VNPRFVAIII EASGGGAFLV
     LPLHKTGRID KSYPTVCGHT GPVLDIDWCP HNDQVIASGS EDCTVMVWQI PENGLTLSLT
     EPVVILEGHS KRVGIVAWHP TARNVLLSAG CDNAIIIWNV GTGEALINLD DMHSDMIYNV
     SWSRNGSLIC TASKDKKVRV IDPRKQEIVA EKEKAHEGAR PMRAIFLADG NVFTTGFSRM
     SERQLALWNP KNMQEPIALH EMDTSNGVLL PFYDPDTSII YLCGKGDSSI RYFEITDESP
     YVHYLNTFSS KEPQRGMGYM PKRGLDVNKC EIARFFKLHE RKCEPIIMTV PRKSDLFQDD
     LYPDTAGPEA ALEAEEWFEG KNADPILISL KHGYIPGKNR DLKVVKKNIL DSKPAANKKS
     ELSCAPKKPT DTASVQNEAK LDEILKEIKS IKETICSQDE RISKLEQQLA KMAA
//