ID O19707_HUMAN Unreviewed; 229 AA. AC O19707; DT 01-JAN-1998, integrated into UniProtKB/TrEMBL. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 138. DE SubName: Full=MHC class II HLA-DQ-beta-1 {ECO:0000313|EMBL:AAC41965.1}; DE Flags: Fragment; GN Name=HLA-DQB1 {ECO:0000313|EMBL:AAC41965.1}; 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 {ECO:0000313|EMBL:AAC41965.1}; RN [1] {ECO:0000313|EMBL:AAC41965.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=8929711; DOI=10.1111/j.1399-0039.1996.tb02512.x; RA Yasunaga S., Kimura A., Hamaguchi K., Ronningen K.S., Sasazuki T.; RT "Different contribution of HLA-DR and -DQ genes in susceptibility and RT resistance to insulin-dependent diabetes mellitus (IDDM)."; RL Tissue Antigens 47:37-48(1996). RN [2] {ECO:0007829|PDB:4Z7U, ECO:0007829|PDB:4Z7V} RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-192 IN COMPLEX WITH FUCOSE, RP GLYCOSYLATION AT ASN-19, AND DISULFIDE BONDS. RX PubMed=25948817; DOI=10.4049/jimmunol.1500161; RA Petersen J., van Bergen J., Loh K.L., Kooy-Winkelaar Y., Beringer D.X., RA Thompson A., Bakker S.F., Mulder C.J., Ladell K., McLaren J.E., Price D.A., RA Rossjohn J., Reid H.H., Koning F.; RT "Determinants of gliadin-specific T cell selection in celiac disease."; RL J. Immunol. 194:6112-6122(2015). RN [3] {ECO:0007829|PDB:5UJT} RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 3-191, AND DISULFIDE BONDS. RX PubMed=29255035; DOI=10.1073/pnas.1716527115; RA Wang Y., Sosinowski T., Novikov A., Crawford F., Neau D.B., Yang J., RA Kwok W.W., Marrack P., Kappler J.W., Dai S.; RT "C-terminal modification of the insulin B:11-23 peptide creates RT superagonists in mouse and human type 1 diabetes."; RL Proc. Natl. Acad. Sci. U.S.A. 115:162-167(2018). RN [4] {ECO:0007829|PDB:6XC9, ECO:0007829|PDB:6XCO} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-192, AND DISULFIDE BONDS. RX PubMed=34433824; DOI=10.1038/s41467-021-25404-x; RA Tran M.T., Faridi P., Lim J.J., Ting Y.T., Onwukwe G., Bhattacharjee P., RA Jones C.M., Tresoldi E., Cameron F.J., La Gruta N.L., Purcell A.W., RA Mannering S.I., Rossjohn J., Reid H.H.; RT "T cell receptor recognition of hybrid insulin peptides bound to HLA-DQ8."; RL Nat. Commun. 12:5110-5110(2021). CC -!- SUBCELLULAR LOCATION: Endosome membrane CC {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004530}. Lysosome membrane CC {ECO:0000256|ARBA:ARBA00004352}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004352}. 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; L34097; AAC41965.1; -; mRNA. DR PDB; 4Z7U; X-ray; 2.70 A; B/D=1-192. DR PDB; 4Z7V; X-ray; 2.65 A; B/D=1-192. DR PDB; 4Z7W; X-ray; 2.89 A; B/D=1-192. DR PDB; 5UJT; X-ray; 1.94 A; B/E/H=3-191. DR PDB; 6XC9; X-ray; 2.40 A; C/H=1-192. DR PDB; 6XCO; X-ray; 2.90 A; B=1-192. DR PDB; 6XCP; X-ray; 3.30 A; C=1-192. DR PDBsum; 4Z7U; -. DR PDBsum; 4Z7V; -. DR PDBsum; 4Z7W; -. DR PDBsum; 5UJT; -. DR AlphaFoldDB; O19707; -. DR SMR; O19707; -. DR GlyCosmos; O19707; 1 site, No reported glycans. DR PeptideAtlas; O19707; -. DR ChiTaRS; HLA-DQB1; human. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR CDD; cd21001; IgC1_MHC_II_beta_HLA-DQ_I-A; 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; 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:SF101; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DQ BETA 1 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. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4Z7U, ECO:0007829|PDB:4Z7V}; KW Adaptive immunity {ECO:0000256|ARBA:ARBA00023130}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Endosome {ECO:0000256|ARBA:ARBA00022753}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Immunity {ECO:0000256|ARBA:ARBA00022859}; KW Lysosome {ECO:0000256|ARBA:ARBA00023228}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|ARBA:ARBA00023182}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 199..219 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 97..201 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT CARBOHYD 19 FT /note="N-acetyl-D-glucosamine" FT /evidence="ECO:0007829|PDB:6XC9, ECO:0007829|PDB:6XCO" FT CARBOHYD 19 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:6XC9, ECO:0007829|PDB:6XCO" FT DISULFID 15..79 FT /evidence="ECO:0007829|PDB:4Z7U, ECO:0007829|PDB:4Z7V" FT DISULFID 117..173 FT /evidence="ECO:0007829|PDB:4Z7U, ECO:0007829|PDB:4Z7V" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAC41965.1" SQ SEQUENCE 229 AA; 26489 MW; 9424CC5558AF92DF CRC64; RDSPEDFVYQ FKGMCYFTNG TERVRLVTRY IYNREEYARF DSDVGVYRAV TPLGPPAAEY WNSQKEVLER TRAELDTVCR HNYQLELRTT LQRRVEPTVT ISPSRTEALN HHNLLVCSVT DFYPAQIKVR WFRNDQEETT GVVSTPLIRN GDWTFQILVM LEMTPQRGDV YTCHVEHPSL QNPIIVEWRA QSESAQSKML SGIGGFVLGL IFLGLGLIIH HRSQKGLLH //