##gff-version 3 O75509 UniProtKB Signal peptide 1 41 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 O75509 UniProtKB Chain 42 655 . . . ID=PRO_0000034602;Note=Tumor necrosis factor receptor superfamily member 21 O75509 UniProtKB Topological domain 42 349 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75509 UniProtKB Transmembrane 350 370 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75509 UniProtKB Topological domain 371 655 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75509 UniProtKB Repeat 50 88 . . . Note=TNFR-Cys 1 O75509 UniProtKB Repeat 90 131 . . . Note=TNFR-Cys 2 O75509 UniProtKB Repeat 133 167 . . . Note=TNFR-Cys 3 O75509 UniProtKB Repeat 170 211 . . . Note=TNFR-Cys 4 O75509 UniProtKB Domain 415 498 . . . Note=Death;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00064 O75509 UniProtKB Region 243 286 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75509 UniProtKB Region 318 337 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75509 UniProtKB Compositional bias 245 286 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75509 UniProtKB Lipidation 368 368 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Glycosylation 82 82 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Glycosylation 141 141 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Glycosylation 252 252 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Glycosylation 257 257 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Glycosylation 278 278 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Glycosylation 289 289 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Disulfide bond 67 80 . . . . O75509 UniProtKB Disulfide bond 70 88 . . . . O75509 UniProtKB Disulfide bond 91 106 . . . . O75509 UniProtKB Disulfide bond 109 123 . . . . O75509 UniProtKB Disulfide bond 113 131 . . . . O75509 UniProtKB Disulfide bond 133 144 . . . . O75509 UniProtKB Disulfide bond 150 168 . . . . O75509 UniProtKB Disulfide bond 171 186 . . . . O75509 UniProtKB Disulfide bond 192 211 . . . . O75509 UniProtKB Mutagenesis 82 82 . . . Note=Abolishes one glycosylation site and reduces total N-glycosylation%3B when associated with Q-252%3B Q-278 and Q-289. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Mutagenesis 141 141 . . . Note=Abolishes one glycosylation site and reduces total N-glycosylation%3B when associated with Q-82%3B Q-252%3B Q-278 and Q-289. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Mutagenesis 252 252 . . . Note=Abolishes one glycosylation site and reduces total N-glycosylation%3B when associated with Q-278 and Q-289. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Mutagenesis 257 257 . . . Note=Abolishes one glycosylation site and reduces total N-glycosylation%3B when associated with Q-82%3B Q-141%3B Q-252%3B Q-278 and Q-289. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Mutagenesis 278 278 . . . Note=Abolishes one glycosylation site and reduces total N-glycosylation. Abolishes one glycosylation site and reduces total N-glycosylation%3B when associated with Q-82%3B Q-141%3B Q-252%3B Q-257 and Q-289. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Mutagenesis 289 289 . . . Note=Abolishes one glycosylation site and reduces total N-glycosylation%3B when associated with Q-278. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19654028;Dbxref=PMID:19654028 O75509 UniProtKB Mutagenesis 368 368 . . . Note=Abolishes palmitoylation. C->V O75509 UniProtKB Beta strand 53 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Turn 59 61 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 64 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 74 78 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3T O75509 UniProtKB Beta strand 87 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3V O75509 UniProtKB Beta strand 118 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 130 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 137 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 143 146 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 154 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 162 164 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 167 170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 181 183 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Helix 193 195 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 198 201 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 205 207 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 210 212 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U3P O75509 UniProtKB Beta strand 571 573 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DBH O75509 UniProtKB Helix 579 591 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DBH O75509 UniProtKB Helix 598 606 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DBH O75509 UniProtKB Helix 609 616 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DBH O75509 UniProtKB Helix 621 635 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DBH O75509 UniProtKB Helix 637 650 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DBH O75509 UniProtKB Helix 652 654 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DBH