##gff-version 3 O75044 UniProtKB Chain 1 1071 . . . ID=PRO_0000056767;Note=SLIT-ROBO Rho GTPase-activating protein 2 O75044 UniProtKB Domain 22 325 . . . Note=F-BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01077 O75044 UniProtKB Domain 489 679 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 O75044 UniProtKB Domain 728 787 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 O75044 UniProtKB Region 181 211 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75044 UniProtKB Region 698 726 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75044 UniProtKB Region 837 936 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75044 UniProtKB Region 983 1012 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75044 UniProtKB Region 1029 1071 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75044 UniProtKB Coiled coil 362 401 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 O75044 UniProtKB Coiled coil 940 967 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 O75044 UniProtKB Compositional bias 181 204 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75044 UniProtKB Compositional bias 850 884 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75044 UniProtKB Compositional bias 896 931 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75044 UniProtKB Compositional bias 1045 1071 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75044 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D4A208 O75044 UniProtKB Modified residue 427 427 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D4A208 O75044 UniProtKB Modified residue 500 500 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Z67 O75044 UniProtKB Modified residue 691 691 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D4A208 O75044 UniProtKB Modified residue 695 695 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Z67 O75044 UniProtKB Modified residue 724 724 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 O75044 UniProtKB Modified residue 795 795 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O75044 UniProtKB Modified residue 916 916 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O75044 UniProtKB Modified residue 927 927 . . . Note=Symmetric dimethylarginine%3B by PRMT5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810653;Dbxref=PMID:20810653 O75044 UniProtKB Modified residue 930 930 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 O75044 UniProtKB Modified residue 990 990 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Z67 O75044 UniProtKB Modified residue 994 994 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O75044 UniProtKB Modified residue 1013 1013 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O75044 UniProtKB Modified residue 1027 1027 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O75044 UniProtKB Natural variant 874 874 . . . ID=VAR_055834;Note=R->G;Dbxref=dbSNP:rs17018890 O75044 UniProtKB Mutagenesis 54 55 . . . Note=In F-BARx-R5E mutant%3B abolished binding to membranes%3B when associated with 234--E--E-238. RK->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28333212;Dbxref=PMID:28333212 O75044 UniProtKB Mutagenesis 108 108 . . . Note=Does not affect protein stability. R->K%2CL%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28333212;Dbxref=PMID:28333212 O75044 UniProtKB Mutagenesis 108 108 . . . Note=Decreased protein stability. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28333212;Dbxref=PMID:28333212 O75044 UniProtKB Mutagenesis 234 238 . . . Note=In F-BARx-R5E mutant%3B abolished binding to membranes%3B when associated with 54-E-E-55. KRQAK->EEQAE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28333212;Dbxref=PMID:28333212 O75044 UniProtKB Mutagenesis 527 527 . . . Note=Abolished RAC1 GTPase activity%3B when associated with A-566. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27373832;Dbxref=PMID:27373832 O75044 UniProtKB Mutagenesis 566 566 . . . Note=Abolished RAC1 GTPase activity%3B when associated with L-527. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27373832;Dbxref=PMID:27373832 O75044 UniProtKB Mutagenesis 765 765 . . . Note=Abolished interaction with ROBO1. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26365803;Dbxref=PMID:26365803 O75044 UniProtKB Mutagenesis 781 781 . . . Note=Abolished interaction with ROBO1. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26365803;Dbxref=PMID:26365803 O75044 UniProtKB Mutagenesis 807 807 . . . Note=Increased interaction with ROBO1. P->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26365803;Dbxref=PMID:26365803 O75044 UniProtKB Mutagenesis 927 927 . . . Note=Loss of the ability to stimulate cell migration%2C to localize at the plasma membrane protrusions and to dimerize. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810653;Dbxref=PMID:20810653 O75044 UniProtKB Sequence conflict 709 709 . . . Note=S->P O75044 UniProtKB Helix 10 76 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Helix 94 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Helix 124 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Helix 188 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Helix 223 269 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Helix 271 278 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Turn 279 281 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Helix 284 318 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Helix 322 332 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Helix 334 337 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Beta strand 348 350 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6J O75044 UniProtKB Helix 362 402 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Helix 410 413 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Helix 436 478 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I6R O75044 UniProtKB Beta strand 731 737 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RUG O75044 UniProtKB Beta strand 742 746 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DL8 O75044 UniProtKB Beta strand 754 762 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RUG O75044 UniProtKB Beta strand 765 770 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RUG O75044 UniProtKB Beta strand 773 778 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RUG O75044 UniProtKB Helix 779 781 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RUG O75044 UniProtKB Beta strand 782 784 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RUG O75044 UniProtKB Helix 791 795 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RUG O75044 UniProtKB Helix 800 804 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RUG