##gff-version 3 P51149 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25944712;Dbxref=PMID:25944712 P51149 UniProtKB Chain 2 207 . . . ID=PRO_0000121121;Note=Ras-related protein Rab-7a P51149 UniProtKB Motif 37 45 . . . Note=Effector region;Ontology_term=ECO:0000250;evidence=ECO:0000250 P51149 UniProtKB Binding site 15 22 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15933719,ECO:0000269|PubMed:20028791;Dbxref=PMID:15933719,PMID:20028791 P51149 UniProtKB Binding site 34 40 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15933719,ECO:0000269|PubMed:20028791;Dbxref=PMID:15933719,PMID:20028791 P51149 UniProtKB Binding site 63 67 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15933719,ECO:0000269|PubMed:20028791;Dbxref=PMID:15933719,PMID:20028791 P51149 UniProtKB Binding site 125 128 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15933719,ECO:0000269|PubMed:20028791;Dbxref=PMID:15933719,PMID:20028791 P51149 UniProtKB Binding site 156 157 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15933719,ECO:0000269|PubMed:20028791;Dbxref=PMID:15933719,PMID:20028791 P51149 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25944712;Dbxref=PMID:25944712 P51149 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:20068231,PMID:23186163 P51149 UniProtKB Modified residue 207 207 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 P51149 UniProtKB Lipidation 205 205 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 P51149 UniProtKB Lipidation 207 207 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 P51149 UniProtKB Cross-link 191 191 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36476874;Dbxref=PMID:36476874 P51149 UniProtKB Cross-link 194 194 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36476874;Dbxref=PMID:36476874 P51149 UniProtKB Natural variant 32 32 . . . ID=VAR_037886;Note=K->E;Dbxref=dbSNP:rs11549759 P51149 UniProtKB Natural variant 129 129 . . . ID=VAR_018722;Note=In CMT2B%3B increases GTP hydrolysis%3B decreases affinity for GTP and GDP%3B does not affect interaction with NTRK1%3B results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling%3B increases interaction with PRPH. L->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12545426,ECO:0000269|PubMed:20028791,ECO:0000269|PubMed:21151572,ECO:0000269|PubMed:23179371;Dbxref=dbSNP:rs121909078,PMID:12545426,PMID:20028791,PMID:21151572,PMID:23179371 P51149 UniProtKB Natural variant 157 157 . . . ID=VAR_037887;Note=In CMT2B%3B does not affect interaction with NTRK1%3B results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling%3B increases interaction with PRPH. K->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17060578,ECO:0000269|PubMed:21151572,ECO:0000269|PubMed:23179371;Dbxref=dbSNP:rs121909081,PMID:17060578,PMID:21151572,PMID:23179371 P51149 UniProtKB Natural variant 161 161 . . . ID=VAR_037888;Note=In CMT2B%3B does not affect interaction with NTRK1%3B results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling%3B increases interaction with PRPH. N->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15455439,ECO:0000269|PubMed:21151572,ECO:0000269|PubMed:23179371;Dbxref=dbSNP:rs121909080,PMID:15455439,PMID:21151572,PMID:23179371 P51149 UniProtKB Natural variant 162 162 . . . ID=VAR_018723;Note=In CMT2B%3B increases GTP hydrolysis%3B decreases affinity for GTP and GDP%3B does not affect interaction with NTRK1%3B results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling%3B increases interaction with PRPH. V->M;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12545426,ECO:0000269|PubMed:20028791,ECO:0000269|PubMed:21151572,ECO:0000269|PubMed:23179371;Dbxref=dbSNP:rs121909079,PMID:12545426,PMID:20028791,PMID:21151572,PMID:23179371 P51149 UniProtKB Mutagenesis 8 8 . . . Note=Abolishes interaction with RILP and reduces its localization to late endosomal/lysosomal compartments. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933719;Dbxref=PMID:15933719 P51149 UniProtKB Mutagenesis 10 10 . . . Note=Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933719;Dbxref=PMID:15933719 P51149 UniProtKB Mutagenesis 22 22 . . . Note=Abolishes localization on late endosomes%2C lysosomes and phagosomes and reduces phagosomal fusions. Abolishes association of RILP with the phagosomes. No loss of interaction with CLN5. No loss of interaction with PRPH. Reduced interaction with VPS13A. Inhibits SARS-CoV-2 infection. T->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12944476,ECO:0000269|PubMed:22431521,ECO:0000269|PubMed:23179371,ECO:0000269|PubMed:30709847,ECO:0000269|PubMed:34159616;Dbxref=PMID:12944476,PMID:22431521,PMID:23179371,PMID:30709847,PMID:34159616 P51149 UniProtKB Mutagenesis 67 67 . . . Note=Does not abolish localization on late endosomes%2C lysosomes and phagosomes and does not reduce phagosomal fusions. No loss of interaction with CLN5 and VPS13A. Increases interaction with PRPH. Inhibits SARS-CoV-2 infection. Q->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12944476,ECO:0000269|PubMed:22431521,ECO:0000269|PubMed:23179371,ECO:0000269|PubMed:30709847,ECO:0000269|PubMed:34159616;Dbxref=PMID:12944476,PMID:22431521,PMID:23179371,PMID:30709847,PMID:34159616 P51149 UniProtKB Mutagenesis 180 180 . . . Note=Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933719;Dbxref=PMID:15933719 P51149 UniProtKB Mutagenesis 182 182 . . . Note=Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments%3B when associated with A-183. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933719;Dbxref=PMID:15933719 P51149 UniProtKB Mutagenesis 183 183 . . . Note=Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments%3B when associated with A-182. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933719;Dbxref=PMID:15933719 P51149 UniProtKB Sequence conflict 47 47 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51149 UniProtKB Sequence conflict 108 108 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51149 UniProtKB Sequence conflict 127 127 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51149 UniProtKB Sequence conflict 180 180 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51149 UniProtKB Beta strand 8 14 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Helix 21 30 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Beta strand 42 54 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Beta strand 56 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Helix 68 70 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Helix 76 78 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6IYB P51149 UniProtKB Beta strand 82 89 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Helix 93 97 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Helix 99 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Helix 115 117 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Beta strand 120 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Beta strand 129 131 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6IYB P51149 UniProtKB Helix 136 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Turn 156 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91 P51149 UniProtKB Helix 162 181 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1T91