##gff-version 3 P27695 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12524539,ECO:0000269|PubMed:1380454;Dbxref=PMID:12524539,PMID:1380454 P27695 UniProtKB Chain 2 318 . . . ID=PRO_0000200010;Note=DNA repair nuclease/redox regulator APEX1 P27695 UniProtKB Chain 32 318 . . . ID=PRO_0000402572;Note=DNA repair nuclease/redox regulator APEX1%2C mitochondrial;Ontology_term=ECO:0000250;evidence=ECO:0000250 P27695 UniProtKB Region 1 60 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P27695 UniProtKB Region 2 33 . . . Note=Necessary for interaction with YBX1%2C binding to RNA%2C NPM1-dependent association with rRNA%2C endoribonuclease activity on abasic RNA and localization in the nucleoli;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18809583;Dbxref=PMID:18809583 P27695 UniProtKB Region 23 33 . . . Note=Necessary for interaction with NPM1 and for efficient rRNA binding P27695 UniProtKB Region 289 318 . . . Note=Mitochondrial targeting sequence (MTS) P27695 UniProtKB Motif 8 13 . . . Note=Nuclear localization signal (NLS) P27695 UniProtKB Motif 64 80 . . . Note=Nuclear export signal (NES) P27695 UniProtKB Compositional bias 1 41 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P27695 UniProtKB Active site 171 171 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15380100;Dbxref=PMID:15380100 P27695 UniProtKB Active site 210 210 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:9351835,ECO:0007744|PDB:1BIX;Dbxref=PMID:9351835 P27695 UniProtKB Active site 309 309 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00764 P27695 UniProtKB Binding site 68 68 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00764 P27695 UniProtKB Binding site 96 96 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00764 P27695 UniProtKB Binding site 210 210 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00764 P27695 UniProtKB Binding site 212 212 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00764 P27695 UniProtKB Binding site 308 308 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00764 P27695 UniProtKB Binding site 309 309 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00764 P27695 UniProtKB Site 31 32 . . . Note=Cleavage%3B by granzyme A P27695 UniProtKB Site 212 212 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8932375;Dbxref=PMID:8932375 P27695 UniProtKB Site 283 283 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21762700,ECO:0000269|PubMed:9804799;Dbxref=PMID:21762700,PMID:9804799 P27695 UniProtKB Site 309 309 . . . Note=Interaction with DNA substrate P27695 UniProtKB Modified residue 6 6 . . . Note=N6-acetyllysine%3B by EP300;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14633989;Dbxref=PMID:14633989 P27695 UniProtKB Modified residue 7 7 . . . Note=N6-acetyllysine%3B by EP300;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14633989;Dbxref=PMID:14633989 P27695 UniProtKB Modified residue 27 27 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20699270;Dbxref=PMID:20699270 P27695 UniProtKB Modified residue 31 31 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20699270;Dbxref=PMID:20699270 P27695 UniProtKB Modified residue 32 32 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20699270;Dbxref=PMID:20699270 P27695 UniProtKB Modified residue 35 35 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20699270;Dbxref=PMID:20699270 P27695 UniProtKB Modified residue 54 54 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P27695 UniProtKB Modified residue 65 65 . . . Note=S-nitrosocysteine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17403694;Dbxref=PMID:17403694 P27695 UniProtKB Modified residue 93 93 . . . Note=S-nitrosocysteine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17403694;Dbxref=PMID:17403694 P27695 UniProtKB Modified residue 197 197 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P27695 UniProtKB Modified residue 233 233 . . . Note=Phosphothreonine%3B by CDK5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28352 P27695 UniProtKB Modified residue 310 310 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17403694;Dbxref=PMID:17403694 P27695 UniProtKB Disulfide bond 65 93 . . . Note=Alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305 P27695 UniProtKB Natural variant 51 51 . . . ID=VAR_013455;Note=Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.11;Dbxref=dbSNP:rs1048945 P27695 UniProtKB Natural variant 64 64 . . . ID=VAR_014823;Note=I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.11;Dbxref=dbSNP:rs2307486 P27695 UniProtKB Natural variant 148 148 . . . ID=VAR_019790;Note=D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|Ref.11;Dbxref=dbSNP:rs1130409,PMID:15489334 P27695 UniProtKB Mutagenesis 6 6 . . . Note=Lack of acetylation%2C does not stimulate the YBX1-mediated MDR1 promoter activity and alter nuclear subcellular localization%3B when associated with R-7. Does not inhibit interaction with HDAC1%2C HDAC2 and HDAC3. Absence of increase in nCaRE binding activity. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14633989,ECO:0000269|PubMed:15942031,ECO:0000269|PubMed:18809583,ECO:0000269|PubMed:19934257;Dbxref=PMID:14633989,PMID:15942031,PMID:18809583,PMID:19934257 P27695 UniProtKB Mutagenesis 7 7 . . . Note=Lack of acetylation and does not stimulate the YBX1-mediated MDR1 promoter activity and alter nuclear subcellular localization%3B when associated with R-6. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14633989,ECO:0000269|PubMed:15942031,ECO:0000269|PubMed:18809583,ECO:0000269|PubMed:19934257;Dbxref=PMID:14633989,PMID:15942031,PMID:18809583,PMID:19934257 P27695 UniProtKB Mutagenesis 12 12 . . . Note=Reduces nuclear localization%3B when associated with A-13. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15942031;Dbxref=PMID:15942031 P27695 UniProtKB Mutagenesis 13 13 . . . Note=Reduces nuclear localization%3B when associated with A-12. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15942031;Dbxref=PMID:15942031 P27695 UniProtKB Mutagenesis 24 24 . . . Note=Enhances the interaction with TOMM20. Inhibits rRNA binding%2C interaction with NPM1%2C nuclear localization and modulates its endodeoxyribonuclease activity%3B when associated with A-25%3B A-27%3B A-31 and A-32. Inhibits ubiquitination%3B when associated with K-25 and K-27. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19219073,ECO:0000269|PubMed:20231292,ECO:0000269|PubMed:20699270;Dbxref=PMID:19219073,PMID:20231292,PMID:20699270 P27695 UniProtKB Mutagenesis 25 25 . . . Note=Enhances the interaction with TOMM20. Inhibits rRNA binding%2C interaction with NPM1%2C nuclear localization and modulates its endodeoxyribonuclease activity%3B when associated with A-24%3B A-27%3B A-31 and A-32. Inhibits ubiquitination%3B when associated with K-24 and K-27. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19219073,ECO:0000269|PubMed:20231292,ECO:0000269|PubMed:20699270;Dbxref=PMID:19219073,PMID:20231292,PMID:20699270 P27695 UniProtKB Mutagenesis 27 27 . . . Note=Enhances the interaction with TOMM20. Inhibits rRNA binding%2C interaction with NPM1%2C nuclear localization and modulates its endodeoyribonuclease activity%3B when associated with A-24%3B A-25%3B A-31 and A-32. Inhibits ubiquitination%3B when associated with K-24 and K-25. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19219073,ECO:0000269|PubMed:20231292,ECO:0000269|PubMed:20699270;Dbxref=PMID:19219073,PMID:20231292,PMID:20699270 P27695 UniProtKB Mutagenesis 31 31 . . . Note=Enhances the interaction with TOMM20. Does not inhibit redox and AP endodeoyribonuclease activities. Inhibits rRNA binding%2C interaction with NPM1%2C nuclear localization and modulates its endodeoxyribonuclease activity%3B when associated with A-24%3B A-25%3B A-27 and A-32. Reduces protection from granzyme A-mediated cell death%3B when associated with A-65 and A-210. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12524539,ECO:0000269|PubMed:20231292,ECO:0000269|PubMed:20699270;Dbxref=PMID:12524539,PMID:20231292,PMID:20699270 P27695 UniProtKB Mutagenesis 32 32 . . . Note=Inhibits rRNA binding%2C interaction with NPM1%2C nuclear localization and modulates its endodeoxyribonuclease activity%3B when associated with A-24%3B A-25%3B A-27 and A-31. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20699270;Dbxref=PMID:20699270 P27695 UniProtKB Mutagenesis 65 65 . . . Note=Abolishes the redox activity. Does not abolish the AP endodeoxyribonuclease and phosphodiesterase activities. Reduces protection from granzyme A-mediated cell death%3B when associated with A-31 and A-210. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12524539,ECO:0000269|PubMed:18579163,ECO:0000269|PubMed:8355688;Dbxref=PMID:12524539,PMID:18579163,PMID:8355688 P27695 UniProtKB Mutagenesis 65 65 . . . Note=Does not abolish NO-induced nitrosylation. Enhances NO-induced nuclear export. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12524539,ECO:0000269|PubMed:18579163,ECO:0000269|PubMed:8355688;Dbxref=PMID:12524539,PMID:18579163,PMID:8355688 P27695 UniProtKB Mutagenesis 68 68 . . . Note=Nearly abolishes AP endodeoxyribonuclease activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21762700;Dbxref=PMID:21762700 P27695 UniProtKB Mutagenesis 70 70 . . . Note=Strongly reduces AP endodeoxyribonuclease activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21762700;Dbxref=PMID:21762700 P27695 UniProtKB Mutagenesis 93 93 . . . Note=Abolishes partially the redox activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18579163,ECO:0000269|PubMed:8355688;Dbxref=PMID:18579163,PMID:8355688 P27695 UniProtKB Mutagenesis 93 93 . . . Note=Does not abolish NO-induced nitrosylation. Abolishes NO-induced nitrosylation and translocation from the nucleus to the cytoplasm%3B when associated with S-310. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18579163,ECO:0000269|PubMed:8355688;Dbxref=PMID:18579163,PMID:8355688 P27695 UniProtKB Mutagenesis 96 96 . . . Note=Lacks MYCCRDRNA cleavage activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19401441;Dbxref=PMID:19401441 P27695 UniProtKB Mutagenesis 99 99 . . . Note=Does not abolish the redox activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18579163,ECO:0000269|PubMed:8355688;Dbxref=PMID:18579163,PMID:8355688 P27695 UniProtKB Mutagenesis 138 138 . . . Note=Does not abolish the redox activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18579163,ECO:0000269|PubMed:8355688;Dbxref=PMID:18579163,PMID:8355688 P27695 UniProtKB Mutagenesis 171 171 . . . Note=Abolishes the AP endodeoxyribonuclease activity. Y->A%2CF%2CH;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15380100,ECO:0000269|PubMed:21762700;Dbxref=PMID:15380100,PMID:21762700 P27695 UniProtKB Mutagenesis 208 208 . . . Note=Does not abolish the redox activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18579163,ECO:0000269|PubMed:8355688;Dbxref=PMID:18579163,PMID:8355688 P27695 UniProtKB Mutagenesis 210 210 . . . Note=Abolishes the AP endodeoxyribonuclease activity. Reduces protection from granzyme A-mediated cell death%3B when associated with A-31 and A-65. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12524539;Dbxref=PMID:12524539 P27695 UniProtKB Mutagenesis 212 212 . . . Note=Abolishes AP endodeoxyribonuclease activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8932375;Dbxref=PMID:8932375 P27695 UniProtKB Mutagenesis 212 212 . . . Note=Decreases AP endodeoxyribonuclease activity. N->Q%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8932375;Dbxref=PMID:8932375 P27695 UniProtKB Mutagenesis 266 266 . . . Note=Strongly reduces AP endodeoxyribonuclease activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21762700;Dbxref=PMID:21762700 P27695 UniProtKB Mutagenesis 283 283 . . . Note=Strongly reduces AP endodeoxyribonuclease activity%2C but does not affect RNA cleavage activity. Nearly abolishes AP endodeoxyribonuclease activity%3B when associated with A-308. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21762700,ECO:0000269|PubMed:9804799;Dbxref=PMID:21762700,PMID:9804799 P27695 UniProtKB Mutagenesis 296 296 . . . Note=Does not abolish the redox activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18579163,ECO:0000269|PubMed:8355688;Dbxref=PMID:18579163,PMID:8355688 P27695 UniProtKB Mutagenesis 299 299 . . . Note=Reduces the interaction with TOMM20. Abolishes localization in the mitochondria%3B when associated with A-301. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20231292;Dbxref=PMID:20231292 P27695 UniProtKB Mutagenesis 301 301 . . . Note=Reduces the interaction with TOMM20. Abolishes localization in the mitochondria%3B when associated with A-299. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20231292;Dbxref=PMID:20231292 P27695 UniProtKB Mutagenesis 303 303 . . . Note=Reduces the interaction with TOMM20. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20231292;Dbxref=PMID:20231292 P27695 UniProtKB Mutagenesis 308 308 . . . Note=Reduces AP endodeoxyribonuclease activity. Nearly abolishes AP endodeoxyribonuclease activity%3B when associated with A-283. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21762700,ECO:0000269|PubMed:9804799;Dbxref=PMID:21762700,PMID:9804799 P27695 UniProtKB Mutagenesis 309 309 . . . Note=Abolishes AP endodeoxyribonuclease activity. Lacks MYCCRDRNA cleavage activity. H->N%2CS;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19401441,ECO:0000269|PubMed:21762700,ECO:0000269|PubMed:9804799;Dbxref=PMID:19401441,PMID:21762700,PMID:9804799 P27695 UniProtKB Mutagenesis 310 310 . . . Note=Does not abolish the redox activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18579163,ECO:0000269|PubMed:8355688;Dbxref=PMID:18579163,PMID:8355688 P27695 UniProtKB Mutagenesis 310 310 . . . Note=Does not abolish NO-induced nitrosylation. Abolishes NO-induced nitrosylation and translocation from the nucleus to the cytoplasm%3B when associated with S-93. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18579163,ECO:0000269|PubMed:8355688;Dbxref=PMID:18579163,PMID:8355688 P27695 UniProtKB Sequence conflict 57 57 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P27695 UniProtKB Sequence conflict 306 306 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P27695 UniProtKB Beta strand 62 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Helix 72 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Helix 80 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 90 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5DFF P27695 UniProtKB Helix 106 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Helix 112 114 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4QHE P27695 UniProtKB Beta strand 116 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 122 124 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MEV P27695 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4QHE P27695 UniProtKB Beta strand 131 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 140 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Helix 149 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 152 155 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 157 161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 166 171 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Helix 177 179 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Helix 182 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 205 210 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Helix 217 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Turn 224 228 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Turn 230 232 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LPI P27695 UniProtKB Helix 234 246 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 249 251 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MCR P27695 UniProtKB Helix 252 256 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 257 259 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DE9 P27695 UniProtKB Beta strand 265 267 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7U50 P27695 UniProtKB Helix 270 272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BOW P27695 UniProtKB Helix 273 276 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 283 287 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Helix 289 294 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 295 300 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 306 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3 P27695 UniProtKB Beta strand 312 316 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TC3