{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P01903","secondaryAccessions":["A2BET4","Q30160","Q6IAZ1","Q861I2","Q9TP70"],"uniProtkbId":"DRA_HUMAN","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2021-02-10","entryVersion":238,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"HLA class II histocompatibility antigen, DR alpha chain"}},"alternativeNames":[{"fullName":{"value":"MHC class II antigen DRA"}}],"flag":"Precursor"},"genes":[{"geneName":{"value":"HLA-DRA"},"synonyms":[{"value":"HLA-DRA1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15265931"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15322540"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17182262"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334368"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22327072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23783831"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24190431"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25413013"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27591323"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29884618"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31495665"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8145819"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9075930"}],"value":"An alpha chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the beta chain HLA-DRB, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DR-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells (PubMed:15265931, PubMed:15322540, PubMed:17334368, PubMed:22327072, PubMed:24190431, PubMed:27591323, PubMed:29884618, PubMed:31495665, PubMed:8145819, PubMed:9075930). Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:8145819). In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor-resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (PubMed:31495665). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (PubMed:17182262, PubMed:23783831). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides (PubMed:25413013). The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (PubMed:8145819)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11070170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11080454"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11163233"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12244309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16079912"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334368"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17583734"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18697946"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21115828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23260142"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25413013"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27114505"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29884618"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31619516"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32668259"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7477400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7479981"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9075930"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9354468"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9782128"}],"value":"Heterotrimer that consists of an alpha chain HLA-DRA, a beta chain HLA-DRB and a peptide (peptide-MHCII) (PubMed:11080454, PubMed:11163233, PubMed:12244309, PubMed:16079912, PubMed:17583734, PubMed:18697946, PubMed:31619516, PubMed:32668259, PubMed:7477400, PubMed:9354468, PubMed:9782128). Newly synthesized alpha and beta chains forms a heterodimer (MHCII) that associates with the CD74/invariant chain (Ii) in the endoplasmic reticulum (ER). Ii is a trimer composed of three subunits and each subunit interacts with one MHCII dimer, blocking the peptide-binding cleft (PubMed:7479981). As a result, MHCII molecules cannot bind peptides present in the ER (PubMed:7479981). The complex of MHCII and CD74/Ii is transported in vesicles from ER to Golgi to lysosomes, where it encounters antigenic peptides generated via proteolysis of endocytosed antigens. MHCII dimers are dissociated from CD74/Ii by the combined action of proteolysis and HLA-DM (PubMed:21115828, PubMed:23260142, PubMed:25413013). Lysosomal enzymes such as cathepsin, degrade CD74/Ii leaving a 24 amino acid remnant called class II-associated Ii or CLIP. Interacts (via the peptide binding cleft) with CLIP; this interaction inhibits antigen peptide binding before entry in the endosomal compartment (PubMed:7477400, PubMed:9075930). The displacement of CLIP and replacement by a high affinity peptide in lysosomes is performed by HLA-DM heterodimer. HLA-DM catalyzes CLIP dissociation from MHCII, stabilizes empty MHCII and mediates the selection of high affinity peptides (PubMed:11070170, PubMed:23260142, PubMed:9075930). Interacts with HLA-DM heterodimer; this interaction is direct (PubMed:25413013). Interacts (via alpha-1 domain) with TCR (via CDRs) (PubMed:17334368, PubMed:29884618). Interacts (via alpha-2 domain) with CD4 (via Ig-like V-type domain); this interaction increases the affinity of TCR for peptide-MHCII (PubMed:27114505)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11864610"}],"value":"(Microbial infection) Interacts with Epstein-Barr virus BZLF2/gp42"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11432818"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21081917"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2210803"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2658055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8152483"}],"value":"(Microbial infection) Interacts with Staphylococcus aureus enterotoxin A/entA, enterotoxin B/entB, enterotoxin C1/entC1, enterotoxin D/entD, and enterotoxin H/entH"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15322540"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18305173"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29884618"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9075930"}],"value":"The MHCII complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation (PubMed:18305173, PubMed:9075930). Component of immunological synapses at the interface between T cell and APC (PubMed:15322540, PubMed:29884618)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15322540"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18305173"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29884618"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass type I membrane protein","id":"SL-9905"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18305173"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass type I membrane protein","id":"SL-9905"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19117940"}],"value":"Early endosome membrane","id":"SL-0093"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass type I membrane protein","id":"SL-9905"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18305173"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19117940"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9075930"}],"value":"Late endosome membrane","id":"SL-0151"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass type I membrane protein","id":"SL-9905"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18305173"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9075930"}],"value":"Lysosome membrane","id":"SL-0157"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass type I membrane protein","id":"SL-9905"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17182262"}],"value":"Autolysosome membrane","id":"SL-0536"},"topology":{"value":"Single-pass type I membrane protein","id":"SL-9905"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15322540"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23783831"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31495665"}],"value":"Expressed in professional APCs: macrophages, dendritic cells and B cells (at protein level) (PubMed:15322540, PubMed:23783831, PubMed:31495665). Expressed in thymic epithelial cells (at protein level) (PubMed:23783831)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15322540"}],"value":"Up-regulated in dendritic cells upon maturation"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17583734"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29884618"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8145819"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9354468"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9782128"}],"value":"The alpha-1 domain is a structural part of the peptide-binding cleft. It contains one alpha helix and 4 beta sheets, respectively forming part of the wall and the floor of the peptide-binding cleft. The other 4 beta sheets of the floor and the second alpha helix wall is formed by the beta-1 domain of HLA-DRB. Forms hydrogen bonds with the peptide main chain via conserved amino acids (PubMed:17583734, PubMed:29884618, PubMed:8145819, PubMed:9354468, PubMed:9782128). The peptide-bound alpha-1 domain forms hydrogen bonds with CDR2 and CDR3 alpha-domain of TCR (PubMed:29884618)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27114505"}],"value":"The alpha-2 Ig-like domain mediates the interaction with CD4 coreceptor"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19117940"}],"value":"Ubiquitinated by MARCHF1 or MARCHF8 at Lys-244 leading to down-regulation of MHCII. When associated with ubiquitination of the beta chain at 'Lys-254', the down-regulation of MHCII may be highly effective"}],"commentType":"PTM"},{"texts":[{"value":"The following alleles of DRA are known: DRA*01:01 and DRA*01:02. The sequence shown is that of DRA*01:02"}],"commentType":"POLYMORPHISM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the MHC class II family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"CAA25076.1","note":"Truncated N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6600932"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6812963"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6955253"}]},{"type":"Chain","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"HLA class II histocompatibility antigen, DR alpha chain","featureId":"PRO_0000018947"},{"type":"Topological 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C1-type"},{"type":"Region","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"Alpha-1"},{"type":"Region","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"Alpha-2"},{"type":"Region","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"Connecting peptide"},{"type":"Site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Self- and pathogen-derived peptide antigen","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17583734"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21115828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23260142"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8145819"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4GBX"}]},{"type":"Site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"Self-peptide antigen","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31619516"}]},{"type":"Site","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"Self- and pathogen-derived peptide 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asparagine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19159218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7477400"}],"featureId":""},{"type":"Disulfide bond","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00114"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11163233"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12244309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16079912"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17583734"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31619516"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7477400"}]},{"type":"Cross-link","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in 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Decreases the affinity of the interaction with TCR by more than five-fold.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23260142"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29884618"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Decreases the interaction with HLA-DM complex and peptide exchange.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23260142"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"Decreases the affinity of the interaction with TCR by more than five-fold.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29884618"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["L"]}},{"type":"Mutagenesis","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"Decreases the interaction with CD4.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27114505"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["R"]}},{"type":"Mutagenesis","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"Decreases the interaction with CD4.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27114505"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["R"]}},{"type":"Mutagenesis","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"Decreases the interaction with HLA-DM complex and peptide exchange.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23260142"}],"alternativeSequence":{"originalSequence":"P","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Impairs the interaction with HLA-DM complex and peptide exchange.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23260142"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"Almost no change in down-regulation of MHCII. 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