COF1_MOUSE
ID COF1_MOUSE Reviewed; 166 AA.
AC P18760;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Cofilin-1;
DE AltName: Full=Cofilin, non-muscle isoform;
GN Name=Cfl1;
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=Swiss Webster;
RX PubMed=2349104; DOI=10.1093/nar/18.10.3053;
RA Moriyama K., Matsumoto S., Nishida E., Sakai H., Yahara I.;
RT "Nucleotide sequence of mouse cofilin cDNA.";
RL Nucleic Acids Res. 18:3053-3053(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PROTEIN SEQUENCE OF 2-13 AND 153-166, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 54-73 AND 96-112, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP FUNCTION, ACTIN BINDING, 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 [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15649475; DOI=10.1016/j.ydbio.2004.11.010;
RA Gurniak C.B., Perlas E., Witke W.;
RT "The actin depolymerizing factor n-cofilin is essential for neural tube
RT morphogenesis and neural crest cell migration.";
RL Dev. Biol. 278:231-241(2005).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-68 AND TYR-140, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3 AND SER-8, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION AT SER-3, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=25107909; DOI=10.1074/jbc.m114.588079;
RA Lee I.C., Leung T., Tan I.;
RT "Adaptor protein LRAP25 mediates myotonic dystrophy kinase-related Cdc42-
RT binding kinase (MRCK) regulation of LIMK1 protein in lamellipodial F-actin
RT dynamics.";
RL J. Biol. Chem. 289:26989-27003(2014).
RN [13]
RP FUNCTION, INTERACTION WITH TLE6 AND NLRP5, AND MUTAGENESIS OF SER-3.
RX PubMed=25208553; DOI=10.1038/ncomms5887;
RA Yu X.J., Yi Z., Gao Z., Qin D., Zhai Y., Chen X., Ou-Yang Y., Wang Z.B.,
RA Zheng P., Zhu M.S., Wang H., Sun Q.Y., Dean J., Li L.;
RT "The subcortical maternal complex controls symmetric division of mouse
RT zygotes by regulating F-actin dynamics.";
RL Nat. Commun. 5:4887-4887(2014).
RN [14]
RP INTERACTION WITH C9ORF72, AND SUBCELLULAR LOCATION.
RX PubMed=27723745; DOI=10.1038/nn.4407;
RA Sivadasan R., Hornburg D., Drepper C., Frank N., Jablonka S., Hansel A.,
RA Lojewski X., Sterneckert J., Hermann A., Shaw P.J., Ince P.G., Mann M.,
RA Meissner F., Sendtner M.;
RT "C9ORF72 interaction with cofilin modulates actin dynamics in motor
RT neurons.";
RL Nat. Neurosci. 19:1610-1618(2016).
RN [15]
RP PHOSPHORYLATION AT SER-3; THR-63; TYR-82 AND SER-156, ACETYLATION AT ALA-2,
RP 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).
CC -!- FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin
CC depolymerizing activity (PubMed:11809832). 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:25208553). Required for the
CC centralization of the mitotic spindle and symmetric division of zygotes
CC (PubMed:25208553). Plays a role in the regulation of cell morphology
CC and cytoskeletal organization in epithelial cells (By similarity).
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 (By similarity). Required for
CC neural tube morphogenesis and neural crest cell migration
CC (PubMed:15649475). {ECO:0000250|UniProtKB:P23528,
CC ECO:0000269|PubMed:11809832, ECO:0000269|PubMed:15649475,
CC ECO:0000269|PubMed:25208553}.
CC -!- SUBUNIT: Can bind G- and F-actin in a 1:1 ratio of cofilin to actin
CC (PubMed:11809832). 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 and NLRP5
CC (PubMed:25208553). Interacts with C9orf72 (PubMed:27723745).
CC {ECO:0000250|UniProtKB:P10668, ECO:0000269|PubMed:11809832,
CC ECO:0000269|PubMed:25208553, ECO:0000269|PubMed:27723745}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:P10668}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P10668}. Cell
CC projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P10668}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium membrane
CC {ECO:0000250|UniProtKB:P10668}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P10668}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:25107909}. Cell projection, growth cone
CC {ECO:0000269|PubMed:27723745}. Cell projection, axon
CC {ECO:0000269|PubMed:27723745}. 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. {ECO:0000250|UniProtKB:P23528}.
CC -!- TISSUE SPECIFICITY: Widely distributed in various tissues. Not found in
CC skeletal muscle. {ECO:0000269|PubMed:11809832}.
CC -!- DEVELOPMENTAL STAGE: In 10.5 dpc embryo somites is expressed in a
CC ventral cell layer (myotome). {ECO:0000269|PubMed:15649475}.
CC -!- PTM: Inactivated by phosphorylation on Ser-3. Phosphorylated on Ser-3
CC in resting cells (PubMed:25107909). Dephosphorylated by
CC PDXP/chronophin; 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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:25107909}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; D00472; BAA00364.1; -; mRNA.
DR EMBL; BC046225; AAH46225.1; -; mRNA.
DR EMBL; BC058726; AAH58726.1; -; mRNA.
DR CCDS; CCDS84409.1; -.
DR PIR; S12584; S12584.
DR RefSeq; NP_031713.1; NM_007687.5.
DR AlphaFoldDB; P18760; -.
DR BMRB; P18760; -.
DR SMR; P18760; -.
DR BioGRID; 198684; 23.
DR DIP; DIP-38073N; -.
DR IntAct; P18760; 12.
DR MINT; P18760; -.
DR STRING; 10090.ENSMUSP00000112259; -.
DR iPTMnet; P18760; -.
DR PhosphoSitePlus; P18760; -.
DR SwissPalm; P18760; -.
DR REPRODUCTION-2DPAGE; P18760; -.
DR SWISS-2DPAGE; P18760; -.
DR CPTAC; non-CPTAC-3906; -.
DR EPD; P18760; -.
DR jPOST; P18760; -.
DR PaxDb; P18760; -.
DR PeptideAtlas; P18760; -.
DR PRIDE; P18760; -.
DR ProteomicsDB; 283418; -.
DR TopDownProteomics; P18760; -.
DR Antibodypedia; 16010; 1070 antibodies from 41 providers.
DR DNASU; 12631; -.
DR Ensembl; ENSMUST00000209469; ENSMUSP00000147514; ENSMUSG00000056201.
DR GeneID; 12631; -.
DR KEGG; mmu:12631; -.
DR UCSC; uc008gdq.2; mouse.
DR CTD; 1072; -.
DR MGI; MGI:101757; Cfl1.
DR VEuPathDB; HostDB:ENSMUSG00000056201; -.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR InParanoid; P18760; -.
DR OMA; QEDIEWE; -.
DR OrthoDB; 1370477at2759; -.
DR PhylomeDB; P18760; -.
DR BioGRID-ORCS; 12631; 6 hits in 20 CRISPR screens.
DR ChiTaRS; Cfl1; mouse.
DR PRO; PR:P18760; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P18760; protein.
DR Bgee; ENSMUSG00000056201; Expressed in midbrain and 73 other tissues.
DR ExpressionAtlas; P18760; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0090732; C:cofilin-actin rod; ISO:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:ARUK-UCL.
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:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0030030; P:cell projection organization; ISO:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; ISO:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR GO; GO:0071354; P:cellular response to interleukin-6; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:MGI.
DR GO; GO:0051293; P:establishment of spindle localization; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; ISO:MGI.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; ISO:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:2000146; P:negative regulation of cell motility; ISO:MGI.
DR GO; GO:0045792; P:negative regulation of cell size; ISO:MGI.
DR GO; GO:1902951; P:negative regulation of dendritic spine maintenance; ISO:MGI.
DR GO; GO:0010593; P:negative regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:1905875; P:negative regulation of postsynaptic density organization; ISO:MGI.
DR GO; GO:0051511; P:negative regulation of unidimensional cell growth; ISO:MGI.
DR GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR GO; GO:0001842; P:neural fold formation; IMP:MGI.
DR GO; GO:0044794; P:positive regulation by host of viral process; ISO:MGI.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IDA:CACAO.
DR GO; GO:2000814; P:positive regulation of barbed-end actin filament capping; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:2000147; P:positive regulation of cell motility; ISO:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:2000784; P:positive regulation of establishment of cell polarity regulating cell shape; ISO:MGI.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; ISO:MGI.
DR GO; GO:1905873; P:positive regulation of protein localization to cell leading edge; ISO:MGI.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043200; P:response to amino acid; IDA:MGI.
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 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 Acetylation; Actin-binding; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Isopeptide bond; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19131326"
FT CHAIN 2..166
FT /note="Cofilin-1"
FT /id="PRO_0000214900"
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.3,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25107909,
FT ECO:0000269|PubMed:30550596, ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23528"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P23528"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23528"
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:17947660"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23528"
FT MOD_RES 82
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:30550596"
FT MOD_RES 140
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:17947660"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23528"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30550596,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P23528"
FT MUTAGEN 3
FT /note="S->A: Decreases abundance and increases
FT disorganization of zygotic subcortical F-actin, disrupts
FT centralization of the mitotic spindle and leads to
FT asymmetric two-cell embryos."
FT /evidence="ECO:0000269|PubMed:25208553"
FT MUTAGEN 3
FT /note="S->E: No effect on zygotic subcortical F-actin
FT abundance and centralization of the mitotic spindle."
FT /evidence="ECO:0000269|PubMed:25208553"
SQ SEQUENCE 166 AA; 18560 MW; 19834E8CA80747B2 CRC64;
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV
GQTVDDPYTT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPENAP LKSKMIYASS
KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL
