ID A0A1Z2RP67_HUMAN Unreviewed; 220 AA. AC A0A1Z2RP67; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 11-DEC-2019, entry version 8. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:ASA45562.1}; DE Flags: Fragment; GN Name=HLA-DQB1 {ECO:0000313|EMBL:ASA45562.1}; 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:ASA45562.1}; RN [1] {ECO:0000313|EMBL:ASA45562.1} RP NUCLEOTIDE SEQUENCE. RA Oh H.-B., Kim S.-K., Park B.G., Jun J.-H., Im J.; RT "DQB1*variant allele."; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. 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; KY658454; ASA45562.1; -; Genomic_DNA. DR SMR; A0A1Z2RP67; -. DR ChiTaRS; HLA-DQB1; human. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 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 3: Inferred from homology; KW Adaptive immunity {ECO:0000256|SAAS:SAAS01191061}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00288615}; KW Immunity {ECO:0000256|SAAS:SAAS00288599}; KW Membrane {ECO:0000256|SAAS:SAAS00288628}; KW MHC II {ECO:0000256|SAAS:SAAS00288621}; Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00288613}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00288610}. FT SIGNAL 1..32 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 33..220 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5011111122" FT DOMAIN 129..217 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT NON_TER 220 FT /evidence="ECO:0000313|EMBL:ASA45562.1" SQ SEQUENCE 220 AA; 25452 MW; F97DE43EACF282F4 CRC64; MSWKKALRIP GGLRVATVTL MLAMLSTPVA EGRDSPEDFV FQFKGMCYFT NGTELVRGVT RYIYNREEYA RFDSDVGVYR AVTPLGRLDA EYWNSQKDIL EEDRASVDTV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNDQEE TTGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQNPIIVEW //