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 24-JAN-2024, entry version 197. 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=BAA01570.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 21. 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 GlyCosmos; Q03173; 1 site, 1 glycan. DR GlyGen; Q03173; 8 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (7 sites). DR iPTMnet; Q03173; -. DR PhosphoSitePlus; Q03173; -. DR SwissPalm; Q03173; -. DR EPD; Q03173; -. DR jPOST; Q03173; -. DR MaxQB; Q03173; -. DR PaxDb; 10090-ENSMUSP00000077781; -. DR PeptideAtlas; 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 Pumba; Q03173; -. DR Antibodypedia; 34644; 252 antibodies from 33 providers. DR DNASU; 13800; -. DR Ensembl; ENSMUST00000193703.6; ENSMUSP00000141462.2; ENSMUSG00000022995.18. [Q03173-3] DR GeneID; 13800; -. DR KEGG; mmu:13800; -. DR UCSC; uc007dxs.2; mouse. [Q03173-3] DR AGR; MGI:108360; -. DR CTD; 55740; -. DR MGI; MGI:108360; Enah. DR VEuPathDB; HostDB:ENSMUSG00000022995; -. DR eggNOG; KOG4590; Eukaryota. DR GeneTree; ENSGT00940000157376; -. DR InParanoid; Q03173; -. DR OrthoDB; 2884005at2759; -. DR PhylomeDB; Q03173; -. DR Reactome; R-MMU-376176; Signaling by ROBO receptors. DR BioGRID-ORCS; 13800; 5 hits in 78 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 258 other cell types or tissues. DR ExpressionAtlas; Q03173; baseline and differential. 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 CDD; cd01207; EVH1_Ena_VASP-like; 1. DR CDD; cd22185; WH2_hVASP-like; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 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 PANTHER; PTHR11202:SF1; PROTEIN ENABLED HOMOLOG; 1. DR PANTHER; PTHR11202; SPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1. DR Pfam; PF08776; VASP_tetra; 1. DR Pfam; PF00568; WH1; 1. DR PRINTS; PR01217; PRICHEXTENSN. DR SMART; SM00461; WH1; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF118370; Vasodilator-stimulated phosphoprotein, VASP, tetramerisation domain; 1. DR PROSITE; PS50229; WH1; 1. DR Genevisible; Q03173; MM. 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 FT N-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 FT N-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 FT N-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 FT N-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 //