##gff-version 3 P03950 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2866794;Dbxref=PMID:2866794 P03950 UniProtKB Chain 25 147 . . . ID=PRO_0000030843;Note=Angiogenin;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2866794,ECO:0000269|PubMed:2866795;Dbxref=PMID:2866794,PMID:2866795 P03950 UniProtKB Motif 55 59 . . . Note=Nucleolar localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7945327;Dbxref=PMID:7945327 P03950 UniProtKB Active site 37 37 . . . Note=Proton acceptor;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11468363,ECO:0000269|PubMed:9918722;Dbxref=PMID:11468363,PMID:9918722 P03950 UniProtKB Active site 138 138 . . . Note=Proton donor;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11468363,ECO:0000269|PubMed:9918722;Dbxref=PMID:11468363,PMID:9918722 P03950 UniProtKB Binding site 64 68 . . . . P03950 UniProtKB Modified residue 25 25 . . . Note=Pyrrolidone carboxylic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2866794;Dbxref=PMID:2866794 P03950 UniProtKB Disulfide bond 50 105 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2866794;Dbxref=PMID:2866794 P03950 UniProtKB Disulfide bond 63 116 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2866794;Dbxref=PMID:2866794 P03950 UniProtKB Disulfide bond 81 131 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2866794;Dbxref=PMID:2866794 P03950 UniProtKB Natural variant 12 12 . . . ID=VAR_044145;Note=In ALS9. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18087731;Dbxref=PMID:18087731 P03950 UniProtKB Natural variant 20 20 . . . ID=VAR_044146;Note=In ALS9. P->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17886298,ECO:0000269|PubMed:18087731;Dbxref=PMID:17886298,PMID:18087731 P03950 UniProtKB Natural variant 36 36 . . . ID=VAR_044147;Note=In ALS9%3B reduced ribonucleolytic activity%3B low angiogenic activity%3B reduced mitogenic activity%3B wild type far-UVCD spectra. Q->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16501576,ECO:0000269|PubMed:17900154;Dbxref=dbSNP:rs121909535,PMID:16501576,PMID:17900154 P03950 UniProtKB Natural variant 38 38 . . . ID=VAR_073021;Note=In ALS9. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22292843;Dbxref=dbSNP:rs1032422334,PMID:22292843 P03950 UniProtKB Natural variant 41 41 . . . ID=VAR_044148;Note=In ALS9%3B reduced ribonucleolytic activity. K->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16501576,ECO:0000269|PubMed:17900154;Dbxref=dbSNP:rs121909537,PMID:16501576,PMID:17900154 P03950 UniProtKB Natural variant 41 41 . . . ID=VAR_044149;Note=In ALS9%3B loss of angiogenic activity%3B reduced ribonucleolytic activity%3B retains nuclear translocation. K->I;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16501576,ECO:0000269|PubMed:17886298,ECO:0000269|PubMed:17900154,ECO:0000269|PubMed:22292843;Dbxref=dbSNP:rs121909536,PMID:16501576,PMID:17886298,PMID:17900154,PMID:22292843 P03950 UniProtKB Natural variant 46 46 . . . ID=VAR_073022;Note=In ALS9%3B homodimerization is similar to wild-type%3B localization in the nucleus is similar to the wild-type%3B strongly reduces ribonucleolytic activity. D->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22292843,ECO:0000269|PubMed:25372031;Dbxref=dbSNP:rs1440927797,PMID:22292843,PMID:25372031 P03950 UniProtKB Natural variant 52 52 . . . ID=VAR_044150;Note=In ALS9%3B loss of angiogenic activity%3B reduced ribonucleolytic activity%3B unable to translocate to the nucleus. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17886298;Dbxref=dbSNP:rs121909542,PMID:17886298 P03950 UniProtKB Natural variant 55 55 . . . ID=VAR_044151;Note=In ALS9%3B marginally reduced ribonucleolytic activity%3B wild type far-UVCD spectra. R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16501576,ECO:0000269|PubMed:17900154;Dbxref=dbSNP:rs121909538,PMID:16501576,PMID:17900154 P03950 UniProtKB Natural variant 63 63 . . . ID=VAR_044152;Note=In ALS9%3B reduced ribonucleolytic activity%3B low angiogenic activity%3B reduced mitogenic activity%3B reduced thermal stability. C->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16501576,ECO:0000269|PubMed:17900154;Dbxref=dbSNP:rs121909539,PMID:16501576,PMID:17900154 P03950 UniProtKB Natural variant 64 64 . . . ID=VAR_044153;Note=In ALS9%3B reduced ribonucleolytic activity%3B low angiogenic activity%3B reduced mitogenic activity%3B moderate reduction of thermal stability. K->I;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15557516,ECO:0000269|PubMed:16501576,ECO:0000269|PubMed:17900154;Dbxref=dbSNP:rs121909540,PMID:15557516,PMID:16501576,PMID:17900154 P03950 UniProtKB Natural variant 70 70 . . . ID=VAR_044154;Note=In some ALS9 patients%3B uncertain significance%3B reduced ribonucleolytic activity%3B moderate reduction of thermal stability. I->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16501576,ECO:0000269|PubMed:17900154,ECO:0000269|PubMed:18087731;Dbxref=dbSNP:rs121909541,PMID:16501576,PMID:17900154,PMID:18087731 P03950 UniProtKB Natural variant 84 84 . . . ID=VAR_013148;Note=K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11919285;Dbxref=dbSNP:rs17560,PMID:11919285 P03950 UniProtKB Natural variant 136 136 . . . ID=VAR_044155;Note=In ALS9%3B loss of angiogenic activity%3B reduced ribonucleolytic activity%3B unable to translocate to the nucleus. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17886298;Dbxref=dbSNP:rs121909543,PMID:17886298 P03950 UniProtKB Natural variant 137 137 . . . ID=VAR_044156;Note=In ALS9. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18087731;Dbxref=dbSNP:rs121909544,PMID:18087731 P03950 UniProtKB Natural variant 138 138 . . . ID=VAR_044157;Note=In ALS9. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18087731;Dbxref=PMID:18087731 P03950 UniProtKB Mutagenesis 29 29 . . . Note=Significantly decreases binding affinity for RNH1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10413501;Dbxref=PMID:10413501 P03950 UniProtKB Mutagenesis 32 32 . . . Note=Significantly decreases binding affinity for RNH1. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9050852;Dbxref=PMID:9050852 P03950 UniProtKB Mutagenesis 36 36 . . . Note=Slightly decreases binding affinity for RNH1. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9050852;Dbxref=PMID:9050852 P03950 UniProtKB Mutagenesis 59 59 . . . Note=Homodimerization is similar to wild-type%3B causes mislocalization in the cytoplasm%3B strongly reduces ribonucleolytic activity. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25372031;Dbxref=PMID:25372031 P03950 UniProtKB Mutagenesis 64 64 . . . Note=Significantly decreases binding affinity for RNH1. K->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10413501,ECO:0000269|PubMed:9050852;Dbxref=PMID:10413501,PMID:9050852 P03950 UniProtKB Mutagenesis 92 92 . . . Note=Slightly decreases binding affinity for RNH1. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9050852;Dbxref=PMID:9050852 P03950 UniProtKB Mutagenesis 109 110 . . . Note=Significantly decreases binding affinity for RNH1. GG->RR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19354288;Dbxref=PMID:19354288 P03950 UniProtKB Mutagenesis 132 132 . . . Note=Slightly decreases binding affinity for RNH1. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9050852;Dbxref=PMID:9050852 P03950 UniProtKB Mutagenesis 140 140 . . . Note=15- to 18-fold increase in RNase activity. D->H%2CS%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11851402;Dbxref=PMID:11851402 P03950 UniProtKB Mutagenesis 141 141 . . . Note=Over 18-fold increase in RNase activity. Q->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11851402;Dbxref=PMID:11851402 P03950 UniProtKB Mutagenesis 143 144 . . . Note=3- to 5-fold increase in RNase activity. IF->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11851402;Dbxref=PMID:11851402 P03950 UniProtKB Sequence conflict 59 59 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 P03950 UniProtKB Helix 28 37 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Helix 47 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Turn 60 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Beta strand 65 70 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Helix 74 78 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Helix 79 81 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Turn 83 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Beta strand 86 89 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Turn 90 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Beta strand 93 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Beta strand 100 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Beta strand 112 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Beta strand 117 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Beta strand 128 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Beta strand 135 139 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH P03950 UniProtKB Helix 141 144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOH