ENAH_MOUSE
ID ENAH_MOUSE Reviewed; 802 AA.
AC Q03173; P70430; P70431; P70432; P70433; Q5D053;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Protein enabled homolog;
DE AltName: Full=NPC-derived proline-rich protein 1;
DE Short=NDPP-1;
GN Name=Enah; Synonyms=Mena, Ndpp1;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1420303; DOI=10.1016/0167-4781(92)90156-t;
RA Sazuka T., Tomooka Y., Kathju S., Ikawa Y., Noda M., Kumar S.;
RT "Identification of a developmentally regulated gene in the mouse central
RT nervous system which encodes a novel proline rich protein.";
RL Biochim. Biophys. Acta 1132:240-248(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), FUNCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, ROLE IN L.MONOCYTOGENES MOBILITY,
RP MISCELLANEOUS, AND INTERACTION WITH PFN1.
RC TISSUE=Brain;
RX PubMed=8861907; DOI=10.1016/s0092-8674(00)81341-0;
RA Gertler F.B., Niebuhr K., Reinhard M., Wehland J., Soriano P.;
RT "Mena, a relative of VASP and Drosophila Enabled, is implicated in the
RT control of microfilament dynamics.";
RL Cell 87:227-239(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP INTERACTION WITH PRPF40A.
RX PubMed=9171351; DOI=10.1093/emboj/16.9.2376;
RA Bedford M.T., Chan D.C., Leder P.;
RT "FBP WW domains and the Abl SH3 domain bind to a specific class of proline-
RT rich ligands.";
RL EMBO J. 16:2376-2383(1997).
RN [5]
RP INTERACTION WITH APBB1; NEDD4 AND YAP1.
RX PubMed=9407065; DOI=10.1074/jbc.272.52.32869;
RA Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F., Russo T.,
RA Sudol M.;
RT "The WW domain of neural protein FE65 interacts with proline-rich motifs in
RT Mena, the mammalian homolog of Drosophila enabled.";
RL J. Biol. Chem. 272:32869-32877(1997).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=10069337; DOI=10.1016/s0896-6273(00)81092-2;
RA Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M., Macklis J.D.,
RA Kwiatkowski D., Soriano P., Gertler F.B.;
RT "Mena is required for neurulation and commissure formation.";
RL Neuron 22:313-325(1999).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-255 AND SER-637.
RX PubMed=12134088; DOI=10.1091/mbc.e01-10-0102;
RA Loureiro J.J., Rubinson D.A., Bear J.E., Baltus G.A., Kwiatkowski A.V.,
RA Gertler F.B.;
RT "Critical roles of phosphorylation and actin binding motifs, but not the
RT central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein
RT (VASP) function during cell migration.";
RL Mol. Biol. Cell 13:2533-2546(2002).
RN [8]
RP INTERACTION WITH ROBO4.
RC STRAIN=FVB/N;
RX PubMed=12941633; DOI=10.1016/s0012-1606(03)00258-6;
RA Park K.W., Morrison C.M., Sorensen L.K., Jones C.A., Rao Y., Chien C.-B.,
RA Wu J.Y., Urness L.D., Li D.Y.;
RT "Robo4 is a vascular-specific receptor that inhibits endothelial
RT migration.";
RL Dev. Biol. 261:251-267(2003).
RN [9]
RP ALTERNATIVE SPLICING (ISOFORM 6), PHOSPHORYLATION AT TYR-557, AND
RP INTERACTION WITH ABI1.
RX PubMed=12672821; DOI=10.1074/jbc.m301447200;
RA Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H.,
RA Shishido T.;
RT "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian
RT enabled (Mena) by c-Abl kinase.";
RL J. Biol. Chem. 278:21685-21692(2003).
RN [10]
RP INTERACTION WITH DNMBP.
RX PubMed=14506234; DOI=10.1074/jbc.m308104200;
RA Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
RA Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
RT "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
RT domains, links dynamin to regulation of the actin cytoskeleton.";
RL J. Biol. Chem. 278:49031-49043(2003).
RN [11]
RP INTERACTION WITH FAT1.
RX PubMed=15148305; DOI=10.1083/jcb.200403006;
RA Tanoue T., Takeichi M.;
RT "Mammalian Fat1 cadherin regulates actin dynamics and cell-cell contact.";
RL J. Cell Biol. 165:517-528(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [13]
RP FUNCTION, AND PHOSPHORYLATION AT SER-255.
RX PubMed=15066263; DOI=10.1016/s0896-6273(04)00108-4;
RA Lebrand C., Dent E.W., Strasser G.A., Lanier L.M., Krause M.,
RA Svitkina T.M., Borisy G.G., Gertler F.B.;
RT "Critical role of Ena/VASP proteins for filopodia formation in neurons and
RT in function downstream of netrin-1.";
RL Neuron 42:37-49(2004).
RN [14]
RP INTERACTION WITH APBB1IP.
RX PubMed=15642358; DOI=10.1016/j.febslet.2004.10.110;
RA Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.;
RT "PREL1 provides a link from Ras signalling to the actin cytoskeleton via
RT Ena/VASP proteins.";
RL FEBS Lett. 579:455-463(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-383, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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 [16] {ECO:0007744|PDB:1EVH}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-112 IN COMPLEX WITH PRO-RICH
RP PEPTIDE OF L.MONOCYTOGENES ACTA.
RX PubMed=10338211; DOI=10.1016/s0092-8674(00)80757-6;
RA Prehoda K.E., Lee D.J., Lim W.A.;
RT "Structure of the enabled/VASP homology 1 domain-peptide complex: a key
RT component in the spatial control of actin assembly.";
RL Cell 97:471-480(1999).
RN [17] {ECO:0007744|PDB:4CC3}
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 547-558 IN COMPLEX WITH HUMAN
RP DNMBP.
RX PubMed=24332715; DOI=10.1016/j.str.2013.10.017;
RA Polle L., Rigano L.A., Julian R., Ireton K., Schubert W.D.;
RT "Structural details of human tuba recruitment by InlC of Listeria
RT monocytogenes elucidate bacterial cell-cell spreading.";
RL Structure 22:304-314(2014).
CC -!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a
CC range of processes dependent on cytoskeleton remodeling and cell
CC polarity such as axon guidance and lamellipodial and filopodial
CC dynamics in migrating cells. ENAH induces the formation of F-actin rich
CC outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and
CC downstream of NTN1 to promote filipodia formation.
CC {ECO:0000269|PubMed:10069337, ECO:0000269|PubMed:12134088,
CC ECO:0000269|PubMed:15066263, ECO:0000269|PubMed:8861907}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with APBB1IP, APBB1,
CC PFN1 and ROBO4. Isoforms, containing the polyproline-rich regions with
CC PPLP motifs, bind the WW domain of APBB1IP. Isoforms, containing the
CC PPSY motif, bind, in vitro, to the WW2 and WW3 domains of NEDD4 and to
CC the WW1 domain of YAP1. Binds the SH3 domain of BAIAP2-alpha but only
CC after the autoinhibitory region of BAIAP2-alpha has been blocked by
CC interaction with CDC42. Interacts, via the EVH1/WH1 domain, with the
CC Pro-rich domains from VCL, ZYX and Listeria monocytogenes actA and with
CC TES (via LIM domain). The TES LIM domain and the Pro-rich domains from
CC VCL or ZYX compete for the same binding site. Interaction with ZYX is
CC important for targeting ENAH to focal adhesions and enhances production
CC of actin-rich structures at the apical surface of cells. Binds GPHN.
CC Heterotrimer with TES and ACTL7A (By similarity). Interacts with FAT1
CC (via EVH1 domains) (PubMed:15148305). Interacts, through the Pro-rich
CC region, with the C-terminal SH3 domain of DNMPB (PubMed:14506234)
CC (Probable). Interacts with PRPF40A (PubMed:9171351). {ECO:0000250,
CC ECO:0000269|PubMed:10338211, ECO:0000269|PubMed:12672821,
CC ECO:0000269|PubMed:12941633, ECO:0000269|PubMed:14506234,
CC ECO:0000269|PubMed:15148305, ECO:0000269|PubMed:15642358,
CC ECO:0000269|PubMed:8861907, ECO:0000269|PubMed:9171351,
CC ECO:0000269|PubMed:9407065, ECO:0000305|PubMed:24332715}.
CC -!- INTERACTION:
CC Q03173; Q9UQB8: BAIAP2; Xeno; NbExp=3; IntAct=EBI-6083294, EBI-525456;
CC Q03173-1; Q6XZF7-1: DNMBP; Xeno; NbExp=2; IntAct=EBI-16085647, EBI-16085546;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10069337,
CC ECO:0000269|PubMed:12134088, ECO:0000269|PubMed:8861907}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Cell projection, lamellipodium
CC {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Synapse
CC {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}.
CC Note=Targeted to the leading edge of lamellipodia and filopodia by MRL
CC family members. Colocalizes at filopodial tips with a number of other
CC proteins including vinculin and zyxlin. Colocalizes with N-WASP at the
CC leading edge. Colocalizes with GPHN and PFN at synapses (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=5; Synonyms=Neural variant Mena+++, 140 kDa isoform;
CC IsoId=Q03173-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q03173-2; Sequence=VSP_007255;
CC Name=2; Synonyms=Mena, 80 kDa isoform;
CC IsoId=Q03173-3; Sequence=VSP_007259, VSP_007260;
CC Name=3; Synonyms=Neural variant Mena+;
CC IsoId=Q03173-4; Sequence=VSP_007259;
CC Name=4; Synonyms=Neural variant Mena++;
CC IsoId=Q03173-5; Sequence=VSP_007257, VSP_007258;
CC Name=6; Synonyms=Mena(S);
CC IsoId=Q03173-6; Sequence=VSP_007259, VSP_007260, VSP_010565;
CC -!- TISSUE SPECIFICITY: Expressed in heart and testis, lower levels in
CC lung, skeletal muscle, kidney, pancreas and brain. Isoform 5 is
CC expressed exclusively in the brain. Isoform 2 is expressed
CC predominantly in brain, testis, ovary and fat. In the brain, isoforms 2
CC and 5 are expressed at highest levels in the hippocampus, cortex and
CC midbrain, and at lowest levels in the striatum and cerebellum. Isoform
CC 6 is expressed in brain and spleen. {ECO:0000269|PubMed:10069337,
CC ECO:0000269|PubMed:1420303, ECO:0000269|PubMed:8861907}.
CC -!- DEVELOPMENTAL STAGE: At 8.5 dpc, particularly enriched in the
CC neuroepithelium, the forebrain and the somites. Highly expressed in the
CC edges of the neural folds. By 10.5 dpc, detected in the brain, dorsal
CC root ganglia (DRG), somites and limb buds. Highly expressed in the
CC branchial and pharyngeal arches, neural crest-derived structures that
CC give rise to portions of the face and neck. At 11 dpc, isoform 2,
CC isoform 3 and isoform 5 are expressed in embryonic brain (at protein
CC level). Expression of isoform 3 decreases steadily and becomes almost
CC undetectable by 16 dpc, while expression of isoform 5 begins to
CC increase from 13 dpc and peaks between 16 and 18 dpc (at protein
CC level). {ECO:0000269|PubMed:10069337}.
CC -!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a
CC thymosin-like domain required for G-actin binding. The KLKR motif
CC within this block is essential for the G-actin binding and for actin
CC polymerization. Block B is required for F-actin binding and subcellular
CC location, and Block C for tetramerization.
CC -!- PTM: NTN1-induced PKA phosphorylation on Ser-255 directly parallels the
CC formation of filopodial protrusions. {ECO:0000269|PubMed:12672821,
CC ECO:0000269|PubMed:15066263}.
CC -!- DISRUPTION PHENOTYPE: Mutant animals are viable and recovered in the
CC appropriate Mendelian ratios. they are smaller than their littermates
CC until adulthood and exhibit abnormal cage behavior, including reduced
CC activity. {ECO:0000269|PubMed:10069337}.
CC -!- MISCELLANEOUS: Required to transform actin polymerization into active
CC movement for the propulsive force of Listeria monocytogenes.
CC -!- MISCELLANEOUS: [Isoform 3]: Phosphorylated during neural development.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01570.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 1]:
CC Sequence=BAA01570.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D10727; BAA01570.1; ALT_FRAME; mRNA.
DR EMBL; U72520; AAC52863.1; -; mRNA.
DR EMBL; U72521; AAC52864.1; -; mRNA.
DR EMBL; U72522; AAC52865.1; -; mRNA.
DR EMBL; U72523; AAC52866.1; -; mRNA.
DR EMBL; BC062927; AAH62927.1; -; mRNA.
DR CCDS; CCDS78764.1; -. [Q03173-3]
DR PIR; S27200; S27200.
DR RefSeq; NP_001076590.1; NM_001083121.2. [Q03173-3]
DR PDB; 1EVH; X-ray; 1.80 A; A=1-112.
DR PDB; 4CC3; X-ray; 1.97 A; B/D/F/H=547-558.
DR PDBsum; 1EVH; -.
DR PDBsum; 4CC3; -.
DR AlphaFoldDB; Q03173; -.
DR SMR; Q03173; -.
DR BioGRID; 199446; 18.
DR DIP; DIP-29359N; -.
DR ELM; Q03173; -.
DR IntAct; Q03173; 10.
DR MINT; Q03173; -.
DR STRING; 10090.ENSMUSP00000077781; -.
DR GlyConnect; 2625; 1 N-Linked glycan (1 site).
DR GlyGen; Q03173; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q03173; -.
DR PhosphoSitePlus; Q03173; -.
DR EPD; Q03173; -.
DR jPOST; Q03173; -.
DR MaxQB; Q03173; -.
DR PaxDb; Q03173; -.
DR PeptideAtlas; Q03173; -.
DR PRIDE; Q03173; -.
DR ProteomicsDB; 277866; -. [Q03173-1]
DR ProteomicsDB; 277867; -. [Q03173-2]
DR ProteomicsDB; 277868; -. [Q03173-3]
DR ProteomicsDB; 277869; -. [Q03173-4]
DR ProteomicsDB; 277870; -. [Q03173-5]
DR ProteomicsDB; 277871; -. [Q03173-6]
DR Antibodypedia; 34644; 215 antibodies from 33 providers.
DR DNASU; 13800; -.
DR Ensembl; ENSMUST00000111025; ENSMUSP00000106654; ENSMUSG00000022995. [Q03173-6]
DR Ensembl; ENSMUST00000193703; ENSMUSP00000141462; ENSMUSG00000022995. [Q03173-3]
DR GeneID; 13800; -.
DR KEGG; mmu:13800; -.
DR UCSC; uc007dxs.2; mouse. [Q03173-3]
DR CTD; 55740; -.
DR MGI; MGI:108360; Enah.
DR VEuPathDB; HostDB:ENSMUSG00000022995; -.
DR eggNOG; KOG4590; Eukaryota.
DR GeneTree; ENSGT00940000157376; -.
DR InParanoid; Q03173; -.
DR OrthoDB; 972128at2759; -.
DR PhylomeDB; Q03173; -.
DR Reactome; R-MMU-376176; Signaling by ROBO receptors.
DR BioGRID-ORCS; 13800; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Enah; mouse.
DR EvolutionaryTrace; Q03173; -.
DR PRO; PR:Q03173; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q03173; protein.
DR Bgee; ENSMUSG00000022995; Expressed in vestibular membrane of cochlear duct and 256 other tissues.
DR ExpressionAtlas; Q03173; baseline and differential.
DR Genevisible; Q03173; MM.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005522; F:profilin binding; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
DR GO; GO:0050699; F:WW domain binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IDA:MGI.
DR GO; GO:0070358; P:actin polymerization-dependent cell motility; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR038023; VASP_sf.
DR InterPro; IPR014885; VASP_tetra.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR Pfam; PF08776; VASP_tetra; 1.
DR Pfam; PF00568; WH1; 1.
DR SMART; SM00461; WH1; 1.
DR SUPFAM; SSF118370; SSF118370; 1.
DR PROSITE; PS50229; WH1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell junction;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Neurogenesis; Phosphoprotein;
KW Reference proteome; Repeat; SH3-binding; Synapse.
FT CHAIN 1..802
FT /note="Protein enabled homolog"
FT /id="PRO_0000086972"
FT DOMAIN 1..111
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REPEAT 175..179
FT /note="1"
FT REPEAT 180..184
FT /note="2"
FT REPEAT 185..189
FT /note="3"
FT REPEAT 190..194
FT /note="4"
FT REPEAT 195..199
FT /note="5"
FT REPEAT 200..204
FT /note="6"
FT REPEAT 205..209
FT /note="7"
FT REGION 143..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..209
FT /note="7 X 5 AA tandem repeats of [LM]-E-[QR]-[EQ]-[QR]"
FT REGION 245..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..799
FT /note="EVH2"
FT REGION 623..643
FT /note="EVH2 block A"
FT REGION 639..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..691
FT /note="EVH2 block B"
FT REGION 691..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..799
FT /note="EVH2 block C"
FT COILED 154..258
FT /evidence="ECO:0000255"
FT COILED 767..797
FT /evidence="ECO:0000255"
FT MOTIF 632..635
FT /note="KLKR"
FT COMPBIAS 143..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..391
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 255
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:15066263,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 557
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:12672821"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N8S7"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N8S7"
FT VAR_SEQ 1..412
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:1420303"
FT /id="VSP_007255"
FT VAR_SEQ 117..135
FT /note="Missing (in isoform 2, isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8861907"
FT /id="VSP_007259"
FT VAR_SEQ 117..131
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8861907"
FT /id="VSP_007257"
FT VAR_SEQ 132..135
FT /note="CIFC -> VFYL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8861907"
FT /id="VSP_007258"
FT VAR_SEQ 259..500
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8861907"
FT /id="VSP_007260"
FT VAR_SEQ 561..594
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_010565"
FT MUTAGEN 255
FT /note="S->A: No change in subcellular location nor
FT colocalization with vinculin at focal adhesions nor with N-
FT WASP at the leading edge. Loss of cell mobility function;
FT when associated with A-637."
FT /evidence="ECO:0000269|PubMed:12134088"
FT MUTAGEN 255
FT /note="S->D: No change in subcellular location nor
FT colocalization with vinculin at focal adhesions nor with N-
FT WASP at the leading edge. No loss of cell mobility
FT function; when associated with D-637."
FT /evidence="ECO:0000269|PubMed:12134088"
FT MUTAGEN 637
FT /note="S->A: No change in subcellular location nor
FT colocalization with vinculin at focal adhesions nor with N-
FT WASP at the leading edge. No loss of cell mobility
FT function. when associated with A-255."
FT /evidence="ECO:0000269|PubMed:12134088"
FT MUTAGEN 637
FT /note="S->D: No change in subcellular location nor
FT colocalization with vinculin at focal adhesions nor with N-
FT WASP at the leading edge. No loss of cell mobility
FT function. when associated with D-255."
FT /evidence="ECO:0000269|PubMed:12134088"
FT CONFLICT 500
FT /note="G -> A (in Ref. 1; BAA01570)"
FT /evidence="ECO:0000305"
FT STRAND 3..17
FT /evidence="ECO:0007829|PDB:1EVH"
FT TURN 18..21
FT /evidence="ECO:0007829|PDB:1EVH"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1EVH"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1EVH"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1EVH"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:1EVH"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:1EVH"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1EVH"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1EVH"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1EVH"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1EVH"
FT HELIX 94..111
FT /evidence="ECO:0007829|PDB:1EVH"
SQ SEQUENCE 802 AA; 85844 MW; 592BB975EE20F77F CRC64;
MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI
NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQEAAQSK
VTATQDSTNL RCIFCGPTLP RQNSQLPAQV QNGPSQEELE IQRRQLQEQQ RQKELERERM
ERERLERERL ERERLERERL EQEQLERQRQ EREHVERLER ERLERLERER QERERERLEQ
LEREQVEWER ERRMSNAAPS SDSSLSSAPL PEYSSCQPPS APPPSYAKVI SAPVSDATPD
YAVVTALPPT STPPTPPLRH AATRFATSLG SAFHPVLPHY ATVPRPLNKN SRPSSPVNTP
SSQPPAAKSC AWPTSNFSPL PPSPPIMISS PPGKATGPRP VLPVCVSSPV PQMPPSPTAP
NGSLDSVTYP VSPPPTSGPA APPPPPPPPP PPPPPPLPPP PLPPLASLSH CGSQASPPPG
TPLASTPSSK PSVLPSPSAG APASAETPLN PELGDSSASE PGLQAASQPA ESPTPQGLVL
GPPAPPPPPP LPSGPAYASA LPPPPGPPPP PPLPSTGPPP PPPPPPPLPN QAPPPPPPPP
APPLPASGIF SGSTSEDNRP LTGLAAAIAG AKLRKVSRVE DGSFPGGGNT GSVSLASSKA
DAGRGNGPLP LGGSGLMEEM SALLARRRRI AEKGSTIETE QKEDRNEDAE PITAKAPSTS
TPEPTRKPWE RTNTMNGSKS PVISRPKSTP SSQPSANGVQ TEGLDYDRLK QDILDEMRKE
LAKLKEELID AIRQELSKSN TA
