ID DQA1_HUMAN Reviewed; 254 AA. AC P01909; O19630; O19706; P01907; P01908; P04225; P04226; P05536; P79553; AC Q06751; Q29876; Q29994; Q2Q6Y6; Q2Q6Y7; Q2Q6Y8; Q2WCM3; Q30064; Q30067; AC Q30068; Q30070; Q30071; Q30072; Q30073; Q30086; Q30101; Q5Y7D5; Q5Y7F5; AC Q6ICU6; Q6PR46; Q6QDB1; Q860W2; Q860W4; Q9BD37; Q9TPM3; Q9UM31; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 210. DE RecName: Full=HLA class II histocompatibility antigen, DQ alpha 1 chain; DE AltName: Full=DC-1 alpha chain; DE AltName: Full=DC-alpha; DE AltName: Full=HLA-DCA; DE AltName: Full=MHC class II DQA1; DE Flags: Precursor; GN Name=HLA-DQA1; 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 DQA1*02:01). RX PubMed=6415485; DOI=10.1038/305813a0; RA Chang H.-C., Moriuchi T., Silver J.; RT "The heavy chain of human B-cell alloantigen HLA-DS has a variable N- RT terminal region and a constant immunoglobulin-like region."; RL Nature 305:813-815(1983). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQA1*05:01). RX PubMed=6585297; DOI=10.1002/j.1460-2075.1984.tb01826.x; RA Schenning L., Larhammar D., Bill P., Wiman K., Jonsson A.-K., Rask L., RA Peterson P.A.; RT "Both alpha and beta chains of HLA-DC class II histocompatibility antigens RT display extensive polymorphism in their amino-terminal domains."; RL EMBO J. 3:447-452(1984). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DQA1*01:02 AND ALLELE DQA1*03:01). RX PubMed=6584734; DOI=10.1038/308327a0; RA Auffray C., Lillie J.W., Arnot D., Grossberger D., Kappes D., RA Strominger J.L.; RT "Isotypic and allotypic variation of human class II histocompatibility RT antigen alpha-chain genes."; RL Nature 308:327-333(1984). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQA1*05:01). RX PubMed=3584986; RA Schiffenbauer J., Didier D.K., Klearman M., Rice K., Shuman S., RA Tieber V.L., Kittlesen D.J., Schwartz B.D.; RT "Complete sequence of the HLA DQ alpha and DQ beta cDNA from a DR5/DQw3 RT cell line."; RL J. Immunol. 139:228-233(1987). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQA1*05:01). RX PubMed=9271631; DOI=10.1007/s002510050295; RA Ellis M.C., Hetisimer A.H., Ruddy D.A., Hansen S.L., Kronmal G.S., RA McClelland E., Quintana L., Drayna D.T., Aldrich M.S., Mignot E.; RT "HLA class II haplotype and sequence analysis support a role for DQ in RT narcolepsy."; RL Immunogenetics 46:410-417(1997). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DQA1*01:01; DQA1*01:02 AND RP DQA1*03:01). RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DQA1*01:02; DQA1*05:06; RP DQA1*05:07 AND DQA1*05:08). RX PubMed=16866887; DOI=10.1111/j.1399-0039.2006.00645.x; RA Lee K.W., Jung Y.A., Oh D.H.; RT "Four novel human leukocyte antigen-DQA1 alleles identified in the Korean RT population."; RL Tissue Antigens 68:167-172(2006). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQA1*03:01). RX PubMed=3036828; DOI=10.1016/s0021-9258(18)47482-0; RA Jonsson A.-K., Hyldig-Nielsen J.-J., Servenius B., Larhammar D., RA Andersson G., Joergensen F., Peterson P.A., Rask L.; RT "Class II genes of the human major histocompatibility complex. Comparisons RT of the DQ and DX alpha and beta genes."; RL J. Biol. Chem. 262:8767-8777(1987). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQA1*01:01). RA Ashdown M.L., Leas L., Gavrilidis A., Wood J.M., Simons M.J.; RT "Identification of a novel DQA1 allele, DQA1*01012, and confirmatory RT sequence of DQA1*01011."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DQA1*02:01). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DQA1*01:02 AND DQA1*05:09). RA Voorter C.E., van den Berg-Loonen E.M.; RT "New and confirmatory HLA sequences by SBT."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DQA1*01:01). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES DQA1*01:02; RP DQA1*03:01 AND DQA1*05:01). 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 [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DQA1*03:01 AND DQA1*05:01). 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 [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-27 (ALLELES RP DQA1*01:01/DQA1*01:02/DQA1*01:03; DQA1*01:04; DQA1*01:05; RP DQA1*02:01/DQA1*03:01/DQA1*03:03; DQA1*04:01/DQA1*06:01 AND RP DQA1*05:01/DQA1*05:03/DQA1*05:05). RC TISSUE=B-cell; RA Yasunaga S., Kimura A., Sasazuki T.; RT "Sequence polymorphisms in HLA-DQA1 exon1."; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [16] RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-254 (ALLELE DQA1*03:02). RX PubMed=3879967; DOI=10.1073/pnas.82.10.3420; RA Moriuchi J., Moriuchi T., Silver J.; RT "Nucleotide sequence of an HLA-DQ alpha chain derived from a DRw9 cell RT line: genetic and evolutionary implications."; RL Proc. Natl. Acad. Sci. U.S.A. 82:3420-3424(1985). RN [17] RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-254 (ALLELE DQA1*01:02). RX PubMed=3259543; DOI=10.1007/bf00364432; RA Lock C.B., So A.K., Welsh K.I., Parkes J.D., Trowsdale J.; RT "MHC class II sequences of an HLA-DR2 narcoleptic."; RL Immunogenetics 27:449-455(1988). RN [18] RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-250 (ALLELE DQA1*03:02/DQA1*03:03) AND RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-249 (ALLELES DQA1*01:01; DQA1*01:03; RP DQA1*01:04; DQA1*04:01; DQA1*05:03; DQA1*05:05 AND DQA1*06:01). 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 [19] RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-249 (ALLELE DQA1*01:05). RA Yasunaga S.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [20] RP PROTEIN SEQUENCE OF 24-89; 102-120 AND 164-212 (ALLELE DQA1*01:02). RX PubMed=6576979; DOI=10.1515/bchm2.1983.364.1.749; RA Goetz H., Kratzin H., Thinnes F.P., Yang C.-Y., Kruse T., Pauly E., RA Koelbel S., Egert G., Wernet P., Hilschmann N.; RT "Primary structure of human class II histocompatibility antigens 3rd RT communication. Amino acid sequence comparison between DR and DC subclass RT antigens derived from a lymphoblastoid B cell line homozygous at the HLA RT loci (HLA-A3,3; B7,7; Dw2,2; DR2,2: MT1,1; Dc1,1: MB1,1)."; RL Hoppe-Seyler's Z. Physiol. Chem. 364:749-755(1983). RN [21] RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-209 (ALLELE DQA1*05:01). RX PubMed=2493052; RA Kao H.T., Gregersen P.K., Tang J.C., Takahashi T., Wang C.Y., Silver J.; RT "Molecular analysis of the HLA class II genes in two DRw6-related RT haplotypes, DRw13 DQw1 and DRw14 DQw3."; RL J. Immunol. 142:1743-1747(1989). RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-203 (ALLELES DQA1*04:02 AND RP DQA1*04:04). RX PubMed=15853899; DOI=10.1111/j.1399-0039.2005.00389.x; RA Cordovado S.K., Hancock L.N., Simone A.E., Hendrix M., Mueller P.W.; RT "High-resolution genotyping of HLA-DQA1 in the GoKinD study and RT identification of novel alleles HLA-DQA1*040102, HLA-DQA1*0402 and HLA- RT DQA1*0404."; RL Tissue Antigens 65:448-458(2005). RN [23] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-203 (ALLELE DQA1*06:02). RA Simone A.E., Cordovado S.K., Hendrix M.M., Mueller P.W.; RT "Identification of a novel HLA-DQA1*06 allele detected by sequence-based RT typing."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-203 (ALLELE DQA1*01:07). RA Hancock L.N., Cordovado S.K., Mueller P.W.; RT "Identification of a novel HLA-DQA1*01 allele detected by sequence-based RT typing."; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [25] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-110 (ALLELE DQA1*01:02), AND RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-109 (ALLELE DQA1*05:01). RX PubMed=3372263; DOI=10.1016/0198-8859(88)90034-1; RA Horn G.T., Bugawan T.L., Long C.M., Manos M.M., Erlich H.A.; RT "Sequence analysis of HLA class II genes from insulin-dependent diabetic RT individuals."; RL Hum. Immunol. 21:249-263(1988). RN [26] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-109 (ALLELE DQA1*05:04). RA Trejaut J.A., Greville W.D., Dunckley H.; RT "DQA1 subtyping in Australian Aborigines. Additional evidence for RT heterogeneity."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [27] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-109 (ALLELE DQA1*01:06). RX PubMed=10395113; DOI=10.1034/j.1399-0039.1999.530613.x; RA Luo M., Blanchard J., Maclean I., Brunham R.; RT "Identification of a novel HLA-DQA1 allele (DQA1*0106) by sequence-based RT DQA1 typing."; RL Tissue Antigens 53:595-596(1999). RN [28] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-74 (ALLELE DQA1*05:02). RX PubMed=1362295; DOI=10.1111/j.1399-0039.1992.tb02050.x; RA Marsh S.G., Bodomer J.G.; RT "HLA class II nucleotide sequences, 1992."; RL Tissue Antigens 40:229-243(1992). RN [29] RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-254 (ALLELE DQA1*05:01). RX PubMed=3129499; RA Liu C.P., Bach F.H., Wu S.K.; RT "Molecular studies of a rare DR2/LD-5a/DQw3 HLA class II haplotype. RT Multiple genetic mechanisms in the generation of polymorphic HLA class II RT genes."; RL J. Immunol. 140:3631-3639(1988). RN [30] RP ERRATUM OF PUBMED:3129499. RA Liu C.P., Bach F.H., Wu S.K.; RL J. Immunol. 144:15441-15441(1990). RN [31] RP NUCLEOTIDE SEQUENCE [MRNA] OF 40-254 (ALLELE DQA1*03:01). RX PubMed=6815651; DOI=10.1073/pnas.79.20.6337; RA Auffray C., Korman A.J., Roux-Dosseto M., Bono R., Strominger J.L.; RT "cDNA clone for the heavy chain of the human B cell alloantigen DC1: strong RT sequence homology to the HLA-DR heavy chain."; RL Proc. Natl. Acad. Sci. U.S.A. 79:6337-6341(1982). RN [32] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-102 (ALLELE DQA1*05:01), AND RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-103 (ALLELE DQA1*01:02). RX PubMed=2513578; DOI=10.1073/pnas.86.24.9986; RA Gyllensten U.B., Erlich H.A.; RT "Ancient roots for polymorphism at the HLA-DQ alpha locus in primates."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9986-9990(1989). RN [33] RP NUCLEOTIDE SEQUENCE [MRNA] OF 119-254 (ALLELE DQA1*01:02). RX PubMed=2888727; DOI=10.1007/bf00346523; RA Turco E., Care A., Compagnone-Post P., Robinson C., Cascino I., Trucco M.; RT "Allelic forms of the alpha- and beta-chain genes encoding DQw1-positive RT heterodimers."; RL Immunogenetics 26:282-290(1987). RN [34] RP REVIEW. RX PubMed=8598037; DOI=10.1016/s0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [35] RP REVIEW. RX PubMed=11684289; DOI=10.1016/s0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most out RT of them."; RL Mol. Immunol. 38:329-346(2001). RN [36] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [37] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen presentation."; RL EMBO J. 27:1-5(2008). RN [38] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [39] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 27-207 OF HLA-DQA1/HLA-DQB1 RP HETERODIMER IN COMPLEX WITH INS PEPTIDE, SUBUNIT, GLYCOSYLATION AT ASN-103, RP AND DISULFIDE BOND. RX PubMed=11376336; DOI=10.1038/88694; RA Lee K.H., Wucherpfennig K.W., Wiley D.C.; RT "Structure of a human insulin peptide-HLA-DQ8 complex and susceptibility to RT type 1 diabetes."; RL Nat. Immunol. 2:501-507(2001). RN [41] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-219 OF HLA-DQA1/HLA-DQB1 RP HETERODIMER (HLA-DQ0602) IN COMPLEX WITH HCRT PEPTIDE, POLYMORPHISM, RP SUBUNIT, AND DISULFIDE BOND. RX PubMed=14769912; DOI=10.1073/pnas.0308458100; RA Siebold C., Hansen B.E., Wyer J.R., Harlos K., Esnouf R.E., Svejgaard A., RA Bell J.I., Strominger J.L., Jones E.Y., Fugger L.; RT "Crystal structure of HLA-DQ0602 that protects against type 1 diabetes and RT confers strong susceptibility to narcolepsy."; RL Proc. Natl. Acad. Sci. U.S.A. 101:1999-2004(2004). RN [42] RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 24-216 OF HLA-DQA1/HLA-DQB1 RP HETERODIMER (DQ2) IN COMPLEX WITH TRITICUM AESTIVUM ALPHA/BETA-GLIADIN RP PEPTIDE, SUBUNIT, AND POLYMORPHISM. RX PubMed=15020763; DOI=10.1073/pnas.0306885101; RA Kim C.Y., Quarsten H., Bergseng E., Khosla C., Sollid L.M.; RT "Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in RT celiac disease."; RL Proc. Natl. Acad. Sci. U.S.A. 101:4175-4179(2004). RN [43] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 24-206 OF HLA-DQA1/HLA-DQB1 RP HETERODIMER IN COMPLEX WITH TRITICUM AESTIVUM ALPHA/BETA-GLIADIN, SUBUNIT, RP AND DISULFIDE BOND. RX PubMed=17629515; DOI=10.1016/j.immuni.2007.05.015; RA Henderson K.N., Tye-Din J.A., Reid H.H., Chen Z., Borg N.A., Beissbarth T., RA Tatham A., Mannering S.I., Purcell A.W., Dudek N.L., van Heel D.A., RA McCluskey J., Rossjohn J., Anderson R.P.; RT "A structural and immunological basis for the role of human leukocyte RT antigen DQ8 in celiac disease."; RL Immunity 27:23-34(2007). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents them on CC the cell surface for recognition by the CD4 T-cells. The peptide CC binding cleft accommodates peptides of 10-30 residues. The peptides CC presented by MHC class II molecules are generated mostly by degradation CC of proteins that access the endocytic route, where they are processed CC by lysosomal proteases and other hydrolases. Exogenous antigens that CC have been endocytosed by the APC are thus readily available for CC presentation via MHC II molecules, and for this reason this antigen CC presentation pathway is usually referred to as exogenous. As membrane CC proteins on their way to degradation in lysosomes as part of their CC normal turn-over are also contained in the endosomal/lysosomal CC compartments, exogenous antigens must compete with those derived from CC endogenous components. Autophagy is also a source of endogenous CC peptides, autophagosomes constitutively fuse with MHC class II loading CC compartments. In addition to APCs, other cells of the gastrointestinal CC tract, such as epithelial cells, express MHC class II molecules and CC CD74 and act as APCs, which is an unusual trait of the GI tract. To CC produce a MHC class II molecule that presents an antigen, three MHC CC class II molecules (heterodimers of an alpha and a beta chain) CC associate with a CD74 trimer in the ER to form a heterononamer. Soon CC after the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving a CC small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM CC stabilizes MHC class II molecules until primary high affinity antigenic CC peptides are bound. The MHC II molecule bound to a peptide is then CC transported to the cell membrane surface. In B-cells, the interaction CC between HLA-DM and MHC class II molecules is regulated by HLA-DO. CC Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal CC microenvironment has been implicated in the regulation of antigen CC loading into MHC II molecules, increased acidification produces CC increased proteolysis and efficient peptide loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred as CC MHC class II molecule. In the endoplasmic reticulum (ER) it forms a CC heterononamer; 3 MHC class II molecules bind to a CD74 homotrimer (also CC known as invariant chain or HLA class II histocompatibility antigen CC gamma chain). In the endosomal/lysosomal system; CD74 undergoes CC sequential degradation by various proteases; leaving a small fragment CC termed CLIP on each MHC class II molecule. MHC class II molecule CC interacts with HLA_DM, and HLA_DO in B-cells, in order to release CLIP CC and facilitate the binding of antigenic peptides. CC {ECO:0000269|PubMed:11376336, ECO:0000269|PubMed:14769912, CC ECO:0000269|PubMed:15020763, ECO:0000269|PubMed:17629515}. CC -!- INTERACTION: CC P01909; P01920: HLA-DQB1; NbExp=8; IntAct=EBI-713389, EBI-1038012; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I membrane CC protein. Golgi apparatus, trans-Golgi network membrane; Single-pass CC type I membrane protein. Endosome membrane; Single-pass type I membrane CC protein. Lysosome membrane; Single-pass type I membrane protein. CC Note=The MHC class II complex transits through a number of CC intracellular compartments in the endocytic pathway until it reaches CC the cell membrane for antigen presentation. CC -!- POLYMORPHISM: The following alleles of DQA1 are known: DQA1*01:01, CC DQA1*01:02, DQA1*01:03, DQA1*01:04, DQA1*01:05, DQA1*01:06, DQA1*01:07, CC DQA1*02:01, DQA1*03:01, DQA1*03:02, DQA1*03:03, DQA1*04:01, DQA1*04:02, CC DQA1*04:03, DQA1*04:04, DQA1*05:01, DQA1*05:02, DQA1*05:03, DQA1*05:04, CC DQA1*05:05, DQA1*05:06, DQA1*05:07, DQA1*05:08, DQA1*05:09, DQA1*06:01, CC DQA1*06:02. The sequence shown is that of DQA1*05:01. CC -!- POLYMORPHISM: DQ2 (heterodimer of DQA1*05:01/DQB1*02:01) is associated CC with more than 90% of celiac disease patients. A minority displays DQ8 CC (heterodimer of DQA1*03/DQB1*03:02). DQ0602 (heterodimer of CC DQA1*01:02/DQB1*06:02) confers dominant protection against type 1 CC diabetes (T1D) and strong susceptibility to narcolepsy. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD56720.1; Type=Erroneous gene model prediction; Evidence={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; X00033; CAA24917.1; -; mRNA. DR EMBL; X00370; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; X00452; CAA25141.1; -; mRNA. DR EMBL; M16995; AAA59760.1; -; mRNA. DR EMBL; U92032; AAB91990.1; -; Genomic_DNA. DR EMBL; AY663395; AAU87978.1; -; Genomic_DNA. DR EMBL; AY663398; AAU87987.1; -; Genomic_DNA. DR EMBL; AY663400; AAU87992.1; -; Genomic_DNA. DR EMBL; AY663406; AAU88007.1; -; Genomic_DNA. DR EMBL; AY663411; AAU88022.1; -; Genomic_DNA. DR EMBL; AY663413; AAU88028.1; -; Genomic_DNA. DR EMBL; DQ178403; ABA86855.1; -; Genomic_DNA. DR EMBL; DQ178400; ABA86855.1; JOINED; Genomic_DNA. DR EMBL; DQ178401; ABA86855.1; JOINED; Genomic_DNA. DR EMBL; DQ178402; ABA86855.1; JOINED; Genomic_DNA. DR EMBL; DQ178407; ABA86856.1; -; Genomic_DNA. DR EMBL; DQ178404; ABA86856.1; JOINED; Genomic_DNA. DR EMBL; DQ178405; ABA86856.1; JOINED; Genomic_DNA. DR EMBL; DQ178406; ABA86856.1; JOINED; Genomic_DNA. DR EMBL; DQ178411; ABA86857.1; -; Genomic_DNA. DR EMBL; DQ178408; ABA86857.1; JOINED; Genomic_DNA. DR EMBL; DQ178409; ABA86857.1; JOINED; Genomic_DNA. DR EMBL; DQ178410; ABA86857.1; JOINED; Genomic_DNA. DR EMBL; DQ178415; ABA86858.1; -; Genomic_DNA. DR EMBL; DQ178412; ABA86858.1; JOINED; Genomic_DNA. DR EMBL; DQ178413; ABA86858.1; JOINED; Genomic_DNA. DR EMBL; DQ178414; ABA86858.1; JOINED; Genomic_DNA. DR EMBL; M29616; AAA59759.1; -; Genomic_DNA. DR EMBL; M29613; AAA59759.1; JOINED; Genomic_DNA. DR EMBL; AF322870; AAK11577.1; -; Genomic_DNA. DR EMBL; AF322867; AAK11577.1; JOINED; Genomic_DNA. DR EMBL; AF322868; AAK11577.1; JOINED; Genomic_DNA. DR EMBL; AF322869; AAK11577.1; JOINED; Genomic_DNA. DR EMBL; AF395700; AAM69677.1; -; Genomic_DNA. DR EMBL; AF395697; AAM69677.1; JOINED; Genomic_DNA. DR EMBL; AF395698; AAM69677.1; JOINED; Genomic_DNA. DR EMBL; AF395699; AAM69677.1; JOINED; Genomic_DNA. DR EMBL; CR450297; CAG29293.1; -; mRNA. DR EMBL; AM042559; CAJ14960.1; -; Genomic_DNA. DR EMBL; AM042560; CAJ14961.1; -; Genomic_DNA. DR EMBL; AK313975; BAG36689.1; -; mRNA. DR EMBL; BX248406; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL662789; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z84489; CAB06491.1; -; Genomic_DNA. DR EMBL; BC008585; AAH08585.1; -; mRNA. DR EMBL; BC157865; AAI57866.1; -; mRNA. DR EMBL; L46875; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; L46876; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; L46877; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; L46878; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; L46880; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; L46881; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M11124; AAA59754.1; -; mRNA. DR EMBL; M20431; AAA59758.1; -; mRNA. DR EMBL; L34082; AAC41950.1; -; mRNA. DR EMBL; L34085; AAC41953.1; -; mRNA. DR EMBL; L34086; AAC41954.1; -; mRNA. DR EMBL; L34089; AAC41957.1; -; mRNA. DR EMBL; L34090; AAC41958.1; -; mRNA. DR EMBL; L34092; AAC41960.1; -; mRNA. DR EMBL; L34093; AAC41961.1; -; mRNA. DR EMBL; L34094; AAC41962.1; -; mRNA. DR EMBL; L42625; AAA85334.1; -; mRNA. DR EMBL; AY197775; AAO45622.1; -; Genomic_DNA. DR EMBL; AY547314; AAS49496.1; -; Genomic_DNA. DR EMBL; AY206406; AAO47362.1; -; Genomic_DNA. DR EMBL; AY585236; AAT09985.1; -; Genomic_DNA. DR EMBL; M34997; AAA35772.1; -; Genomic_DNA. DR EMBL; M34999; AAA74633.1; -; Genomic_DNA. DR EMBL; U85035; AAB41891.1; -; Genomic_DNA. DR EMBL; AF109734; AAD56720.1; ALT_SEQ; Genomic_DNA. DR EMBL; U03675; AAB60341.1; -; Genomic_DNA. DR EMBL; M20506; AAA59774.1; -; mRNA. DR EMBL; J00199; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M17846; AAA59707.1; -; mRNA. DR PIR; A02211; HLHUD1. DR PIR; A02213; HLHUDQ. DR PIR; A02214; HLHUD7. DR PIR; A02215; HLHU3C. DR PIR; A93326; HLHUDC. DR PIR; B27628; B27628. DR PIR; D34512; D34512. DR RefSeq; NP_002113.2; NM_002122.3. DR PDB; 1JK8; X-ray; 2.40 A; A=27-206. DR PDB; 1S9V; X-ray; 2.22 A; A/D=24-216. DR PDB; 1UVQ; X-ray; 1.80 A; A=24-218. DR PDB; 2NNA; X-ray; 2.10 A; A=24-206. DR PDB; 4GG6; X-ray; 3.20 A; A/C=24-206. DR PDB; 4OZF; X-ray; 2.70 A; A=24-206. DR PDB; 4OZG; X-ray; 3.00 A; A/C=24-206. DR PDB; 4OZH; X-ray; 2.80 A; A/C=24-206. DR PDB; 4OZI; X-ray; 3.20 A; A/C=24-206. DR PDB; 5KSA; X-ray; 2.00 A; A=24-206. DR PDB; 5KSB; X-ray; 2.90 A; A/C=24-206. DR PDB; 5KSU; X-ray; 2.73 A; A/D=24-216. DR PDB; 5KSV; X-ray; 2.19 A; A=24-216. DR PDB; 6MFF; X-ray; 2.60 A; A=24-206. DR PDB; 6MFG; X-ray; 2.00 A; A/C=24-206. DR PDB; 6U3M; X-ray; 1.90 A; A/C=24-206. DR PDB; 6U3N; X-ray; 2.80 A; A=24-206. DR PDB; 6XP6; X-ray; 2.40 A; A/D=24-206. DR PDB; 7SG0; X-ray; 3.00 A; A=24-206. DR PDB; 7SG1; X-ray; 3.10 A; A/F=24-206. DR PDB; 7SG2; X-ray; 3.10 A; A/F=24-206. DR PDB; 8W83; X-ray; 2.82 A; C/G/K/O=24-206. DR PDB; 8W84; X-ray; 2.10 A; C=24-206. DR PDB; 8W85; X-ray; 2.77 A; C/G=24-206. DR PDB; 8W86; X-ray; 2.24 A; C/G=24-206. DR PDBsum; 1JK8; -. DR PDBsum; 1S9V; -. DR PDBsum; 1UVQ; -. DR PDBsum; 2NNA; -. DR PDBsum; 4GG6; -. DR PDBsum; 4OZF; -. DR PDBsum; 4OZG; -. DR PDBsum; 4OZH; -. DR PDBsum; 4OZI; -. DR PDBsum; 5KSA; -. DR PDBsum; 5KSB; -. DR PDBsum; 5KSU; -. DR PDBsum; 5KSV; -. DR PDBsum; 6MFF; -. DR PDBsum; 6MFG; -. DR PDBsum; 6U3M; -. DR PDBsum; 6U3N; -. DR PDBsum; 6XP6; -. DR PDBsum; 7SG0; -. DR PDBsum; 7SG1; -. DR PDBsum; 7SG2; -. DR PDBsum; 8W83; -. DR PDBsum; 8W84; -. DR PDBsum; 8W85; -. DR PDBsum; 8W86; -. DR AlphaFoldDB; P01909; -. DR SMR; P01909; -. DR BioGRID; 109362; 154. DR BioGRID; 1529240; 5. DR IntAct; P01909; 12. DR MINT; P01909; -. DR ChEMBL; CHEMBL4105884; -. DR TCDB; 9.A.75.1.1; the mhc ii receptor (mhc2r) family. DR GlyConnect; 1986; 2 N-Linked glycans (1 site). DR GlyCosmos; P01909; 2 sites, 2 glycans. DR GlyGen; P01909; 4 sites, 2 N-linked glycans (1 site). DR iPTMnet; P01909; -. DR BioMuta; HLA-DQA1; -. DR DMDM; 122188; -. DR jPOST; P01909; -. DR MassIVE; P01909; -. DR PeptideAtlas; P01909; -. DR ProteomicsDB; 51510; -. DR ABCD; P01909; 24 sequenced antibodies. DR Antibodypedia; 2728; 748 antibodies from 38 providers. DR CPTC; P01909; 2 antibodies. DR DNASU; 3117; -. DR Ensembl; ENST00000343139.11; ENSP00000339398.5; ENSG00000196735.13. DR Ensembl; ENST00000374949.2; ENSP00000364087.2; ENSG00000196735.13. DR Ensembl; ENST00000383251.6; ENSP00000372738.2; ENSG00000206305.12. DR Ensembl; ENST00000395363.5; ENSP00000378767.1; ENSG00000196735.13. DR Ensembl; ENST00000399675.5; ENSP00000382583.1; ENSG00000206305.12. DR Ensembl; ENST00000399678.5; ENSP00000382586.1; ENSG00000206305.12. DR Ensembl; ENST00000418023.5; ENSP00000387892.1; ENSG00000232062.9. DR Ensembl; ENST00000444296.6; ENSP00000413237.2; ENSG00000232062.9. DR GeneID; 3117; -. DR KEGG; hsa:3117; -. DR MANE-Select; ENST00000343139.11; ENSP00000339398.5; NM_002122.5; NP_002113.2. DR UCSC; uc003obr.4; human. DR AGR; HGNC:4942; -. DR CTD; 3117; -. DR DisGeNET; 3117; -. DR GeneCards; HLA-DQA1; -. DR GeneReviews; HLA-DQA1; -. DR HGNC; HGNC:4942; HLA-DQA1. DR HPA; ENSG00000196735; Tissue enhanced (lung, lymphoid tissue). DR MalaCards; HLA-DQA1; -. DR MIM; 146880; gene. DR neXtProt; NX_P01909; -. DR NIAGADS; ENSG00000196735; -. DR Orphanet; 391490; Adult-onset myasthenia gravis. DR Orphanet; 930; Idiopathic achalasia. DR Orphanet; 555; NON RARE IN EUROPE: Celiac disease. DR Orphanet; 243377; NON RARE IN EUROPE: Diabetes mellitus type 1. DR PharmGKB; PA35066; -. DR VEuPathDB; HostDB:ENSG00000196735; -. DR HOGENOM; CLU_069380_0_0_1; -. DR InParanoid; P01909; -. DR OrthoDB; 4118190at2759; -. DR PhylomeDB; P01909; -. DR TreeFam; TF333797; -. DR PathwayCommons; P01909; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SignaLink; P01909; -. DR SIGNOR; P01909; -. DR BioGRID-ORCS; 3117; 7 hits in 1073 CRISPR screens. DR ChiTaRS; HLA-DQA1; human. DR EvolutionaryTrace; P01909; -. DR GenomeRNAi; 3117; -. DR Pharos; P01909; Tbio. DR PRO; PR:P01909; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P01909; Protein. DR Bgee; ENSG00000196735; Expressed in gall bladder and 162 other cell types or tissues. DR ExpressionAtlas; P01909; baseline and differential. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; ISS:CAFA. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central. DR GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; ISS:CAFA. 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; IBA:GO_Central. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central. 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 CDD; cd21008; IgC1_MHC_II_alpha_HLA-DQ; 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; IPR001003; MHC_II_a_N. DR PANTHER; PTHR19944:SF59; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DQ ALPHA 1 CHAIN; 1. DR PANTHER; PTHR19944; MHC CLASS II-RELATED; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00993; MHC_II_alpha; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00920; MHC_II_alpha; 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 Genevisible; P01909; HS. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Cell membrane; Direct protein sequencing; KW Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein; KW Golgi apparatus; Immunity; Lysosome; Membrane; MHC II; Reference proteome; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..23 FT /evidence="ECO:0000269|PubMed:6576979" FT CHAIN 24..254 FT /note="HLA class II histocompatibility antigen, DQ alpha 1 FT chain" FT /id="PRO_0000018970" FT TOPO_DOM 24..216 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 217..239 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 240..254 FT /note="Cytoplasmic" FT DOMAIN 112..204 FT /note="Ig-like C1-type" FT REGION 24..119 FT /note="Alpha-1" FT REGION 120..203 FT /note="Alpha-2" FT REGION 204..216 FT /note="Connecting peptide" FT CARBOHYD 103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 143 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 132..188 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:11376336, ECO:0000269|PubMed:14769912, FT ECO:0000269|PubMed:17629515" FT VARIANT 8 FT /note="M -> L (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*04:01 and allele DQA1*06:01; dbSNP:rs1047989)" FT /id="VAR_033399" FT VARIANT 11 FT /note="A -> T (in allele DQA1*05:05, allele DQA1*05:08 and FT allele DQA1*05:09; dbSNP:rs1047992)" FT /id="VAR_033400" FT VARIANT 17 FT /note="V -> M (in allele DQA1*01:04 and allele DQA1*01:05; FT dbSNP:rs12722039)" FT /id="VAR_050380" FT VARIANT 18 FT /note="M -> T (in allele DQA1*03:03; dbSNP:rs11545686)" FT /id="VAR_050381" FT VARIANT 24 FT /note="E -> K (in allele DQA1*05:09; dbSNP:rs41545012)" FT /id="VAR_060493" FT VARIANT 25 FT /note="D -> G (in allele DQA1*01:04 and allele DQA1*01:05; FT dbSNP:rs12722042)" FT /id="VAR_050382" FT VARIANT 34 FT /note="Y -> C (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; dbSNP:rs1129740)" FT /id="VAR_060494" FT VARIANT 41 FT /note="S -> F (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; dbSNP:rs1071630)" FT /id="VAR_033401" FT VARIANT 44 FT /note="P -> L (in allele DQA1*05:04; dbSNP:rs41549715)" FT /id="VAR_060495" FT VARIANT 48 FT /note="Y -> F (in allele DQA1*02:01, allele DQA1*01:03, FT allele DQA1*06:01 and allele DQA1*06:02; dbSNP:rs12722051)" FT /id="VAR_033402" FT VARIANT 49 FT /note="T -> S (in allele DQA1*03:01, allele DQA1*03:02 and FT allele DQA1*03:03; dbSNP:rs1048023)" FT /id="VAR_033403" FT VARIANT 57 FT /note="Q -> E (in allele DQA1*01:01, allele DQA1*01:04, FT allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, FT allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03; FT dbSNP:rs10093)" FT /id="VAR_014604" FT VARIANT 63 FT /note="G -> E (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06, allele DQA1*01:07, allele DQA1*02:01, FT allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03; FT dbSNP:rs1142323)" FT /id="VAR_060496" FT VARIANT 64 FT /note="R -> K (in allele DQA1*01:03; dbSNP:rs36219699)" FT /id="VAR_050383" FT VARIANT 67 FT /note="T -> A (in allele DQA1*01:06; dbSNP:rs41543221)" FT /id="VAR_060497" FT VARIANT 68 FT /note="V -> A (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; dbSNP:rs1142324)" FT /id="VAR_060498" FT VARIANT 70 FT /note="C -> K (in allele DQA1*02:01; requires 2 nucleotide FT substitutions)" FT /id="VAR_060499" FT VARIANT 70 FT /note="C -> Q (in allele DQA1*03:01, allele DQA1*03:02 and FT allele DQA1*03:03; requires 2 nucleotide substitutions)" FT /id="VAR_060500" FT VARIANT 70 FT /note="C -> R (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; dbSNP:rs1142326)" FT /id="VAR_060501" FT VARIANT 70 FT /note="C -> Y (in dbSNP:rs3207983)" FT /id="VAR_033404" FT VARIANT 71 FT /note="L -> W (in allele DQA1*01:01, allele FT DQA1*01:02,allele DQA1*01:03, allele DQA1*01:04, allele FT DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07; FT dbSNP:rs1142328)" FT /id="VAR_060502" FT VARIANT 73 FT /note="V -> D (in dbSNP:rs760671632)" FT /id="VAR_033406" FT VARIANT 73 FT /note="V -> E (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; dbSNP:rs3208105)" FT /id="VAR_060503" FT VARIANT 73 FT /note="V -> L (in allele DQA1*02:01, allele DQA1*03:01, FT allele DQA1*03:02 and allele DQA1*03:03; dbSNP:rs12722061)" FT /id="VAR_033405" FT VARIANT 74 FT /note="L -> F (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06, allele DQA1*01:07, allele DQA1*02:01, FT allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03; FT dbSNP:rs9272698)" FT /id="VAR_060504" FT VARIANT 75 FT /note="R -> H (in allele DQA1*02:01; dbSNP:rs28383449)" FT /id="VAR_060505" FT VARIANT 75 FT /note="R -> S (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; dbSNP:rs9272699)" FT /id="VAR_060506" FT VARIANT 76 FT /note="Q -> K (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; dbSNP:rs1048052)" FT /id="VAR_060507" FT VARIANT 76 FT /note="Q -> R (in allele DQA1*02:01, allele DQA1*03:01, FT allele DQA1*03:02 and allele DQA1*03:03; dbSNP:rs12722069)" FT /id="VAR_060508" FT VARIANT 77 FT /note="F -> L (in allele DQA1*02:01; dbSNP:rs3188043)" FT /id="VAR_060509" FT VARIANT 78 FT /note="R -> GG (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele FT DQA1*01:05,allele DQA1*01:06 and allele DQA1*01:07; FT dbSNP:rs4193)" FT /id="VAR_060510" FT VARIANT 78 FT /note="R -> RR (in allele DQA1*03:01, allele DQA1*03:02 and FT allele DQA1*03:03)" FT /id="VAR_060511" FT VARIANT 81 FT /note="P -> R (in allele DQA1*05:02; dbSNP:rs41541412)" FT /id="VAR_060512" FT VARIANT 83 FT /note="F -> G (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; requires 2 FT nucleotide substitutions)" FT /id="VAR_060513" FT VARIANT 86 FT /note="T -> R (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; dbSNP:rs1142333)" FT /id="VAR_033408" FT VARIANT 88 FT /note="I -> M (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; dbSNP:rs1142334)" FT /id="VAR_033409" FT VARIANT 91 FT /note="L -> A (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; requires 2 FT nucleotide substitutions)" FT /id="VAR_060514" FT VARIANT 91 FT /note="L -> T (in allele DQA1*04:01, allele DQA1*04:02, FT allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02; FT requires 2 nucleotide substitutions)" FT /id="VAR_060515" FT VARIANT 97 FT /note="S -> I (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06, allele DQA1*01:07, allele DQA1*02:01, FT allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, FT allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, FT allele DQA1*06:01 and allele DQA1*06:02; dbSNP:rs9279910)" FT /id="VAR_060516" FT VARIANT 98 FT /note="L -> M (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; dbSNP:rs1064944)" FT /id="VAR_060517" FT VARIANT 98 FT /note="L -> V (in allele DQA1*03:01, allele DQA1*03:02 and FT allele DQA1*03:03; dbSNP:rs1064944)" FT /id="VAR_060518" FT VARIANT 101 FT /note="R -> C (in allele DQA1*01:07; dbSNP:rs41542116)" FT /id="VAR_060519" FT VARIANT 102 FT /note="S -> Y (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:06 and allele DQA1*01:07; dbSNP:rs1129808)" FT /id="VAR_050384" FT VARIANT 124 FT /note="L -> V (in allele DQA1*05:06; dbSNP:rs41555012)" FT /id="VAR_060520" FT VARIANT 129 FT /note="I -> T (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, FT allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, FT allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and FT allele DQA1*06:02; dbSNP:rs707952)" FT /id="VAR_050385" FT VARIANT 151 FT /note="H -> Q (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:04, allele DQA1*01:05 and allele DQA1*01:07; FT dbSNP:rs707950)" FT /id="VAR_050386" FT VARIANT 152 FT /note="S -> A (in allele DQA1*01:03; dbSNP:rs41547417)" FT /id="VAR_060521" FT VARIANT 160 FT /note="T -> I (in allele DQA1*04:02; dbSNP:rs41545514)" FT /id="VAR_060522" FT VARIANT 161 FT /note="S -> I (in allele DQA1*05:08; dbSNP:rs41544114)" FT /id="VAR_060524" FT VARIANT 161 FT /note="S -> R (in allele DQA1*06:02; dbSNP:rs41552014)" FT /id="VAR_060523" FT VARIANT 175 FT /note="Y -> H (in allele DQA1*04:04; dbSNP:rs41550317)" FT /id="VAR_060525" FT VARIANT 178 FT /note="L -> F (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, FT allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, FT allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and FT allele DQA1*06:02; dbSNP:rs707949)" FT /id="VAR_060526" FT VARIANT 182 FT /note="A -> D (in allele DQA1*03:02 and allele DQA1*03:03; FT dbSNP:rs7990)" FT /id="VAR_060527" FT VARIANT 182 FT /note="A -> S (in allele DQA1*05:03, allele DQA1*05:06 and FT allele DQA1*05:07; dbSNP:rs41561312)" FT /id="VAR_060528" FT VARIANT 183 FT /note="E -> D (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, FT allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, FT allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and FT allele DQA1*06:02; dbSNP:rs707963)" FT /id="VAR_060529" FT VARIANT 185 FT /note="S -> I (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, FT allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, FT allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, FT allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and FT allele DQA1*06:02; dbSNP:rs707962)" FT /id="VAR_060530" FT VARIANT 197 FT /note="K -> E (in allele DQA1*02:01, allele DQA1*03:01, FT allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, FT allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and FT allele DQA1*06:02; dbSNP:rs2308891)" FT /id="VAR_060531" FT VARIANT 197 FT /note="K -> Q (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05 and FT allele DQA1*01:07; dbSNP:rs2308891)" FT /id="VAR_060532" FT VARIANT 209 FT /note="A -> T (in allele DQA1*03:01, allele DQA1*03:02 and FT allele DQA1*03:03; dbSNP:rs9272785)" FT /id="VAR_050387" FT VARIANT 221 FT /note="A -> T (in allele DQA1*01:04; dbSNP:rs35087390)" FT /id="VAR_050388" FT VARIANT 229 FT /note="V -> M (in allele DQA1*01:02; dbSNP:rs9260)" FT /id="VAR_033411" FT VARIANT 230 FT /note="G -> C (in allele DQA1*05:07; dbSNP:rs41545416)" FT /id="VAR_060533" FT VARIANT 237 FT /note="F -> L (in allele DQA1*02:01, allele DQA1*03:01, FT allele DQA1*03:02 and allele DQA1*03:03; dbSNP:rs1048430)" FT /id="VAR_033412" FT VARIANT 240 FT /note="R -> Q (in allele DQA1*01:01, allele DQA1*01:02, FT allele DQA1*01:03, allele DQA1*01:04 and allele DQA1*01:05; FT dbSNP:rs1048439)" FT /id="VAR_033413" FT CONFLICT 11 FT /note="A -> S (in Ref. 4; AAA59760)" FT /evidence="ECO:0000305" FT CONFLICT 23..27 FT /note="Missing (in Ref. 16; AAA59754)" FT /evidence="ECO:0000305" FT CONFLICT 91 FT /note="L -> H (in Ref. 4; AAA59760)" FT /evidence="ECO:0000305" FT CONFLICT 107 FT /note="A -> P (in Ref. 16; AAA59754)" FT /evidence="ECO:0000305" FT CONFLICT 156 FT /note="G -> D (in Ref. 3; CAA25141)" FT /evidence="ECO:0000305" FT CONFLICT 213 FT /note="E -> D (in Ref. 16; AAA59754)" FT /evidence="ECO:0000305" FT STRAND 29..40 FT /evidence="ECO:0007829|PDB:6U3M" FT TURN 41..44 FT /evidence="ECO:0007829|PDB:6U3M" FT STRAND 45..52 FT /evidence="ECO:0007829|PDB:6U3M" FT STRAND 55..61 FT /evidence="ECO:0007829|PDB:6U3M" FT TURN 62..65 FT /evidence="ECO:0007829|PDB:6U3M" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:6U3M" FT HELIX 72..76 FT /evidence="ECO:0007829|PDB:6U3M" FT HELIX 81..101 FT /evidence="ECO:0007829|PDB:6U3M" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:1JK8" FT STRAND 113..120 FT /evidence="ECO:0007829|PDB:6U3M" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:4OZF" FT STRAND 128..137 FT /evidence="ECO:0007829|PDB:6U3M" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:6U3M" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:6U3M" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:6U3M" FT STRAND 170..178 FT /evidence="ECO:0007829|PDB:6U3M" FT STRAND 186..191 FT /evidence="ECO:0007829|PDB:6U3M" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:6U3M" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:6U3M" SQ SEQUENCE 254 AA; 27805 MW; 84E12B5A80E2A028 CRC64; MILNKALMLG ALALTTVMSP CGGEDIVADH VASYGVNLYQ SYGPSGQYTH EFDGDEQFYV DLGRKETVWC LPVLRQFRFD PQFALTNIAV LKHNLNSLIK RSNSTAATNE VPEVTVFSKS PVTLGQPNIL ICLVDNIFPP VVNITWLSNG HSVTEGVSET SFLSKSDHSF FKISYLTLLP SAEESYDCKV EHWGLDKPLL KHWEPEIPAP MSELTETVVC ALGLSVGLVG IVVGTVFIIR GLRSVGASRH QGPL //