ID Q95HB9_HUMAN Unreviewed; 260 AA. AC Q95HB9; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 27-SEP-2017, entry version 129. DE SubName: Full=HLA-DPA1 protein {ECO:0000313|EMBL:AAH09956.1}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AHW47932.1}; GN Name=HLA-DPA1 {ECO:0000313|EMBL:AHW47932.1}; 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|EMBL:AAH09956.1}; RN [1] {ECO:0000213|PDB:1M6O, ECO:0000213|PDB:1N2R} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 77-85. RX PubMed=12939341; DOI=10.1084/jem.20030066; RA Macdonald W.A., Purcell A.W., Mifsud N.A., Ely L.K., Williams D.S., RA Chang L., Gorman J.J., Clements C.S., Kjer-Nielsen L., Koelle D.M., RA Burrows S.R., Tait B.D., Holdsworth R., Brooks A.G., Lovrecz G.O., RA Lu L., Rossjohn J., McCluskey J.; RT "A naturally selected dimorphism within the HLA-B44 supertype alters RT class I structure, peptide repertoire, and T cell recognition."; RL J. Exp. Med. 198:679-691(2003). RN [2] {ECO:0000313|EMBL:AAH09956.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Primary B-Cells {ECO:0000313|EMBL:AAH09956.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., RA Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., RA Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., RA Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., RA Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., RA Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., RA Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., RA Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., RA Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., RA Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., RA Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., RA Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., RA Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., RA Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., RA Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., RA Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., RA Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., RA Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., RA Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] {ECO:0000213|PDB:3L3D, ECO:0000213|PDB:3L3G, ECO:0000213|PDB:3L3I} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 77-85. RX PubMed=20212169; DOI=10.1073/pnas.1000032107; RA Theodossis A., Guillonneau C., Welland A., Ely L.K., Clements C.S., RA Williamson N.A., Webb A.I., Wilce J.A., Mulder R.J., Dunstone M.A., RA Doherty P.C., McCluskey J., Purcell A.W., Turner S.J., Rossjohn J.; RT "Constraints within major histocompatibility complex class I RT restricted peptides: presentation and consequences for T-cell RT recognition."; RL Proc. Natl. Acad. Sci. U.S.A. 107:5534-5539(2010). RN [4] {ECO:0000313|EMBL:AHW47932.1} RP NUCLEOTIDE SEQUENCE. RA Pyo C.-W., Wang K., Shen S., Song Y., Wang R., Vu Q., Hall R.J., RA Eng K., Bowman B., Ranade S., Geraghty D.E.; RT "Haplotype-resolved resequencing of conserved extended haploytpes RT associated with disease using fosmid target capture and long-read SMRT RT sequencing technology."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:ALX87261.1} RP NUCLEOTIDE SEQUENCE. RA Chooi Y.-H.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:AMK37689.1} RP NUCLEOTIDE SEQUENCE. RA Lazaro A.M., Hou L., Hurley C.K.; RT "Novel HLA DPA1 allele."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:AML03227.1} RP NUCLEOTIDE SEQUENCE. RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E., RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M., RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. 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; BC009956; AAH09956.1; -; mRNA. DR EMBL; KJ657694; AHW47932.1; -; Genomic_DNA. DR EMBL; KP774796; ALX87261.1; -; Genomic_DNA. DR EMBL; KP774797; ALX87262.1; -; Genomic_DNA. DR EMBL; KP774799; ALX87264.1; -; Genomic_DNA. DR EMBL; KP774800; ALX87265.1; -; Genomic_DNA. DR EMBL; KT725627; AMK37689.1; -; Genomic_DNA. DR EMBL; KT725628; AMK37690.1; -; Genomic_DNA. DR EMBL; KT716042; AML03227.1; -; Genomic_DNA. DR EMBL; KT716046; AML03231.1; -; Genomic_DNA. DR UniGene; Hs.347270; -. DR PDB; 1M6O; X-ray; 1.60 A; C=77-85. DR PDB; 1N2R; X-ray; 1.70 A; C=77-85. DR PDB; 3L3D; X-ray; 1.80 A; C=77-85. DR PDB; 3L3G; X-ray; 2.10 A; C=77-85. DR PDB; 3L3I; X-ray; 1.70 A; C=77-85. DR PDB; 3L3J; X-ray; 2.40 A; C=77-85. DR PDB; 3L3K; X-ray; 2.60 A; C=77-85. DR PDBsum; 1M6O; -. DR PDBsum; 1N2R; -. DR PDBsum; 3L3D; -. DR PDBsum; 3L3G; -. DR PDBsum; 3L3I; -. DR PDBsum; 3L3J; -. DR PDBsum; 3L3K; -. DR eggNOG; ENOG410IZMF; Eukaryota. DR eggNOG; ENOG410YHX9; LUCA. DR HOVERGEN; HBG006862; -. DR ChiTaRS; HLA-DPA1; human. 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; IPR007110; Ig-like_dom. 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:1M6O, ECO:0000213|PDB:1N2R, KW ECO:0000213|PDB:3L3D, ECO:0000213|PDB:3L3G}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437908}; KW Membrane {ECO:0000256|SAAS:SAAS00437963, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437939, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 260 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5010977198. FT TRANSMEM 227 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 118 198 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 260 AA; 29335 MW; 5DD08E383269E05A CRC64; MRPEDRMFHI RAVILRALSL AFLLSLRGAG AIKADHVSTY AAFVQTHRPT GEFMFEFDED EQFYVDLDKK ETVWHLEEFG RAFSFEAQGG LANIAILNNN LNTLIQRSNH TQAANDPPEV TVFPKEPVEL GQPNTLICHI DRFFPPVLNV TWLCNGEPVT EGVAESLFLP RTDYSFHKFH YLTFVPSAED VYDCRVEHWG LDQPLLKHWE AQEPIQMPET TETVLCALGL VLGLVGIIVG TVLIIKSLRS GHDPRAQGPL //