ID DMB_HUMAN Reviewed; 263 AA. AC P28068; O77936; Q13012; Q29751; Q58ZE2; Q5SNZ8; Q5STC4; Q9XRX2; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 2. DT 02-SEP-2026, entry version 219. DE RecName: Full=HLA class II histocompatibility antigen, DM beta chain; DE AltName: Full=MHC class II antigen DMB; DE AltName: Full=Really interesting new gene 7 protein; DE Flags: Precursor; GN Name=HLA-DMB; Synonyms=DMB, RING7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DMB*01:01). RX PubMed=1922365; DOI=10.1038/353571a0; RA Kelly A.P., Monaco J.J., Cho S., Trowsdale J.; RT "A new human HLA class II-related locus, DM."; RL Nature 353:571-573(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DMB*01:01). RX PubMed=8034636; DOI=10.1016/s0021-9258(17)32242-1; RA Radley E., Alderton R.P., Kelly A., Trowsdale J., Beck S.; RT "Genomic organization of HLA-DMA and HLA-DMB. Comparison of the gene RT organization of all six class II families in the human major RT histocompatibility complex."; RL J. Biol. Chem. 269:18834-18838(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DMB*01:01). RX PubMed=8568858; DOI=10.1006/jmbi.1996.0001; RA Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., Hosking L.K., RA Jackson A., Kelly A., Newell W.R., Sanseau P., Radley E., Thorpe K.L., RA Trowsdale J.; RT "Evolutionary dynamics of non-coding sequences within the class II region RT of the human MHC."; RL J. Mol. Biol. 255:1-13(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DMB*01:07). RX PubMed=15787724; DOI=10.1111/j.1399-0039.2005.00385.x; RA Gu H., Moon S.-M., Kim J.-J., Ryu H.-J., Kwack K., Kimm K., Lee J.-K., RA Oh B.; RT "Identification of a novel HLA-DMB allele (DMB*0107) in the Korean RT population."; RL Tissue Antigens 65:393-394(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DMB*01:03). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DMB*01:01). RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 114-207 (ALLELES DMB*01:02 AND RP DMB*01:03). RX PubMed=8225438; DOI=10.1007/bf00171797; RA Sanderson F., Powis S.H., Kelly A.P., Trowsdale J.; RT "Limited polymorphism in HLA-DM does not involve the peptide binding RT groove."; RL Immunogenetics 39:56-58(1994). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 121-200 (ALLELE DMB*01:04). RX PubMed=8406617; DOI=10.1007/bf00184526; RA Carrington M., Yeager M., Mann D.; RT "Characterization of HLA-DMB polymorphism."; RL Immunogenetics 38:446-449(1993). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-207 (ALLELE DMB*01:05). RC TISSUE=Blood; RX PubMed=9157091; DOI=10.1016/0198-8859(95)00171-9; RA Kim T.-G., Carrington M., Choi H.B., Kim H.Y., Han H.; RT "Three HLA-DMB variants in Korean patients with autoimmune diseases."; RL Hum. Immunol. 46:58-60(1996). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-112 AND 152-207 (ALLELE DMB*01:06). RX PubMed=10885572; DOI=10.1034/j.1399-0039.2000.550514.x; RA McTernan C.L., Mijovic C.H., Cockram C.S., Barnett A.H.; RT "The nucleotide sequence of a new DMB allele, DMB*0106."; RL Tissue Antigens 55:470-472(2000). RN [12] RP FUNCTION. RX PubMed=8849454; DOI=10.1126/science.274.5287.618; RA Weber D.A., Evavold B.D., Jensen P.E.; RT "Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA- RT DM."; RL Science 274:618-620(1996). RN [13] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-248 AND LEU-251. RX PubMed=8757605; DOI=10.4049/jimmunol.157.3.1017; RA Copier J., Kleijmeer M.J., Ponnambalam S., Oorschot V., Potter P., RA Trowsdale J., Kelly A.; RT "Targeting signal and subcellular compartments involved in the RT intracellular trafficking of HLA-DMB."; RL J. Immunol. 157:1017-1027(1996). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-218 IN COMPLEX WITH DMA, RP FUNCTION, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=9768757; DOI=10.1016/s1074-7613(00)80620-2; RA Mosyak L., Zaller D.M., Wiley D.C.; RT "The structure of HLA-DM, the peptide exchange catalyst that loads antigen RT onto class II MHC molecules during antigen presentation."; RL Immunity 9:377-383(1998). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 19-218 IN COMPLEX WITH DMA, RP FUNCTION, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=16547258; DOI=10.4049/jimmunol.176.7.4208; RA Nicholson M.J., Moradi B., Seth N.P., Xing X., Cuny G.D., Stein R.L., RA Wucherpfennig K.W.; RT "Small molecules that enhance the catalytic efficiency of HLA-DM."; RL J. Immunol. 176:4208-4220(2006). RN [17] {ECO:0007744|PDB:4FQX, ECO:0007744|PDB:4GBX} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 19-211 IN COMPLEX WITH MHCII, RP SUBUNIT, DISULFIDE BOND, FUNCTION, AND MUTAGENESIS OF GLU-26; ASP-49; RP GLU-65; LEU-69; ALA-73 AND ARG-128. RX PubMed=23260142; DOI=10.1016/j.cell.2012.11.025; RA Pos W., Sethi D.K., Call M.J., Schulze M.S., Anders A.K., Pyrdol J., RA Wucherpfennig K.W.; RT "Crystal structure of the HLA-DM-HLA-DR1 complex defines mechanisms for RT rapid peptide selection."; RL Cell 151:1557-1568(2012). CC -!- FUNCTION: Plays a critical role in catalyzing the release of class II- CC associated invariant chain peptide (CLIP) from newly synthesized MHC CC class II molecules and freeing the peptide binding site for acquisition CC of antigenic peptides. In B-cells, the interaction between HLA-DM and CC MHC class II molecules is regulated by HLA-DO. CC {ECO:0000269|PubMed:16547258, ECO:0000269|PubMed:23260142, CC ECO:0000269|PubMed:8849454, ECO:0000269|PubMed:9768757}. CC -!- SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain (DMB) CC (PubMed:16547258, PubMed:9768757). Interacts with MHCII; this CC interaction mediates rapid selection of high-affinity peptides in a pH- CC dependent manner, with an optimum at pH 5.5 (PubMed:23260142). CC {ECO:0000269|PubMed:16547258, ECO:0000269|PubMed:23260142, CC ECO:0000269|PubMed:9768757}. CC -!- INTERACTION: CC P28068; Q9Y2T2: AP3M1; NbExp=2; IntAct=EBI-2877138, EBI-2371151; CC P28068; P28067: HLA-DMA; NbExp=22; IntAct=EBI-2877138, EBI-3865396; CC -!- SUBCELLULAR LOCATION: Late endosome membrane CC {ECO:0000269|PubMed:8757605}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:8757605}. Lysosome membrane CC {ECO:0000269|PubMed:8757605}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:8757605}. Note=Localizes to late endocytic CC compartment. Associates with lysosome membranes. CC -!- DOMAIN: The YXXZ (Tyr-Xaa-Xaa-Zaa, where Zaa is a hydrophobic residue) CC motif mediates the targeting to the lysosomal compartments. CC -!- POLYMORPHISM: The following alleles of DMB are known: DMB*01:01, CC DMB*01:02, DMB*01:03, DMB*01:04 (DMB3.4), DMB*01:05, DMB*01:06, and CC DMB*01:07. The sequence shown is that of DMB*01:03. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z23139; CAA80670.1; -; mRNA. DR EMBL; U15085; AAB60387.1; -; mRNA. DR EMBL; X76776; CAA54171.1; -; Genomic_DNA. DR EMBL; X87344; CAA60782.1; -; Genomic_DNA. DR EMBL; AY645722; AAV97947.1; -; mRNA. DR EMBL; AL662845; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL645941; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL935042; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX088556; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927138; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR752645; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03657.1; -; Genomic_DNA. DR EMBL; BC027175; AAH27175.1; -; mRNA. DR EMBL; Z24750; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z24751; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U00700; AAA03296.1; -; Genomic_DNA. DR EMBL; U16762; AAC50514.1; -; Genomic_DNA. DR EMBL; AF134890; AAD30279.1; -; Genomic_DNA. DR EMBL; AF072680; AAC26112.1; -; Genomic_DNA. DR CCDS; CCDS4760.1; -. DR PIR; I37533; I37533. DR RefSeq; NP_002109.2; NM_002118.5. DR PDB; 1HDM; X-ray; 2.50 A; B=19-218. DR PDB; 2BC4; X-ray; 2.27 A; B/D=19-218. DR PDB; 4FQX; X-ray; 2.60 A; D=19-211. DR PDB; 4GBX; X-ray; 3.00 A; D=19-211. DR PDB; 4I0P; X-ray; 3.20 A; B/F=21-211. DR AlphaFoldDB; P28068; -. DR SMR; P28068; -. DR BioGRID; 109354; 75. DR DIP; DIP-6185N; -. DR FunCoup; P28068; 455. DR IntAct; P28068; 53. DR MINT; P28068; -. DR NDEx; IQUERY-CP-HLA-DMB; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000398890; -. DR GlyCosmos; P28068; 1 site, No reported glycans. DR GlyGen; P28068; 1 site, 12 N-linked glycans (1 site). DR iPTMnet; P28068; -. DR PhosphoSitePlus; P28068; -. DR BioMuta; HLA-DMB; -. DR DMDM; 133160; -. DR jPOST; P28068; -. DR MassIVE; P28068; -. DR PaxDb; 9606-ENSP00000398890; -. DR PeptideAtlas; P28068; -. DR ProteomicsDB; 54443; -. DR Antibodypedia; 48533; 310 antibodies from 32 providers. DR DNASU; 3109; -. DR Ensembl; ENST00000383231.6; ENSP00000372718.2; ENSG00000241674.8. DR Ensembl; ENST00000395312.7; ENSP00000378723.3; ENSG00000242092.8. DR Ensembl; ENST00000412948.6; ENSP00000413471.2; ENSG00000241296.8. DR Ensembl; ENST00000418107.3; ENSP00000398890.2; ENSG00000242574.10. DR Ensembl; ENST00000424822.6; ENSP00000414817.2; ENSG00000234154.10. DR Ensembl; ENST00000428420.6; ENSP00000393646.2; ENSG00000239329.8. DR Ensembl; ENST00000440078.6; ENSP00000411321.2; ENSG00000226264.10. DR Ensembl; ENST00000450897.6; ENSP00000408453.2; ENSG00000242386.8. DR GeneID; 3109; -. DR KEGG; hsa:3109; -. DR MANE-Select; ENST00000418107.3; ENSP00000398890.2; NM_002118.5; NP_002109.2. DR UCSC; uc003ocl.2; human. DR AGR; HGNC:4935; -. DR ClinPGx; PA35059; -. DR CTD; 3109; -. DR DisGeNET; 3109; -. DR GeneCards; HLA-DMB; -. DR HGNC; HGNC:4935; HLA-DMB. DR HPA; ENSG00000242574; Tissue enhanced (intestine, lymphoid tissue). DR MIM; 142856; gene. DR OpenTargets; ENSG00000242574; -. DR VEuPathDB; HostDB:ENSG00000242574; -. DR eggNOG; ENOG502SAA4; Eukaryota. DR GeneTree; ENSGT00940000160381; -. DR HOGENOM; CLU_092834_0_0_1; -. DR InParanoid; P28068; -. DR OMA; TYCVAYN; -. DR OrthoDB; 9940220at2759; -. DR PAN-GO; P28068; 9 GO annotations based on evolutionary models. DR PhylomeDB; P28068; -. DR PathwayCommons; P28068; -. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR SignaLink; P28068; -. DR SIGNOR; P28068; -. DR Agora; ENSG00000242574; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 3109; 11 hits in 1138 CRISPR screens. DR ChiTaRS; HLA-DMB; human. DR EvolutionaryTrace; P28068; -. DR GeneWiki; HLA-DMB; -. DR GenomeRNAi; 3109; -. DR Pharos; P28068; Tbio. DR PRO; PR:P28068; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P28068; protein. DR Bgee; ENSG00000242574; Expressed in monocyte and 101 other cell types or tissues. DR ExpressionAtlas; P28068; baseline and differential. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; IBA:GO_Central. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:UniProtKB. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002399; P:MHC class II protein complex assembly; IMP:UniProtKB. DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0050778; P:positive regulation of immune response; IBA:GO_Central. DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central. DR GO; GO:2001190; P:positive regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IMP:UniProtKB. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB. DR CDD; cd21002; IgC1_MHC_II_beta_HLA-DM; 1. DR FunFam; 2.60.40.10:FF:000968; MHC class II H2-M beta 2 chain; 1. DR FunFam; 3.10.320.10:FF:000004; MHC class II H2-M beta 2 chain; 1. DR Gene3D; 3.10.320.10; Class II Histocompatibility Antigen, M Beta Chain, Chain B, domain 1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR050160; MHC/Immunoglobulin. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR PANTHER; PTHR19944:SF65; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM BETA CHAIN; 1. DR PANTHER; PTHR19944; MHC CLASS II-RELATED; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. DR PDBsum; 1HDM; -. DR PDBsum; 2BC4; -. DR PDBsum; 4FQX; -. DR PDBsum; 4GBX; -. DR PDBsum; 4I0P; -. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Disulfide bond; Endosome; Glycoprotein; KW Immunity; Immunoglobulin domain; Lysosome; Membrane; MHC II; KW Proteomics identification; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..263 FT /note="HLA class II histocompatibility antigen, DM beta FT chain" FT /id="PRO_0000018960" FT TOPO_DOM 19..218 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 219..239 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 240..263 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 114..208 FT /note="Ig-like C1-type" FT REGION 19..112 FT /note="Beta-1" FT REGION 113..207 FT /note="Beta-2" FT REGION 208..218 FT /note="Connecting peptide" FT /evidence="ECO:0000255" FT MOTIF 248..251 FT /note="YXXZ motif" FT CARBOHYD 110 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT DISULFID 29..97 FT /evidence="ECO:0000269|PubMed:23260142, FT ECO:0007744|PDB:4GBX" FT DISULFID 43..53 FT /evidence="ECO:0000269|PubMed:23260142, FT ECO:0007744|PDB:4GBX" FT DISULFID 135..192 FT /evidence="ECO:0000269|PubMed:23260142, FT ECO:0007744|PDB:4GBX" FT VARIANT 28 FT /note="T -> A (in allele DMB*01:07; dbSNP:rs17583782)" FT /id="VAR_050360" FT VARIANT 45 FT /note="S -> F (in allele DMB*01:06; dbSNP:rs41560814)" FT /id="VAR_016752" FT VARIANT 49 FT /note="D -> V (in allele DMB*01:07; dbSNP:rs17617333)" FT /id="VAR_050361" FT VARIANT 71 FT /note="S -> N (in allele DMB*01:07; dbSNP:rs17617321)" FT /id="VAR_050362" FT VARIANT 162 FT /note="A -> E (in allele DMB*01:02 and allele DMB*01:06; FT dbSNP:rs2071555)" FT /id="VAR_016753" FT VARIANT 162 FT /note="A -> V (in allele DMB*01:04 and allele DMB*01:05; FT dbSNP:rs2071555)" FT /id="VAR_016754" FT VARIANT 197 FT /note="T -> I (in allele DMB*01:01; dbSNP:rs1042337)" FT /evidence="ECO:0000269|PubMed:14574404" FT /id="VAR_016755" FT MUTAGEN 26 FT /note="E->K: Decreases the interaction with MHCII and FT peptide exchange." FT /evidence="ECO:0000269|PubMed:23260142" FT MUTAGEN 49 FT /note="D->K: Decreases the interaction with MHCII and FT peptide exchange." FT /evidence="ECO:0000269|PubMed:23260142" FT MUTAGEN 49 FT /note="D->N: Increases the interaction with MHCII and FT peptide exchange; when associated with Q-65." FT /evidence="ECO:0000269|PubMed:23260142" FT MUTAGEN 65 FT /note="E->Q: Increases the interaction with MHCII and FT peptide exchange; when associated with N-49." FT /evidence="ECO:0000269|PubMed:23260142" FT MUTAGEN 65 FT /note="E->R: Decreases the interaction with MHCII and FT peptide exchange." FT /evidence="ECO:0000269|PubMed:23260142" FT MUTAGEN 69 FT /note="L->D: Decreases the interaction with MHCII and FT peptide exchange." FT /evidence="ECO:0000269|PubMed:23260142" FT MUTAGEN 73 FT /note="A->V: Decreases the interaction with MHCII and FT peptide exchange." FT /evidence="ECO:0000269|PubMed:23260142" FT MUTAGEN 128 FT /note="R->S: Decreases the interaction with MHCII and FT peptide exchange." FT /evidence="ECO:0000269|PubMed:23260142" FT MUTAGEN 248 FT /note="Y->A: Abolishes targeting to endosomes and results FT in relocalization to the cell membrane." FT /evidence="ECO:0000269|PubMed:8757605" FT MUTAGEN 251 FT /note="L->A: Abolishes targeting to endosomes and results FT in relocalization to the cell membrane." FT /evidence="ECO:0000269|PubMed:8757605" FT STRAND 22..32 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:4FQX" FT STRAND 37..46 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 49..55 FT /evidence="ECO:0007829|PDB:2BC4" FT TURN 56..59 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:4I0P" FT HELIX 70..81 FT /evidence="ECO:0007829|PDB:2BC4" FT HELIX 84..91 FT /evidence="ECO:0007829|PDB:2BC4" FT HELIX 93..109 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 116..121 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 128..143 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 154..156 FT /evidence="ECO:0007829|PDB:2BC4" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:4GBX" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 174..182 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 190..195 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:2BC4" FT STRAND 203..207 FT /evidence="ECO:0007829|PDB:2BC4" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:2BC4" SQ SEQUENCE 263 AA; 28931 MW; 9B50E72DD2A2454A CRC64; MITFLPLLLG LSLGCTGAGG FVAHVESTCL LDDAGTPKDF TYCISFNKDL LTCWDPEENK MAPCEFGVLN SLANVLSQHL NQKDTLMQRL RNGLQNCATH TQPFWGSLTN RTRPPSVQVA KTTPFNTREP VMLACYVWGF YPAEVTITWR KNGKLVMPHS SAHKTAQPNG DWTYQTLSHL ALTPSYGDTY TCVVEHTGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGVISW RRAGHSSYTP LPGSNYSEGW HIS //