##gff-version 3 Q03173 UniProtKB Chain 1 802 . . . ID=PRO_0000086972;Note=Protein enabled homolog Q03173 UniProtKB Domain 1 111 . . . Note=WH1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00410 Q03173 UniProtKB Repeat 175 179 . . . Note=1 Q03173 UniProtKB Repeat 180 184 . . . Note=2 Q03173 UniProtKB Repeat 185 189 . . . Note=3 Q03173 UniProtKB Repeat 190 194 . . . Note=4 Q03173 UniProtKB Repeat 195 199 . . . Note=5 Q03173 UniProtKB Repeat 200 204 . . . Note=6 Q03173 UniProtKB Repeat 205 209 . . . Note=7 Q03173 UniProtKB Region 143 166 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Region 175 209 . . . Note=7 X 5 AA tandem repeats of [LM]-E-[QR]-[EQ]-[QR] Q03173 UniProtKB Region 245 287 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Region 341 622 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Region 623 799 . . . Note=EVH2 Q03173 UniProtKB Region 623 643 . . . Note=EVH2 block A Q03173 UniProtKB Region 639 675 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Region 674 691 . . . Note=EVH2 block B Q03173 UniProtKB Region 691 764 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Region 765 799 . . . Note=EVH2 block C Q03173 UniProtKB Coiled coil 154 258 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q03173 UniProtKB Coiled coil 767 797 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q03173 UniProtKB Motif 632 635 . . . Note=KLKR Q03173 UniProtKB Compositional bias 143 160 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Compositional bias 257 274 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Compositional bias 347 376 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Compositional bias 377 391 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Compositional bias 404 418 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Compositional bias 432 466 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Compositional bias 520 534 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Compositional bias 536 606 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Compositional bias 691 711 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Compositional bias 713 760 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03173 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:15345747;Dbxref=PMID:15345747 Q03173 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15066263,ECO:0007744|PubMed:21183079;Dbxref=PMID:15066263,PMID:21183079 Q03173 UniProtKB Modified residue 383 383 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q03173 UniProtKB Modified residue 557 557 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12672821;Dbxref=PMID:12672821 Q03173 UniProtKB Modified residue 738 738 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N8S7 Q03173 UniProtKB Modified residue 740 740 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N8S7 Q03173 UniProtKB Alternative sequence 1 412 . . . ID=VSP_007255;Note=In isoform 1. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1420303;Dbxref=PMID:1420303 Q03173 UniProtKB Alternative sequence 117 135 . . . ID=VSP_007259;Note=In isoform 2%2C isoform 3 and isoform 6. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:8861907;Dbxref=PMID:15489334,PMID:8861907 Q03173 UniProtKB Alternative sequence 117 131 . . . ID=VSP_007257;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8861907;Dbxref=PMID:8861907 Q03173 UniProtKB Alternative sequence 132 135 . . . ID=VSP_007258;Note=In isoform 4. CIFC->VFYL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8861907;Dbxref=PMID:8861907 Q03173 UniProtKB Alternative sequence 259 500 . . . ID=VSP_007260;Note=In isoform 2 and isoform 6. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:8861907;Dbxref=PMID:15489334,PMID:8861907 Q03173 UniProtKB Alternative sequence 561 594 . . . ID=VSP_010565;Note=In isoform 6. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03173 UniProtKB Mutagenesis 255 255 . . . Note=No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. Loss of cell mobility function%3B when associated with A-637. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134088;Dbxref=PMID:12134088 Q03173 UniProtKB Mutagenesis 255 255 . . . Note=No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. No loss of cell mobility function%3B when associated with D-637. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134088;Dbxref=PMID:12134088 Q03173 UniProtKB Mutagenesis 637 637 . . . Note=No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. No loss of cell mobility function. when associated with A-255. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134088;Dbxref=PMID:12134088 Q03173 UniProtKB Mutagenesis 637 637 . . . Note=No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. No loss of cell mobility function. when associated with D-255. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134088;Dbxref=PMID:12134088 Q03173 UniProtKB Sequence conflict 500 500 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03173 UniProtKB Beta strand 3 17 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH Q03173 UniProtKB Turn 18 21 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH Q03173 UniProtKB Beta strand 22 25 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH Q03173 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH Q03173 UniProtKB Beta strand 33 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH Q03173 UniProtKB Turn 41 44 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH Q03173 UniProtKB Beta strand 45 52 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH Q03173 UniProtKB Turn 53 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH Q03173 UniProtKB Beta strand 58 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH Q03173 UniProtKB Beta strand 74 81 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH Q03173 UniProtKB Beta strand 86 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH Q03173 UniProtKB Helix 94 111 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVH