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HLA class II histocompatibility antigen, DQ alpha 2 chain (DX alpha chain) (HLA class II histocompatibility antigen, DQ(6) alpha chain) (HLA-DQA1) (MHC class II DQA2)

 DQA2_HUMAN              Reviewed;         255 AA.
P01906; A2BF37; B0V0E7; O19789; Q5SQ94; Q5SR04;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
05-DEC-2018, entry version 168.
RecName: Full=HLA class II histocompatibility antigen, DQ alpha 2 chain;
AltName: Full=DX alpha chain;
AltName: Full=HLA class II histocompatibility antigen, DQ(6) alpha chain;
AltName: Full=HLA-DQA1;
AltName: Full=MHC class II DQA2;
Flags: Precursor;
Name=HLA-DQA2; Synonyms=HLA-DXA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
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).
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).
PubMed=3610256; DOI=10.1007/BF00345456;
Auffray C., Lillie J.W., Korman A.J., Boss J.M., Frechin N.,
Guillemot F., Cooper J., Mulligan R.C., Strominger J.L.;
"Structure and expression of HLA-DQ alpha and -DX alpha genes:
interallelic alternate splicing of the HLA-DQ alpha gene and
functional splicing of the HLA-DQ alpha gene using a retroviral
Immunogenetics 26:63-73(1987).
AND ASP-247.
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).
PubMed=8026991; DOI=10.1016/0198-8859(94)90264-X;
Rudy G., Lew A.M.;
"Limited polymorphism of the HLA-DQA2 promoter and identification of a
variant octamer.";
Hum. Immunol. 39:225-229(1994).
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
Proc. Natl. Acad. Sci. U.S.A. 86:9986-9990(1989).
Rudy G.B., Lew A.M.;
"The nonpolymorphic MHC class II isotype, HLA-DQA2, is expressed on
the surface of B lymphoblastoid cells.";
J. Immunol. 158:2116-2125(1997).
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).
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).
PubMed=18046453; DOI=10.1038/sj.emboj.7601945;
Rocha N., Neefjes J.;
"MHC class II molecules on the move for successful antigen
EMBO J. 27:1-5(2008).
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).
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).
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).
PubMed=22407913; DOI=10.4049/jimmunol.1103048;
Lenormand C., Bausinger H., Gross F., Signorino-Gelo F., Koch S.,
Peressin M., Fricker D., Cazenave J.P., Bieber T., Hanau D.,
de la Salle H., Tourne S.;
"HLA-DQA2 and HLA-DQB2 genes are specifically expressed in human
Langerhans cells and encode a new HLA class II molecule.";
J. Immunol. 188:3903-3911(2012).
-!- 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. {ECO:0000269|PubMed:22407913}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred
as MHC class II molecule. Dimer formation with HLA-DQB2, but not
with HLA-DQB1, is required for efficient exit from the endoplasmic
reticulum (ER). In the ER, 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. Association with
HLA-DMA also occurs in skin Langerhans cells, in post-Golgi
compartments. {ECO:0000269|PubMed:22407913}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22407913};
Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:22407913};
Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}.
Golgi apparatus, trans-Golgi network membrane
{ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein
{ECO:0000269|PubMed:22407913}. Endosome membrane
{ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein
{ECO:0000269|PubMed:22407913}. Lysosome membrane
{ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein
{ECO:0000269|PubMed:22407913}. 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
-!- TISSUE SPECIFICITY: Restricted to skin Langerhans cells, although
some expression at low levels may occur at the surface of B
lymphoblastoid cells. {ECO:0000269|PubMed:22407913,
-!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; M29615; AAA59834.1; -; Genomic_DNA.
EMBL; M29614; AAA59834.1; JOINED; Genomic_DNA.
EMBL; X00453; CAA25142.1; -; Genomic_DNA.
EMBL; X00454; CAA25142.1; JOINED; Genomic_DNA.
EMBL; X00455; CAA25142.1; JOINED; Genomic_DNA.
EMBL; X00456; CAA25142.1; JOINED; Genomic_DNA.
EMBL; M17237; AAA59605.1; -; Genomic_DNA.
EMBL; M17235; AAA59605.1; JOINED; Genomic_DNA.
EMBL; CR759848; CAQ07531.1; -; Genomic_DNA.
EMBL; AL773543; CAI18490.1; -; Genomic_DNA.
EMBL; BX248406; CAM26195.1; -; Genomic_DNA.
EMBL; BX927131; CAM26195.1; JOINED; Genomic_DNA.
EMBL; BX927131; CAM26196.1; -; Genomic_DNA.
EMBL; BX248406; CAM26196.1; JOINED; Genomic_DNA.
EMBL; AL713890; CAI17623.1; -; Genomic_DNA.
EMBL; AL672104; CAI18437.1; -; Genomic_DNA.
EMBL; CR936921; CAQ07312.1; -; Genomic_DNA.
EMBL; CR753846; CAQ09761.1; -; Genomic_DNA.
EMBL; BX927160; CAQ10975.1; -; Genomic_DNA.
EMBL; BX927168; CAQ10975.1; JOINED; Genomic_DNA.
EMBL; BX927168; CAQ08754.1; -; Genomic_DNA.
EMBL; BX927160; CAQ08754.1; JOINED; Genomic_DNA.
EMBL; S71248; AAD14077.1; -; Genomic_DNA.
CCDS; CCDS4753.1; -.
PIR; A02210; HLHUDX.
PIR; I54439; I54439.
RefSeq; NP_064440.1; NM_020056.4.
UniGene; Hs.591798; -.
ProteinModelPortal; P01906; -.
SMR; P01906; -.
IntAct; P01906; 1.
STRING; 9606.ENSP00000364076; -.
DrugBank; DB00071; Insulin Pork.
iPTMnet; P01906; -.
PhosphoSitePlus; P01906; -.
BioMuta; HLA-DQA2; -.
DMDM; 122192; -.
PaxDb; P01906; -.
PeptideAtlas; P01906; -.
PRIDE; P01906; -.
ProteomicsDB; 51509; -.
Ensembl; ENST00000241802; ENSP00000241802; ENSG00000206301.
Ensembl; ENST00000374940; ENSP00000364076; ENSG00000237541.
Ensembl; ENST00000415898; ENSP00000400695; ENSG00000231526.
Ensembl; ENST00000443184; ENSP00000405833; ENSG00000257473.
Ensembl; ENST00000446482; ENSP00000390725; ENSG00000225103.
Ensembl; ENST00000447735; ENSP00000393431; ENSG00000223793.
Ensembl; ENST00000449560; ENSP00000401098; ENSG00000233192.
Ensembl; ENST00000453672; ENSP00000387768; ENSG00000231823.
Ensembl; ENST00000546801; ENSP00000447668; ENSG00000233192.
Ensembl; ENST00000551533; ENSP00000448003; ENSG00000223793.
GeneID; 3118; -.
KEGG; hsa:3118; -.
UCSC; uc003obx.4; human.
CTD; 3118; -.
DisGeNET; 3118; -.
EuPathDB; HostDB:ENSG00000237541.3; -.
GeneCards; HLA-DQA2; -.
H-InvDB; HIX0058177; -.
H-InvDB; HIX0166445; -.
H-InvDB; HIX0166701; -.
MIM; 613503; gene.
neXtProt; NX_P01906; -.
OpenTargets; ENSG00000237541; -.
PharmGKB; PA35067; -.
eggNOG; ENOG410IZMF; Eukaryota.
GeneTree; ENSGT00940000162892; -.
HOGENOM; HOG000112076; -.
InParanoid; P01906; -.
KO; K06752; -.
OrthoDB; EOG093703IG; -.
PhylomeDB; P01906; -.
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; P01906; -.
GeneWiki; HLA-DQA2; -.
GenomeRNAi; 3118; -.
PRO; PR:P01906; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000237541; Expressed in 89 organ(s), highest expression level in lung.
CleanEx; HS_HLA-DQA2; -.
ExpressionAtlas; P01906; baseline and differential.
Genevisible; P01906; 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:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW.
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; NAS: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:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
Gene3D;; -; 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; PS00290; IG_MHC; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus;
Immunity; Lysosome; Membrane; MHC II; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
CHAIN 24 255 HLA class II histocompatibility antigen,
DQ alpha 2 chain.
TOPO_DOM 24 217 Extracellular. {ECO:0000255}.
TRANSMEM 218 240 Helical. {ECO:0000255}.
TOPO_DOM 241 255 Cytoplasmic. {ECO:0000255}.
DOMAIN 113 205 Ig-like C1-type.
REGION 24 110 Alpha-1.
REGION 111 204 Alpha-2.
REGION 205 217 Connecting peptide.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
DISULFID 133 189 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 227 227 V -> A (in dbSNP:rs9276436).
VARIANT 247 247 G -> D (in dbSNP:rs2071800).
CONFLICT 84 84 S -> T (in Ref. 1; AAA59834).
CONFLICT 101 101 R -> G (in Ref. 4; CAM26196/CAM26195).
SEQUENCE 255 AA; 28033 MW; 85B13D9FDF2905FE CRC64;

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