##gff-version 3 P01903 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6600932,ECO:0000269|PubMed:6812963,ECO:0000269|PubMed:6955253;Dbxref=PMID:6600932,PMID:6812963,PMID:6955253 P01903 UniProtKB Chain 26 254 . . . ID=PRO_0000018947;Note=HLA class II histocompatibility antigen%2C DR alpha chain P01903 UniProtKB Topological domain 26 216 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P01903 UniProtKB Transmembrane 217 239 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P01903 UniProtKB Topological domain 240 254 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P01903 UniProtKB Domain 112 204 . . . Note=Ig-like C1-type P01903 UniProtKB Region 26 109 . . . Note=Alpha-1 P01903 UniProtKB Region 110 203 . . . Note=Alpha-2 P01903 UniProtKB Region 204 216 . . . Note=Connecting peptide P01903 UniProtKB Site 34 34 . . . Note=Self- and pathogen-derived peptide antigen;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17583734,ECO:0000269|PubMed:21115828,ECO:0000269|PubMed:23260142,ECO:0000269|PubMed:8145819,ECO:0007744|PDB:4GBX;Dbxref=PMID:17583734,PMID:21115828,PMID:23260142,PMID:8145819 P01903 UniProtKB Site 74 74 . . . Note=Self-peptide antigen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31619516;Dbxref=PMID:31619516 P01903 UniProtKB Site 76 76 . . . Note=Self- and pathogen-derived peptide antigen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21115828,ECO:0000269|PubMed:8145819;Dbxref=PMID:21115828,PMID:8145819 P01903 UniProtKB Site 77 77 . . . Note=Self-peptide antigen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31619516;Dbxref=PMID:31619516 P01903 UniProtKB Site 78 78 . . . Note=Self- and pathogen-derived peptide antigen;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17583734,ECO:0000269|PubMed:21115828,ECO:0000269|PubMed:31619516,ECO:0000269|PubMed:8145819;Dbxref=PMID:17583734,PMID:21115828,PMID:31619516,PMID:8145819 P01903 UniProtKB Site 80 80 . . . Note=Pathogen-derived peptide antigen;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:23260142,ECO:0007744|PDB:4GBX;Dbxref=PMID:23260142 P01903 UniProtKB Site 87 87 . . . Note=Self- and pathogen-derived peptide antigen;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17583734,ECO:0000269|PubMed:21115828,ECO:0000269|PubMed:23260142,ECO:0000269|PubMed:31619516,ECO:0000269|PubMed:8145819,ECO:0007744|PDB:4GBX;Dbxref=PMID:17583734,PMID:21115828,PMID:23260142,PMID:31619516,PMID:8145819 P01903 UniProtKB Site 94 94 . . . Note=Pathogen-derived peptide antigen;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17583734,ECO:0000269|PubMed:21115828,ECO:0000269|PubMed:23260142,ECO:0000269|PubMed:8145819,ECO:0007744|PDB:4FQX,ECO:0007744|PDB:4GBX;Dbxref=PMID:17583734,PMID:21115828,PMID:23260142,PMID:8145819 P01903 UniProtKB Site 101 101 . . . Note=Self- and pathogen-derived peptide antigen;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17583734,ECO:0000269|PubMed:23260142,ECO:0000269|PubMed:31619516,ECO:0000269|PubMed:8145819,ECO:0007744|PDB:4FQX,ECO:0007744|PDB:4GBX;Dbxref=PMID:17583734,PMID:23260142,PMID:31619516,PMID:8145819 P01903 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19159218,ECO:0000269|PubMed:7477400;Dbxref=PMID:19159218,PMID:7477400 P01903 UniProtKB Glycosylation 143 143 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19159218,ECO:0000269|PubMed:7477400;Dbxref=PMID:19159218,PMID:7477400 P01903 UniProtKB Disulfide bond 132 188 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:11163233,ECO:0000269|PubMed:12244309,ECO:0000269|PubMed:16079912,ECO:0000269|PubMed:17583734,ECO:0000269|PubMed:31619516,ECO:0000269|PubMed:7477400;Dbxref=PMID:11163233,PMID:12244309,PMID:16079912,PMID:17583734,PMID:31619516,PMID:7477400 P01903 UniProtKB Cross-link 244 244 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19117940;Dbxref=PMID:19117940 P01903 UniProtKB Natural variant 16 16 . . . ID=VAR_035241;Note=V->L;Dbxref=dbSNP:rs16822586 P01903 UniProtKB Natural variant 242 242 . . . ID=VAR_004399;Note=In allele DRA*01:01. L->V;Dbxref=dbSNP:rs7192 P01903 UniProtKB Mutagenesis 65 65 . . . Note=Impairs the interaction with HLA-DM complex%2C CLIP dissociation and peptide exchange. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11070170,ECO:0000269|PubMed:23260142;Dbxref=PMID:11070170,PMID:23260142 P01903 UniProtKB Mutagenesis 68 68 . . . Note=Decreases the interaction with HLA-DM complex and peptide exchange. W->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23260142;Dbxref=PMID:23260142 P01903 UniProtKB Mutagenesis 74 74 . . . Note=Increases the interaction with HLA-DM complex and peptide exchange. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23260142;Dbxref=PMID:23260142 P01903 UniProtKB Mutagenesis 76 76 . . . Note=Impairs the interaction with HLA-DM complex%2C CLIP dissociation and peptide exchange. F->A%2CS%2CV%2CL;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11070170,ECO:0000269|PubMed:23260142;Dbxref=PMID:11070170,PMID:23260142 P01903 UniProtKB Mutagenesis 76 76 . . . Note=Increases the interaction with HLA-DM complex and peptide exchange. F->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23260142;Dbxref=PMID:23260142 P01903 UniProtKB Mutagenesis 78 78 . . . Note=Decreases the interaction with HLA-DM complex and peptide exchange. S->D%2CH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23260142;Dbxref=PMID:23260142 P01903 UniProtKB Mutagenesis 79 79 . . . Note=Increases the interaction with HLA-DM complex and peptide exchange. F->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23260142;Dbxref=PMID:23260142 P01903 UniProtKB Mutagenesis 80 80 . . . Note=Increases the interaction with HLA-DM complex and peptide exchange. Decreases the affinity of the interaction with TCR by more than five-fold. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23260142,ECO:0000269|PubMed:29884618;Dbxref=PMID:23260142,PMID:29884618 P01903 UniProtKB Mutagenesis 82 82 . . . Note=Decreases the interaction with HLA-DM complex and peptide exchange. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23260142;Dbxref=PMID:23260142 P01903 UniProtKB Mutagenesis 93 93 . . . Note=Decreases the affinity of the interaction with TCR by more than five-fold. A->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29884618;Dbxref=PMID:29884618 P01903 UniProtKB Mutagenesis 115 115 . . . Note=Decreases the interaction with CD4. T->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27114505;Dbxref=PMID:27114505 P01903 UniProtKB Mutagenesis 117 117 . . . Note=Decreases the interaction with CD4. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27114505;Dbxref=PMID:27114505 P01903 UniProtKB Mutagenesis 121 121 . . . Note=Decreases the interaction with HLA-DM complex and peptide exchange. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23260142;Dbxref=PMID:23260142 P01903 UniProtKB Mutagenesis 125 125 . . . Note=Impairs the interaction with HLA-DM complex and peptide exchange. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23260142;Dbxref=PMID:23260142 P01903 UniProtKB Mutagenesis 244 244 . . . Note=Almost no change in down-regulation of MHCII. No ubiquitination and complete loss of down-regulation of MHCII%3B when associated with 'R-254' of HLA-DRB. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19117940;Dbxref=PMID:19117940 P01903 UniProtKB Sequence conflict 28 29 . . . Note=EE->AD;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Sequence conflict 33 33 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Sequence conflict 34 35 . . . Note=QA->YP;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Sequence conflict 48 48 . . . Note=M->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Sequence conflict 54 54 . . . Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Sequence conflict 59 59 . . . Note=V->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Sequence conflict 64 64 . . . Note=K->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Sequence conflict 67 67 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Sequence conflict 69 69 . . . Note=R->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Sequence conflict 75 75 . . . Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Sequence conflict 78 78 . . . Note=S->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Sequence conflict 149 149 . . . Note=N->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 P01903 UniProtKB Beta strand 29 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Turn 41 43 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Beta strand 44 51 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Beta strand 54 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Turn 61 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Beta strand 65 70 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Helix 71 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Helix 82 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Turn 102 104 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3C5J P01903 UniProtKB Beta strand 113 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3S4S P01903 UniProtKB Beta strand 128 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Beta strand 143 148 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4X5W P01903 UniProtKB Beta strand 155 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2FSE P01903 UniProtKB Beta strand 166 168 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6CPN P01903 UniProtKB Beta strand 170 178 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Beta strand 186 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9 P01903 UniProtKB Beta strand 195 197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YX9 P01903 UniProtKB Beta strand 199 203 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NI9