ID E9PMV2_HUMAN Unreviewed; 214 AA. AC E9PMV2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-JAN-2019, entry version 54. DE SubName: Full=HLA class II histocompatibility antigen, DQ alpha 1 chain {ECO:0000313|Ensembl:ENSP00000437302}; DE Flags: Fragment; GN Name=HLA-DQA1 {ECO:0000313|Ensembl:ENSP00000437302}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000437302, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000437302, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA 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., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PDB:1UVQ} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 24-204, AND DISULFIDE BONDS. RX PubMed=14769912; DOI=10.1073/pnas.0308458100; RA Siebold C., Hansen B.E., Wyer J.R., Harlos K., Esnouf R.E., RA Svejgaard A., Bell J.I., Strominger J.L., Jones E.Y., Fugger L.; RT "Crystal structure of HLA-DQ0602 that protects against type 1 diabetes RT and confers strong susceptibility to narcolepsy."; RL Proc. Natl. Acad. Sci. U.S.A. 101:1999-2004(2004). RN [3] {ECO:0000313|Ensembl:ENSP00000437302} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|RuleBase:RU004238, ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL662789; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PDB; 1UVQ; X-ray; 1.80 A; A=24-204. DR PDBsum; 1UVQ; -. DR ProteinModelPortal; E9PMV2; -. DR SMR; E9PMV2; -. DR STRING; 9606.ENSP00000339398; -. DR jPOST; E9PMV2; -. DR MaxQB; E9PMV2; -. DR PaxDb; E9PMV2; -. DR PeptideAtlas; E9PMV2; -. DR PRIDE; E9PMV2; -. DR Ensembl; ENST00000496318; ENSP00000437302; ENSG00000196735. DR UCSC; uc063nra.1; human. DR EuPathDB; HostDB:ENSG00000196735.11; -. DR HGNC; HGNC:4942; HLA-DQA1. DR OpenTargets; ENSG00000196735; -. DR eggNOG; ENOG410IZMF; Eukaryota. DR eggNOG; ENOG410YHX9; LUCA. DR GeneTree; ENSGT00940000162892; -. DR ChiTaRS; HLA-DQA1; human. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000196735; Expressed in 186 organ(s), highest expression level in leukocyte. DR ExpressionAtlas; E9PMV2; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR001003; MHC_II_a_N. 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; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1UVQ}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW Metal-binding {ECO:0000213|PDB:1UVQ}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:E9PMV2, KW ECO:0000213|PeptideAtlas:E9PMV2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}; KW Zinc {ECO:0000213|PDB:1UVQ}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 214 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003245364. FT DOMAIN 113 193 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT REGION 151 153 Fucose binding. {ECO:0000213|PDB:1UVQ}. FT METAL 188 188 Zinc. {ECO:0000213|PDB:1UVQ}. FT METAL 203 203 Zinc; via pros nitrogen. FT {ECO:0000213|PDB:1UVQ}. FT CARBOHYD 104 104 N-linked (GlcNAc...) asparagine. FT {ECO:0000213|PDB:1UVQ}. FT CARBOHYD 144 144 N-linked (GlcNAc...) asparagine. FT {ECO:0000213|PDB:1UVQ}. FT DISULFID 133 189 {ECO:0000213|PDB:1UVQ}. FT NON_TER 214 214 {ECO:0000313|Ensembl:ENSP00000437302}. SQ SEQUENCE 214 AA; 23674 MW; 0D93F22BF7419A3B CRC64; MILNKALLLG ALALTTVMSP CGGEDIVADH VASCGVNLYQ FYGPSGQYTH EFDGDEQFYV DLERKETAWR WPEFSKFGGF DPQGALRNMA VAKHNLNIMI KRYNSTAATN EVPEVTVFSK SPVTLGQPNT LICLVDNIFP PVVNITWLSN GQSVTEGVSE TSFLSKSDHS FFKISYLTFL PSADEIYDCK VEHWGLDQPL LKHWGASPST GAEE //