ID A0A0G2JH46_HUMAN Unreviewed; 229 AA. AC A0A0G2JH46; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 16-JAN-2019, entry version 25. DE SubName: Full=HLA class II histocompatibility antigen, DR alpha chain {ECO:0000313|Ensembl:ENSP00000372745}; GN Name=HLA-DRA {ECO:0000313|Ensembl:ENSP00000372745}; 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:ENSP00000372745, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000372745, 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|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000213|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [4] {ECO:0000313|Ensembl:ENSP00000372745} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. RN [5] {ECO:0000313|Ensembl:ENSP00000411610} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) 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; AL935032; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX120007; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR354545; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753634; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759779; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; A0A0G2JH46; -. DR jPOST; A0A0G2JH46; -. DR PRIDE; A0A0G2JH46; -. DR Ensembl; ENST00000383258; ENSP00000372745; ENSG00000206308. DR Ensembl; ENST00000411505; ENSP00000411610; ENSG00000228987. DR Ensembl; ENST00000415767; ENSP00000392789; ENSG00000226260. DR Ensembl; ENST00000418111; ENSP00000412562; ENSG00000230726. DR Ensembl; ENST00000427753; ENSP00000398838; ENSG00000234794. DR HGNC; HGNC:4947; HLA-DRA. DR ChiTaRS; HLA-DRA; human. DR Proteomes; UP000005640; Chromosome 6. 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: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; 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; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A0G2JH46, KW ECO:0000213|PeptideAtlas:A0A0G2JH46}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 229 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014514175. FT TRANSMEM 196 217 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 30 109 MHC_II_alpha. FT {ECO:0000259|SMART:SM00920}. FT DOMAIN 110 173 IGc1. {ECO:0000259|SMART:SM00407}. SQ SEQUENCE 229 AA; 25846 MW; 1FAD7B100397335C CRC64; MAISGVPVLG FFIIAVLMSA QESWAIKEEH VIIQAEFYLN PDQSGEFMFD FDGDEIFHVD MAKKETVWRL EEFGRFASFE AQGALANIAV DKANLEIMTK RSNYTPITND KFTPPVVNVT WLRNGKPVTT GVSETVFLPR EDHLFRKFHY LPFLPSTEDV YDCRVEHWGL DEPLLKHWEF DAPSPLPETT ENVVCALGLT VGLVGIIIGT IFIIKGVRKS NAAERRGPL //