DMB_HUMAN
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 03-AUG-2022, entry version 201.
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;
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; 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}.
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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_002118.4.
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 PDBsum; 1HDM; -.
DR PDBsum; 2BC4; -.
DR PDBsum; 4FQX; -.
DR PDBsum; 4GBX; -.
DR PDBsum; 4I0P; -.
DR AlphaFoldDB; P28068; -.
DR BioGRID; 109354; 65.
DR DIP; DIP-6185N; -.
DR IntAct; P28068; 11.
DR MINT; P28068; -.
DR STRING; 9606.ENSP00000398890; -.
DR GlyGen; P28068; 1 site.
DR iPTMnet; P28068; -.
DR PhosphoSitePlus; P28068; -.
DR BioMuta; HLA-DMB; -.
DR DMDM; 133160; -.
DR jPOST; P28068; -.
DR MassIVE; P28068; -.
DR PaxDb; P28068; -.
DR PeptideAtlas; P28068; -.
DR PRIDE; P28068; -.
DR ProteomicsDB; 54443; -.
DR Antibodypedia; 48533; 296 antibodies from 29 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; ENSG00000242574.9.
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 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 neXtProt; NX_P28068; -.
DR OpenTargets; ENSG00000242574; -.
DR PharmGKB; PA35059; -.
DR VEuPathDB; HostDB:ENSG00000242574; -.
DR eggNOG; ENOG502SAA4; Eukaryota.
DR GeneTree; ENSGT00940000160381; -.
DR HOGENOM; CLU_092834_0_0_1; -.
DR InParanoid; P28068; -.
DR OrthoDB; 1029280at2759; -.
DR PhylomeDB; P28068; -.
DR TreeFam; TF335727; -.
DR PathwayCommons; P28068; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR SignaLink; P28068; -.
DR SIGNOR; P28068; -.
DR BioGRID-ORCS; 3109; 11 hits in 1061 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 100 other tissues.
DR ExpressionAtlas; P28068; baseline and differential.
DR Genevisible; P28068; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:UniProtKB.
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: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 Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.320.10; -; 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; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR014745; MHC_II_a/b_N.
DR InterPro; IPR000353; MHC_II_b_N.
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; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Disulfide bond; Endosome; Glycoprotein;
KW Immunity; Immunoglobulin domain; Lysosome; Membrane; MHC II;
KW Reference proteome; Signal; Transmembrane; 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 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
