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HLA class II histocompatibility antigen, DQ alpha 1 chain (DC-1 alpha chain) (DC-alpha) (HLA-DCA) (MHC class II DQA1)

 DQA1_HUMAN              Reviewed;         254 AA.
P01909; O19630; O19706; P01907; P01908; P04225; P04226; P05536;
P79553; Q06751; Q29876; Q29994; Q2Q6Y6; Q2Q6Y7; Q2Q6Y8; Q2WCM3;
Q30064; Q30067; Q30068; Q30070; Q30071; Q30072; Q30073; Q30086;
Q30101; Q5Y7D5; Q5Y7F5; Q6ICU6; Q6PR46; Q6QDB1; Q860W2; Q860W4;
Q9BD37; Q9TPM3; Q9UM31;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
28-MAR-2018, entry version 176.
RecName: Full=HLA class II histocompatibility antigen, DQ alpha 1 chain;
AltName: Full=DC-1 alpha chain;
AltName: Full=DC-alpha;
AltName: Full=HLA-DCA;
AltName: Full=MHC class II DQA1;
Flags: Precursor;
Name=HLA-DQA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQA1*02:01).
PubMed=6415485; DOI=10.1038/305813a0;
Chang H.-C., Moriuchi T., Silver J.;
"The heavy chain of human B-cell alloantigen HLA-DS has a variable N-
terminal region and a constant immunoglobulin-like region.";
Nature 305:813-815(1983).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQA1*05:01).
PubMed=6585297;
Schenning L., Larhammar D., Bill P., Wiman K., Jonsson A.-K., Rask L.,
Peterson P.A.;
"Both alpha and beta chains of HLA-DC class II histocompatibility
antigens display extensive polymorphism in their amino-terminal
domains.";
EMBO J. 3:447-452(1984).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DQA1*01:02 AND ALLELE DQA1*03:01).
PubMed=6584734; DOI=10.1038/308327a0;
Auffray C., Lillie J.W., Arnot D., Grossberger D., Kappes D.,
Strominger J.L.;
"Isotypic and allotypic variation of human class II histocompatibility
antigen alpha-chain genes.";
Nature 308:327-333(1984).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQA1*05:01).
PubMed=3584986;
Schiffenbauer J., Didier D.K., Klearman M., Rice K., Shuman S.,
Tieber V.L., Kittlesen D.J., Schwartz B.D.;
"Complete sequence of the HLA DQ alpha and DQ beta cDNA from a
DR5/DQw3 cell line.";
J. Immunol. 139:228-233(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQA1*05:01).
PubMed=9271631; DOI=10.1007/s002510050295;
Ellis M.C., Hetisimer A.H., Ruddy D.A., Hansen S.L., Kronmal G.S.,
McClelland E., Quintana L., Drayna D.T., Aldrich M.S., Mignot E.;
"HLA class II haplotype and sequence analysis support a role for DQ in
narcolepsy.";
Immunogenetics 46:410-417(1997).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DQA1*01:01; DQA1*01:02 AND
DQA1*03:01).
PubMed=16140993; DOI=10.1101/gr.3554305;
Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S.,
Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.;
"Ancient haplotypes of the HLA Class II region.";
Genome Res. 15:1250-1257(2005).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DQA1*01:02; DQA1*05:06;
DQA1*05:07 AND DQA1*05:08).
PubMed=16866887; DOI=10.1111/j.1399-0039.2006.00645.x;
Lee K.W., Jung Y.A., Oh D.H.;
"Four novel human leukocyte antigen-DQA1 alleles identified in the
Korean population.";
Tissue Antigens 68:167-172(2006).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQA1*03:01).
PubMed=3036828;
Jonsson A.-K., Hyldig-Nielsen J.-J., Servenius B., Larhammar D.,
Andersson G., Joergensen F., Peterson P.A., Rask L.;
"Class II genes of the human major histocompatibility complex.
Comparisons of the DQ and DX alpha and beta genes.";
J. Biol. Chem. 262:8767-8777(1987).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQA1*01:01).
Ashdown M.L., Leas L., Gavrilidis A., Wood J.M., Simons M.J.;
"Identification of a novel DQA1 allele, DQA1*01012, and confirmatory
sequence of DQA1*01011.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DQA1*02:01).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DQA1*01:02 AND DQA1*05:09).
Voorter C.E., van den Berg-Loonen E.M.;
"New and confirmatory HLA sequences by SBT.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DQA1*01:01).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES DQA1*01:02;
DQA1*03:01 AND DQA1*05:01).
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DQA1*03:01 AND
DQA1*05:01).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-27 (ALLELES
DQA1*01:01/DQA1*01:02/DQA1*01:03; DQA1*01:04; DQA1*01:05;
DQA1*02:01/DQA1*03:01/DQA1*03:03; DQA1*04:01/DQA1*06:01 AND
DQA1*05:01/DQA1*05:03/DQA1*05:05).
TISSUE=B-cell;
Yasunaga S., Kimura A., Sasazuki T.;
"Sequence polymorphisms in HLA-DQA1 exon1.";
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 19-254 (ALLELE DQA1*03:02).
PubMed=3879967; DOI=10.1073/pnas.82.10.3420;
Moriuchi J., Moriuchi T., Silver J.;
"Nucleotide sequence of an HLA-DQ alpha chain derived from a DRw9 cell
line: genetic and evolutionary implications.";
Proc. Natl. Acad. Sci. U.S.A. 82:3420-3424(1985).
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 23-254 (ALLELE DQA1*01:02).
PubMed=3259543; DOI=10.1007/BF00364432;
Lock C.B., So A.K., Welsh K.I., Parkes J.D., Trowsdale J.;
"MHC class II sequences of an HLA-DR2 narcoleptic.";
Immunogenetics 27:449-455(1988).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 24-250 (ALLELE DQA1*03:02/DQA1*03:03)
AND NUCLEOTIDE SEQUENCE [MRNA] OF 24-249 (ALLELES DQA1*01:01;
DQA1*01:03; DQA1*01:04; DQA1*04:01; DQA1*05:03; DQA1*05:05 AND
DQA1*06:01).
PubMed=8929711; DOI=10.1111/j.1399-0039.1996.tb02512.x;
Yasunaga S., Kimura A., Hamaguchi K., Ronningen K.S., Sasazuki T.;
"Different contribution of HLA-DR and -DQ genes in susceptibility and
resistance to insulin-dependent diabetes mellitus (IDDM).";
Tissue Antigens 47:37-48(1996).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 24-249 (ALLELE DQA1*01:05).
Yasunaga S.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[20]
PROTEIN SEQUENCE OF 24-89; 102-120 AND 164-212 (ALLELE DQA1*01:02).
PubMed=6576979;
Goetz H., Kratzin H., Thinnes F.P., Yang C.-Y., Kruse T., Pauly E.,
Koelbel S., Egert G., Wernet P., Hilschmann N.;
"Primary structure of human class II histocompatibility antigens 3rd
communication. Amino acid sequence comparison between DR and DC
subclass antigens derived from a lymphoblastoid B cell line homozygous
at the HLA loci (HLA-A3,3; B7,7; Dw2,2; DR2,2: MT1,1; Dc1,1: MB1,1).";
Hoppe-Seyler's Z. Physiol. Chem. 364:749-755(1983).
[21]
NUCLEOTIDE SEQUENCE [MRNA] OF 24-209 (ALLELE DQA1*05:01).
PubMed=2493052;
Kao H.T., Gregersen P.K., Tang J.C., Takahashi T., Wang C.Y.,
Silver J.;
"Molecular analysis of the HLA class II genes in two DRw6-related
haplotypes, DRw13 DQw1 and DRw14 DQw3.";
J. Immunol. 142:1743-1747(1989).
[22]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-203 (ALLELES DQA1*04:02 AND
DQA1*04:04).
PubMed=15853899; DOI=10.1111/j.1399-0039.2005.00389.x;
Cordovado S.K., Hancock L.N., Simone A.E., Hendrix M., Mueller P.W.;
"High-resolution genotyping of HLA-DQA1 in the GoKinD study and
identification of novel alleles HLA-DQA1*040102, HLA-DQA1*0402 and
HLA-DQA1*0404.";
Tissue Antigens 65:448-458(2005).
[23]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-203 (ALLELE DQA1*06:02).
Simone A.E., Cordovado S.K., Hendrix M.M., Mueller P.W.;
"Identification of a novel HLA-DQA1*06 allele detected by sequence-
based typing.";
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[24]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-203 (ALLELE DQA1*01:07).
Hancock L.N., Cordovado S.K., Mueller P.W.;
"Identification of a novel HLA-DQA1*01 allele detected by sequence-
based typing.";
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[25]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-110 (ALLELE DQA1*01:02), AND
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-109 (ALLELE DQA1*05:01).
PubMed=3372263; DOI=10.1016/0198-8859(88)90034-1;
Horn G.T., Bugawan T.L., Long C.M., Manos M.M., Erlich H.A.;
"Sequence analysis of HLA class II genes from insulin-dependent
diabetic individuals.";
Hum. Immunol. 21:249-263(1988).
[26]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-109 (ALLELE DQA1*05:04).
Trejaut J.A., Greville W.D., Dunckley H.;
"DQA1 subtyping in Australian Aborigines. Additional evidence for
heterogeneity.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[27]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-109 (ALLELE DQA1*01:06).
PubMed=10395113; DOI=10.1034/j.1399-0039.1999.530613.x;
Luo M., Blanchard J., Maclean I., Brunham R.;
"Identification of a novel HLA-DQA1 allele (DQA1*0106) by sequence-
based DQA1 typing.";
Tissue Antigens 53:595-596(1999).
[28]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-74 (ALLELE DQA1*05:02).
PubMed=1362295; DOI=10.1111/j.1399-0039.1992.tb02050.x;
Marsh S.G., Bodomer J.G.;
"HLA class II nucleotide sequences, 1992.";
Tissue Antigens 40:229-243(1992).
[29]
NUCLEOTIDE SEQUENCE [MRNA] OF 36-254 (ALLELE DQA1*05:01).
PubMed=3129499;
Liu C.P., Bach F.H., Wu S.K.;
"Molecular studies of a rare DR2/LD-5a/DQw3 HLA class II haplotype.
Multiple genetic mechanisms in the generation of polymorphic HLA class
II genes.";
J. Immunol. 140:3631-3639(1988).
[30]
ERRATUM.
Liu C.P., Bach F.H., Wu S.K.;
J. Immunol. 144:15441-15441(1990).
[31]
NUCLEOTIDE SEQUENCE [MRNA] OF 40-254 (ALLELE DQA1*03:01).
PubMed=6815651; DOI=10.1073/pnas.79.20.6337;
Auffray C., Korman A.J., Roux-Dosseto M., Bono R., Strominger J.L.;
"cDNA clone for the heavy chain of the human B cell alloantigen DC1:
strong sequence homology to the HLA-DR heavy chain.";
Proc. Natl. Acad. Sci. U.S.A. 79:6337-6341(1982).
[32]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-102 (ALLELE DQA1*05:01), AND
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-103 (ALLELE DQA1*01:02).
PubMed=2513578; DOI=10.1073/pnas.86.24.9986;
Gyllensten U.B., Erlich H.A.;
"Ancient roots for polymorphism at the HLA-DQ alpha locus in
primates.";
Proc. Natl. Acad. Sci. U.S.A. 86:9986-9990(1989).
[33]
NUCLEOTIDE SEQUENCE [MRNA] OF 119-254 (ALLELE DQA1*01:02).
PubMed=2888727; DOI=10.1007/BF00346523;
Turco E., Care A., Compagnone-Post P., Robinson C., Cascino I.,
Trucco M.;
"Allelic forms of the alpha- and beta-chain genes encoding DQw1-
positive heterodimers.";
Immunogenetics 26:282-290(1987).
[34]
REVIEW.
PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9;
Cresswell P.;
"Invariant chain structure and MHC class II function.";
Cell 84:505-507(1996).
[35]
REVIEW.
PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4;
Villadangos J.A.;
"Presentation of antigens by MHC class II molecules: getting the most
out of them.";
Mol. Immunol. 38:329-346(2001).
[36]
REVIEW.
PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005;
Menendez-Benito V., Neefjes J.;
"Autophagy in MHC class II presentation: sampling from within.";
Immunity 26:1-3(2007).
[37]
REVIEW.
PubMed=18046453; DOI=10.1038/sj.emboj.7601945;
Rocha N., Neefjes J.;
"MHC class II molecules on the move for successful antigen
presentation.";
EMBO J. 27:1-5(2008).
[38]
REVIEW.
PubMed=19092054; DOI=10.1242/jcs.035089;
Berger A.C., Roche P.A.;
"MHC class II transport at a glance.";
J. Cell Sci. 122:1-4(2009).
[39]
REVIEW.
PubMed=19533806; DOI=10.3748/wjg.15.2855;
Beswick E.J., Reyes V.E.;
"CD74 in antigen presentation, inflammation, and cancers of the
gastrointestinal tract.";
World J. Gastroenterol. 15:2855-2861(2009).
[40]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 27-207 OF HLA-DQA1/HLA-DQB1
HETERODIMER IN COMPLEX WITH INS PEPTIDE, SUBUNIT, GLYCOSYLATION AT
ASN-103, AND DISULFIDE BOND.
PubMed=11376336; DOI=10.1038/88694;
Lee K.H., Wucherpfennig K.W., Wiley D.C.;
"Structure of a human insulin peptide-HLA-DQ8 complex and
susceptibility to type 1 diabetes.";
Nat. Immunol. 2:501-507(2001).
[41]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-219 OF HLA-DQA1/HLA-DQB1
HETERODIMER (HLA-DQ0602) IN COMPLEX WITH HCRT PEPTIDE, POLYMORPHISM,
SUBUNIT, AND DISULFIDE BOND.
PubMed=14769912; DOI=10.1073/pnas.0308458100;
Siebold C., Hansen B.E., Wyer J.R., Harlos K., Esnouf R.E.,
Svejgaard A., Bell J.I., Strominger J.L., Jones E.Y., Fugger L.;
"Crystal structure of HLA-DQ0602 that protects against type 1 diabetes
and confers strong susceptibility to narcolepsy.";
Proc. Natl. Acad. Sci. U.S.A. 101:1999-2004(2004).
[42]
X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 24-216 OF HLA-DQA1/HLA-DQB1
HETERODIMER (DQ2) IN COMPLEX WITH TRITICUM AESTIVUM ALPHA/BETA-GLIADIN
PEPTIDE, SUBUNIT, AND POLYMORPHISM.
PubMed=15020763; DOI=10.1073/pnas.0306885101;
Kim C.Y., Quarsten H., Bergseng E., Khosla C., Sollid L.M.;
"Structural basis for HLA-DQ2-mediated presentation of gluten epitopes
in celiac disease.";
Proc. Natl. Acad. Sci. U.S.A. 101:4175-4179(2004).
[43]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 24-206 OF HLA-DQA1/HLA-DQB1
HETERODIMER IN COMPLEX WITH TRITICUM AESTIVUM ALPHA/BETA-GLIADIN,
SUBUNIT, AND DISULFIDE BOND.
PubMed=17629515; DOI=10.1016/j.immuni.2007.05.015;
Henderson K.N., Tye-Din J.A., Reid H.H., Chen Z., Borg N.A.,
Beissbarth T., Tatham A., Mannering S.I., Purcell A.W., Dudek N.L.,
van Heel D.A., McCluskey J., Rossjohn J., Anderson R.P.;
"A structural and immunological basis for the role of human leukocyte
antigen DQ8 in celiac disease.";
Immunity 27:23-34(2007).
-!- FUNCTION: Binds peptides derived from antigens that access the
endocytic route of antigen presenting cells (APC) and presents
them on the cell surface for recognition by the CD4 T-cells. The
peptide binding cleft accommodates peptides of 10-30 residues. The
peptides presented by MHC class II molecules are generated mostly
by degradation of proteins that access the endocytic route, where
they are processed by lysosomal proteases and other hydrolases.
Exogenous antigens that have been endocytosed by the APC are thus
readily available for presentation via MHC II molecules, and for
this reason this antigen presentation pathway is usually referred
to as exogenous. As membrane proteins on their way to degradation
in lysosomes as part of their normal turn-over are also contained
in the endosomal/lysosomal compartments, exogenous antigens must
compete with those derived from endogenous components. Autophagy
is also a source of endogenous peptides, autophagosomes
constitutively fuse with MHC class II loading compartments. In
addition to APCs, other cells of the gastrointestinal tract, such
as epithelial cells, express MHC class II molecules and CD74 and
act as APCs, which is an unusual trait of the GI tract. To produce
a MHC class II molecule that presents an antigen, three MHC class
II molecules (heterodimers of an alpha and a beta chain) associate
with a CD74 trimer in the ER to form a heterononamer. Soon after
the entry of this complex into the endosomal/lysosomal system
where antigen processing occurs, CD74 undergoes a sequential
degradation by various proteases, including CTSS and CTSL, leaving
a small fragment termed CLIP (class-II-associated invariant chain
peptide). The removal of CLIP is facilitated by HLA-DM via direct
binding to the alpha-beta-CLIP complex so that CLIP is released.
HLA-DM stabilizes MHC class II molecules until primary high
affinity antigenic peptides are bound. The MHC II molecule bound
to a peptide is then transported to the cell membrane surface. In
B-cells, the interaction between HLA-DM and MHC class II molecules
is regulated by HLA-DO. Primary dendritic cells (DCs) also to
express HLA-DO. Lysosomal microenvironment has been implicated in
the regulation of antigen loading into MHC II molecules, increased
acidification produces increased proteolysis and efficient peptide
loading.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred
as MHC class II molecule. In the endoplasmic reticulum (ER) it
forms a heterononamer; 3 MHC class II molecules bind to a CD74
homotrimer (also known as invariant chain or HLA class II
histocompatibility antigen gamma chain). In the
endosomal/lysosomal system; CD74 undergoes sequential degradation
by various proteases; leaving a small fragment termed CLIP on each
MHC class II molecule. MHC class II molecule interacts with
HLA_DM, and HLA_DO in B-cells, in order to release CLIP and
facilitate the binding of antigenic peptides.
{ECO:0000269|PubMed:11376336, ECO:0000269|PubMed:14769912,
ECO:0000269|PubMed:15020763, ECO:0000269|PubMed:17629515}.
-!- INTERACTION:
P04233:CD74; NbExp=2; IntAct=EBI-713389, EBI-2622890;
P01920:HLA-DQB1; NbExp=2; IntAct=EBI-713389, EBI-1038012;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Endoplasmic reticulum membrane; Single-pass type I
membrane protein. Golgi apparatus, trans-Golgi network membrane;
Single-pass type I membrane protein. Endosome membrane; Single-
pass type I membrane protein. Lysosome membrane; Single-pass type
I membrane protein. Note=The MHC class II complex transits through
a number of intracellular compartments in the endocytic pathway
until it reaches the cell membrane for antigen presentation.
-!- POLYMORPHISM: The following alleles of DQA1 are known: DQA1*01:01,
DQA1*01:02, DQA1*01:03, DQA1*01:04, DQA1*01:05, DQA1*01:06,
DQA1*01:07, DQA1*02:01, DQA1*03:01, DQA1*03:02, DQA1*03:03,
DQA1*04:01, DQA1*04:02, DQA1*04:03, DQA1*04:04, DQA1*05:01,
DQA1*05:02, DQA1*05:03, DQA1*05:04, DQA1*05:05, DQA1*05:06,
DQA1*05:07, DQA1*05:08, DQA1*05:09, DQA1*06:01, DQA1*06:02. The
sequence shown is that of DQA1*05:01.
-!- POLYMORPHISM: DQ2 (heterodimer of DQA1*05:01/DQB1*02:01) is
associated with more than 90% of celiac disease patients. A
minority displays DQ8 (heterodimer of DQA1*03/DQB1*03:02). DQ0602
(heterodimer of DQA1*01:02/DQB1*06:02) confers dominant protection
against type 1 diabetes (T1D) and strong susceptibility to
narcolepsy.
-!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD56720.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X00033; CAA24917.1; -; mRNA.
EMBL; X00370; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; X00452; CAA25141.1; -; mRNA.
EMBL; M16995; AAA59760.1; -; mRNA.
EMBL; U92032; AAB91990.1; -; Genomic_DNA.
EMBL; AY663395; AAU87978.1; -; Genomic_DNA.
EMBL; AY663398; AAU87987.1; -; Genomic_DNA.
EMBL; AY663400; AAU87992.1; -; Genomic_DNA.
EMBL; AY663406; AAU88007.1; -; Genomic_DNA.
EMBL; AY663411; AAU88022.1; -; Genomic_DNA.
EMBL; AY663413; AAU88028.1; -; Genomic_DNA.
EMBL; DQ178403; ABA86855.1; -; Genomic_DNA.
EMBL; DQ178400; ABA86855.1; JOINED; Genomic_DNA.
EMBL; DQ178401; ABA86855.1; JOINED; Genomic_DNA.
EMBL; DQ178402; ABA86855.1; JOINED; Genomic_DNA.
EMBL; DQ178407; ABA86856.1; -; Genomic_DNA.
EMBL; DQ178404; ABA86856.1; JOINED; Genomic_DNA.
EMBL; DQ178405; ABA86856.1; JOINED; Genomic_DNA.
EMBL; DQ178406; ABA86856.1; JOINED; Genomic_DNA.
EMBL; DQ178411; ABA86857.1; -; Genomic_DNA.
EMBL; DQ178408; ABA86857.1; JOINED; Genomic_DNA.
EMBL; DQ178409; ABA86857.1; JOINED; Genomic_DNA.
EMBL; DQ178410; ABA86857.1; JOINED; Genomic_DNA.
EMBL; DQ178415; ABA86858.1; -; Genomic_DNA.
EMBL; DQ178412; ABA86858.1; JOINED; Genomic_DNA.
EMBL; DQ178413; ABA86858.1; JOINED; Genomic_DNA.
EMBL; DQ178414; ABA86858.1; JOINED; Genomic_DNA.
EMBL; M29616; AAA59759.1; -; Genomic_DNA.
EMBL; M29613; AAA59759.1; JOINED; Genomic_DNA.
EMBL; AF322870; AAK11577.1; -; Genomic_DNA.
EMBL; AF322867; AAK11577.1; JOINED; Genomic_DNA.
EMBL; AF322868; AAK11577.1; JOINED; Genomic_DNA.
EMBL; AF322869; AAK11577.1; JOINED; Genomic_DNA.
EMBL; AF395700; AAM69677.1; -; Genomic_DNA.
EMBL; AF395697; AAM69677.1; JOINED; Genomic_DNA.
EMBL; AF395698; AAM69677.1; JOINED; Genomic_DNA.
EMBL; AF395699; AAM69677.1; JOINED; Genomic_DNA.
EMBL; CR450297; CAG29293.1; -; mRNA.
EMBL; AM042559; CAJ14960.1; -; Genomic_DNA.
EMBL; AM042560; CAJ14961.1; -; Genomic_DNA.
EMBL; AK313975; BAG36689.1; -; mRNA.
EMBL; BX248406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z84489; CAB06491.1; -; Genomic_DNA.
EMBL; BC008585; AAH08585.1; -; mRNA.
EMBL; BC157865; AAI57866.1; -; mRNA.
EMBL; L46875; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; L46876; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; L46877; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; L46878; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; L46880; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; L46881; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M11124; AAA59754.1; -; mRNA.
EMBL; M20431; AAA59758.1; -; mRNA.
EMBL; L34082; AAC41950.1; -; mRNA.
EMBL; L34085; AAC41953.1; -; mRNA.
EMBL; L34086; AAC41954.1; -; mRNA.
EMBL; L34089; AAC41957.1; -; mRNA.
EMBL; L34090; AAC41958.1; -; mRNA.
EMBL; L34092; AAC41960.1; -; mRNA.
EMBL; L34093; AAC41961.1; -; mRNA.
EMBL; L34094; AAC41962.1; -; mRNA.
EMBL; L42625; AAA85334.1; -; mRNA.
EMBL; AY197775; AAO45622.1; -; Genomic_DNA.
EMBL; AY547314; AAS49496.1; -; Genomic_DNA.
EMBL; AY206406; AAO47362.1; -; Genomic_DNA.
EMBL; AY585236; AAT09985.1; -; Genomic_DNA.
EMBL; M34997; AAA35772.1; -; Genomic_DNA.
EMBL; M34999; AAA74633.1; -; Genomic_DNA.
EMBL; U85035; AAB41891.1; -; Genomic_DNA.
EMBL; AF109734; AAD56720.1; ALT_SEQ; Genomic_DNA.
EMBL; U03675; AAB60341.1; -; Genomic_DNA.
EMBL; M20506; AAA59774.1; -; mRNA.
EMBL; J00199; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M17846; AAA59707.1; -; mRNA.
PIR; A02211; HLHUD1.
PIR; A02213; HLHUDQ.
PIR; A02214; HLHUD7.
PIR; A02215; HLHU3C.
PIR; A93326; HLHUDC.
PIR; B27628; B27628.
PIR; D34512; D34512.
RefSeq; NP_002113.2; NM_002122.3.
UniGene; Hs.387679; -.
UniGene; Hs.591798; -.
UniGene; Hs.706240; -.
PDB; 1JK8; X-ray; 2.40 A; A=27-206.
PDB; 1NBN; Model; -; A=27-206.
PDB; 1S9V; X-ray; 2.22 A; A/D=24-216.
PDB; 1UVQ; X-ray; 1.80 A; A=24-218.
PDB; 2NNA; X-ray; 2.10 A; A=24-206.
PDB; 4GG6; X-ray; 3.20 A; A/C=24-206.
PDB; 4OZF; X-ray; 2.70 A; A=24-206.
PDB; 4OZG; X-ray; 3.00 A; A/C=24-206.
PDB; 4OZH; X-ray; 2.80 A; A/C=24-206.
PDB; 4OZI; X-ray; 3.20 A; A/C=24-206.
PDB; 5KSA; X-ray; 2.00 A; A=24-206.
PDB; 5KSB; X-ray; 2.90 A; A/C=24-206.
PDB; 5KSU; X-ray; 2.73 A; A/D=24-216.
PDB; 5KSV; X-ray; 2.19 A; A=24-216.
PDBsum; 1JK8; -.
PDBsum; 1NBN; -.
PDBsum; 1S9V; -.
PDBsum; 1UVQ; -.
PDBsum; 2NNA; -.
PDBsum; 4GG6; -.
PDBsum; 4OZF; -.
PDBsum; 4OZG; -.
PDBsum; 4OZH; -.
PDBsum; 4OZI; -.
PDBsum; 5KSA; -.
PDBsum; 5KSB; -.
PDBsum; 5KSU; -.
PDBsum; 5KSV; -.
ProteinModelPortal; P01909; -.
SMR; P01909; -.
BioGrid; 109362; 34.
BioGrid; 1529240; 1.
IntAct; P01909; 11.
MINT; P01909; -.
BioMuta; HLA-DQA1; -.
DMDM; 122188; -.
PeptideAtlas; P01909; -.
PRIDE; P01909; -.
DNASU; 3117; -.
Ensembl; ENST00000343139; ENSP00000339398; ENSG00000196735.
Ensembl; ENST00000374949; ENSP00000364087; ENSG00000196735.
Ensembl; ENST00000383251; ENSP00000372738; ENSG00000206305.
Ensembl; ENST00000395363; ENSP00000378767; ENSG00000196735.
Ensembl; ENST00000399675; ENSP00000382583; ENSG00000206305.
Ensembl; ENST00000399678; ENSP00000382586; ENSG00000206305.
Ensembl; ENST00000418023; ENSP00000387892; ENSG00000232062.
Ensembl; ENST00000444296; ENSP00000413237; ENSG00000232062.
GeneID; 3117; -.
KEGG; hsa:3117; -.
UCSC; uc003obr.4; human.
CTD; 3117; -.
DisGeNET; 3117; -.
EuPathDB; HostDB:ENSG00000196735.11; -.
GeneCards; HLA-DQA1; -.
GeneReviews; HLA-DQA1; -.
HGNC; HGNC:4942; HLA-DQA1.
HPA; HPA012315; -.
MalaCards; HLA-DQA1; -.
MIM; 146880; gene.
neXtProt; NX_P01909; -.
Orphanet; 555; Celiac disease.
Orphanet; 243377; Diabetes mellitus type 1.
Orphanet; 930; Idiopathic achalasia.
PharmGKB; PA35066; -.
HOVERGEN; HBG006862; -.
InParanoid; P01909; -.
KO; K06752; -.
OrthoDB; EOG091G0IC9; -.
PhylomeDB; P01909; -.
TreeFam; TF333797; -.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-389948; PD-1 signaling.
Reactome; R-HSA-877300; Interferon gamma signaling.
SIGNOR; P01909; -.
ChiTaRS; HLA-DQA1; human.
EvolutionaryTrace; P01909; -.
GenomeRNAi; 3117; -.
PRO; PR:P01909; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000196735; -.
CleanEx; HS_HLA-DQA1; -.
ExpressionAtlas; P01909; baseline and differential.
Genevisible; P01909; HS.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0042613; C:MHC class II protein complex; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB.
GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.320.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR014745; MHC_II_a/b_N.
InterPro; IPR001003; MHC_II_a_N.
Pfam; PF07654; C1-set; 1.
Pfam; PF00993; MHC_II_alpha; 1.
SMART; SM00407; IGc1; 1.
SMART; SM00920; MHC_II_alpha; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Endosome; Glycoprotein; Golgi apparatus; Immunity; Lysosome; Membrane;
MHC II; Polymorphism; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000269|PubMed:6576979}.
CHAIN 24 254 HLA class II histocompatibility antigen,
DQ alpha 1 chain.
/FTId=PRO_0000018970.
TOPO_DOM 24 216 Extracellular. {ECO:0000255}.
TRANSMEM 217 239 Helical. {ECO:0000255}.
TOPO_DOM 240 254 Cytoplasmic.
DOMAIN 112 204 Ig-like C1-type.
REGION 24 119 Alpha-1.
REGION 120 203 Alpha-2.
REGION 204 216 Connecting peptide.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 132 188 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:11376336,
ECO:0000269|PubMed:14769912,
ECO:0000269|PubMed:17629515}.
VARIANT 8 8 M -> L (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*04:01 and allele DQA1*06:01;
dbSNP:rs1047989).
/FTId=VAR_033399.
VARIANT 11 11 A -> T (in allele DQA1*05:05, allele
DQA1*05:08 and allele DQA1*05:09;
dbSNP:rs1047992).
/FTId=VAR_033400.
VARIANT 17 17 V -> M (in allele DQA1*01:04 and allele
DQA1*01:05; dbSNP:rs12722039).
/FTId=VAR_050380.
VARIANT 18 18 M -> T (in allele DQA1*03:03;
dbSNP:rs11545686).
/FTId=VAR_050381.
VARIANT 24 24 E -> K (in allele DQA1*05:09;
dbSNP:rs41545012).
/FTId=VAR_060493.
VARIANT 25 25 D -> G (in allele DQA1*01:04 and allele
DQA1*01:05; dbSNP:rs12722042).
/FTId=VAR_050382.
VARIANT 34 34 Y -> C (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs1129740).
/FTId=VAR_060494.
VARIANT 41 41 S -> F (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs1071630).
/FTId=VAR_033401.
VARIANT 44 44 P -> L (in allele DQA1*05:04;
dbSNP:rs41549715).
/FTId=VAR_060495.
VARIANT 48 48 Y -> F (in allele DQA1*02:01, allele
DQA1*01:03, allele DQA1*06:01 and allele
DQA1*06:02; dbSNP:rs12722051).
/FTId=VAR_033402.
VARIANT 49 49 T -> S (in allele DQA1*03:01, allele
DQA1*03:02 and allele DQA1*03:03;
dbSNP:rs1048023).
/FTId=VAR_033403.
VARIANT 57 57 Q -> E (in allele DQA1*01:01, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:07, allele DQA1*02:01, allele
DQA1*03:01, allele DQA1*03:02 and allele
DQA1*03:03; dbSNP:rs10093).
/FTId=VAR_014604.
VARIANT 63 63 G -> E (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06, allele DQA1*01:07, allele
DQA1*02:01, allele DQA1*03:01, allele
DQA1*03:02 and allele DQA1*03:03;
dbSNP:rs1142323).
/FTId=VAR_060496.
VARIANT 64 64 R -> K (in allele DQA1*01:03;
dbSNP:rs36219699).
/FTId=VAR_050383.
VARIANT 67 67 T -> A (in allele DQA1*01:06;
dbSNP:rs41543221).
/FTId=VAR_060497.
VARIANT 68 68 V -> A (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs1142324).
/FTId=VAR_060498.
VARIANT 70 70 C -> K (in allele DQA1*02:01; requires 2
nucleotide substitutions).
/FTId=VAR_060499.
VARIANT 70 70 C -> Q (in allele DQA1*03:01, allele
DQA1*03:02 and allele DQA1*03:03;
requires 2 nucleotide substitutions).
/FTId=VAR_060500.
VARIANT 70 70 C -> R (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs1142326).
/FTId=VAR_060501.
VARIANT 70 70 C -> Y (in dbSNP:rs3207983).
/FTId=VAR_033404.
VARIANT 71 71 L -> W (in allele DQA1*01:01, allele
DQA1*01:02,allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs1142328).
/FTId=VAR_060502.
VARIANT 73 73 V -> D (in dbSNP:rs760671632).
/FTId=VAR_033406.
VARIANT 73 73 V -> E (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs3208105).
/FTId=VAR_060503.
VARIANT 73 73 V -> L (in allele DQA1*02:01, allele
DQA1*03:01, allele DQA1*03:02 and allele
DQA1*03:03; dbSNP:rs12722061).
/FTId=VAR_033405.
VARIANT 74 74 L -> F (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06, allele DQA1*01:07, allele
DQA1*02:01, allele DQA1*03:01, allele
DQA1*03:02 and allele DQA1*03:03;
dbSNP:rs9272698).
/FTId=VAR_060504.
VARIANT 75 75 R -> H (in allele DQA1*02:01).
/FTId=VAR_060505.
VARIANT 75 75 R -> S (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs9272699).
/FTId=VAR_060506.
VARIANT 76 76 Q -> K (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs1048052).
/FTId=VAR_060507.
VARIANT 76 76 Q -> R (in allele DQA1*02:01, allele
DQA1*03:01, allele DQA1*03:02 and allele
DQA1*03:03; dbSNP:rs12722069).
/FTId=VAR_060508.
VARIANT 77 77 F -> L (in allele DQA1*02:01;
dbSNP:rs3188043).
/FTId=VAR_060509.
VARIANT 78 78 R -> GG (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05,allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs4193).
/FTId=VAR_060510.
VARIANT 78 78 R -> RR (in allele DQA1*03:01, allele
DQA1*03:02 and allele DQA1*03:03).
/FTId=VAR_060511.
VARIANT 81 81 P -> R (in allele DQA1*05:02;
dbSNP:rs41541412).
/FTId=VAR_060512.
VARIANT 83 83 F -> G (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
requires 2 nucleotide substitutions).
/FTId=VAR_060513.
VARIANT 86 86 T -> R (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs1142333).
/FTId=VAR_033408.
VARIANT 88 88 I -> M (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs1142334).
/FTId=VAR_033409.
VARIANT 91 91 L -> A (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
requires 2 nucleotide substitutions).
/FTId=VAR_060514.
VARIANT 91 91 L -> T (in allele DQA1*04:01, allele
DQA1*04:02, allele DQA1*04:04, allele
DQA1*06:01 and allele DQA1*06:02;
requires 2 nucleotide substitutions).
/FTId=VAR_060515.
VARIANT 97 97 S -> I (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06, allele DQA1*01:07, allele
DQA1*02:01, allele DQA1*03:01, allele
DQA1*03:02, allele DQA1*03:03, allele
DQA1*04:01, allele DQA1*04:02, allele
DQA1*04:04, allele DQA1*06:01 and allele
DQA1*06:02; dbSNP:rs9279910).
/FTId=VAR_060516.
VARIANT 98 98 L -> M (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs1064944).
/FTId=VAR_060517.
VARIANT 98 98 L -> V (in allele DQA1*03:01, allele
DQA1*03:02 and allele DQA1*03:03;
dbSNP:rs1064944).
/FTId=VAR_060518.
VARIANT 101 101 R -> C (in allele DQA1*01:07;
dbSNP:rs41542116).
/FTId=VAR_060519.
VARIANT 102 102 S -> Y (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:06 and allele DQA1*01:07;
dbSNP:rs1129808).
/FTId=VAR_050384.
VARIANT 124 124 L -> V (in allele DQA1*05:06;
dbSNP:rs41555012).
/FTId=VAR_060520.
VARIANT 129 129 I -> T (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:07, allele DQA1*02:01, allele
DQA1*03:01, allele DQA1*03:02, allele
DQA1*03:03, allele DQA1*04:01, allele
DQA1*04:02, allele DQA1*04:04, allele
DQA1*06:01 and allele DQA1*06:02;
dbSNP:rs707952).
/FTId=VAR_050385.
VARIANT 151 151 H -> Q (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:04, allele
DQA1*01:05 and allele DQA1*01:07;
dbSNP:rs707950).
/FTId=VAR_050386.
VARIANT 152 152 S -> A (in allele DQA1*01:03;
dbSNP:rs41547417).
/FTId=VAR_060521.
VARIANT 160 160 T -> I (in allele DQA1*04:02;
dbSNP:rs41545514).
/FTId=VAR_060522.
VARIANT 161 161 S -> I (in allele DQA1*05:08;
dbSNP:rs41544114).
/FTId=VAR_060524.
VARIANT 161 161 S -> R (in allele DQA1*06:02;
dbSNP:rs41552014).
/FTId=VAR_060523.
VARIANT 175 175 Y -> H (in allele DQA1*04:04;
dbSNP:rs41550317).
/FTId=VAR_060525.
VARIANT 178 178 L -> F (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:07, allele DQA1*02:01, allele
DQA1*03:01, allele DQA1*03:02, allele
DQA1*03:03, allele DQA1*04:01, allele
DQA1*04:02, allele DQA1*04:04, allele
DQA1*06:01 and allele DQA1*06:02;
dbSNP:rs707949).
/FTId=VAR_060526.
VARIANT 182 182 A -> D (in allele DQA1*03:02 and allele
DQA1*03:03; dbSNP:rs7990).
/FTId=VAR_060527.
VARIANT 182 182 A -> S (in allele DQA1*05:03, allele
DQA1*05:06 and allele DQA1*05:07;
dbSNP:rs41561312).
/FTId=VAR_060528.
VARIANT 183 183 E -> D (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:07, allele DQA1*02:01, allele
DQA1*03:01, allele DQA1*03:02, allele
DQA1*03:03, allele DQA1*04:01, allele
DQA1*04:02, allele DQA1*04:04, allele
DQA1*06:01 and allele DQA1*06:02;
dbSNP:rs707963).
/FTId=VAR_060529.
VARIANT 185 185 S -> I (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05, allele
DQA1*01:07, allele DQA1*02:01, allele
DQA1*03:01, allele DQA1*03:02, allele
DQA1*03:03, allele DQA1*04:01, allele
DQA1*04:02, allele DQA1*04:04, allele
DQA1*06:01 and allele DQA1*06:02;
dbSNP:rs707962).
/FTId=VAR_060530.
VARIANT 197 197 K -> E (in allele DQA1*02:01, allele
DQA1*03:01, allele DQA1*03:02, allele
DQA1*03:03, allele DQA1*04:01, allele
DQA1*04:02, allele DQA1*04:04, allele
DQA1*06:01 and allele DQA1*06:02;
dbSNP:rs2308891).
/FTId=VAR_060531.
VARIANT 197 197 K -> Q (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04, allele DQA1*01:05 and allele
DQA1*01:07; dbSNP:rs2308891).
/FTId=VAR_060532.
VARIANT 209 209 A -> T (in allele DQA1*03:01, allele
DQA1*03:02 and allele DQA1*03:03;
dbSNP:rs9272785).
/FTId=VAR_050387.
VARIANT 221 221 A -> T (in allele DQA1*01:04;
dbSNP:rs35087390).
/FTId=VAR_050388.
VARIANT 229 229 V -> M (in allele DQA1*01:02;
dbSNP:rs9260).
/FTId=VAR_033411.
VARIANT 230 230 G -> C (in allele DQA1*05:07;
dbSNP:rs41545416).
/FTId=VAR_060533.
VARIANT 237 237 F -> L (in allele DQA1*02:01, allele
DQA1*03:01, allele DQA1*03:02 and allele
DQA1*03:03; dbSNP:rs1048430).
/FTId=VAR_033412.
VARIANT 240 240 R -> Q (in allele DQA1*01:01, allele
DQA1*01:02, allele DQA1*01:03, allele
DQA1*01:04 and allele DQA1*01:05;
dbSNP:rs1048439).
/FTId=VAR_033413.
CONFLICT 11 11 A -> S (in Ref. 4; AAA59760).
{ECO:0000305}.
CONFLICT 23 27 Missing (in Ref. 16; AAA59754).
{ECO:0000305}.
CONFLICT 91 91 L -> H (in Ref. 4; AAA59760).
{ECO:0000305}.
CONFLICT 107 107 A -> P (in Ref. 16; AAA59754).
{ECO:0000305}.
CONFLICT 156 156 G -> D (in Ref. 3; CAA25141).
{ECO:0000305}.
CONFLICT 213 213 E -> D (in Ref. 16; AAA59754).
{ECO:0000305}.
STRAND 29 40 {ECO:0000244|PDB:5KSA}.
TURN 41 44 {ECO:0000244|PDB:5KSA}.
STRAND 45 52 {ECO:0000244|PDB:5KSA}.
STRAND 55 61 {ECO:0000244|PDB:5KSA}.
TURN 62 65 {ECO:0000244|PDB:5KSA}.
STRAND 66 71 {ECO:0000244|PDB:5KSA}.
HELIX 72 76 {ECO:0000244|PDB:5KSA}.
HELIX 81 101 {ECO:0000244|PDB:5KSA}.
TURN 102 104 {ECO:0000244|PDB:1JK8}.
STRAND 113 120 {ECO:0000244|PDB:5KSA}.
STRAND 124 126 {ECO:0000244|PDB:4OZF}.
STRAND 128 137 {ECO:0000244|PDB:5KSA}.
STRAND 143 148 {ECO:0000244|PDB:5KSA}.
STRAND 151 153 {ECO:0000244|PDB:5KSA}.
STRAND 157 159 {ECO:0000244|PDB:5KSA}.
STRAND 170 178 {ECO:0000244|PDB:5KSA}.
STRAND 186 191 {ECO:0000244|PDB:5KSA}.
STRAND 195 197 {ECO:0000244|PDB:5KSA}.
STRAND 199 203 {ECO:0000244|PDB:5KSA}.
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


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