ID DPA1_HUMAN Reviewed; 260 AA. AC P20036; A9YWH7; B9UKH4; O19722; O46883; P01905; P79554; Q2Q060; Q2Q061; AC Q5EY03; Q5STP1; Q6DQK4; Q9BCQ1; Q9TPX3; Q9XS10; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 04-NOV-2026, entry version 208. DE RecName: Full=HLA class II histocompatibility antigen, DP alpha 1 chain; DE AltName: Full=DP(W3); DE AltName: Full=DP(W4); DE AltName: Full=HLA-SB alpha chain; DE AltName: Full=MHC class II DP3-alpha; DE AltName: Full=MHC class II DPA1; DE Flags: Precursor; GN Name=HLA-DPA1; Synonyms=HLA-DP1A, HLASB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DPA1*01:03). RX PubMed=2997750; DOI=10.1093/nar/13.20.7515; RA Lawrance S.K., Das H.K., Pan J., Weissman S.M.; RT "The genomic organisation and nucleotide sequence of the HLA-SB(DP) alpha RT gene."; RL Nucleic Acids Res. 13:7515-7528(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DPA1*01:03). RX PubMed=3036829; DOI=10.1016/s0021-9258(18)47483-2; RA Gustafsson K., Widmark E., Jonsson A.-K., Servenius B., Sachs D.H., RA Larhammar D., Rask L., Peterson P.A.; RT "Class II genes of the human major histocompatibility complex. Evolution of RT the DP region as deduced from nucleotide sequences of the four genes."; RL J. Biol. Chem. 262:8778-8786(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DPA1*01:03). RX PubMed=2461352; DOI=10.1016/0198-8859(88)90016-x; RA Young J.A., Lindsay J., Bodmer J.G., Trowsdale J.; RT "Epitope recognition by a DP alpha chain-specific monoclonal antibody RT (DP11.1) is influenced by the interaction between the DP alpha chain and RT its polymorphic DP beta chain partner."; RL Hum. Immunol. 23:37-44(1988). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DPA1*01:03). 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., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., 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., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-260 (ALLELE DPA1*01:03). RX PubMed=6584734; DOI=10.1038/308327a0; RA Auffray C., Lillie J.W., Arnot D., Grossberger D., Kappes D., RA Strominger J.L.; RT "Isotypic and allotypic variation of human class II histocompatibility RT antigen alpha-chain genes."; RL Nature 308:327-333(1984). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-115 (ALLELE DPA1*02:03). RX PubMed=9234495; DOI=10.1111/j.1399-0039.1997.tb02821.x; RA Muntau B., Thye T., Pirmez C., Horstmann R.D.; RT "A novel DPA1 allele (DPA1*0203) composed of known epitopes."; RL Tissue Antigens 49:668-669(1997). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-115 (ALLELE DPA1*03:02). RX PubMed=9694359; DOI=10.1111/j.1399-0039.1998.tb03009.x; RA Steiner L.L., Cavalli A., Zimmerman P.A., Boatin B.A., Titanji V.P., RA Bradley J.E., Lucius R., Nutman T.B., Begovich A.B.; RT "Three new DP alleles identified in sub-Saharan Africa: DPB1*7401, RT DPA1*02013, and DPA1*0302."; RL Tissue Antigens 51:653-657(1998). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-116 AND 211-260 (ALLELE RP DPA1*01:04), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-229 (ALLELE RP DPA1*02:01), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-116 AND 211-260 RP (ALLELE DPA1*02:02), AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-115 AND RP 211-260 (ALLELES DPA1*03:01 AND DPA1*401). RX PubMed=7725312; DOI=10.1111/j.1399-0039.1995.tb02415.x; RA Rozemuller E.H., Bouwens A.G., van Oort E., Versluis L.F., Marsh S.G., RA Bodmer J.G., Tilanus M.G.; RT "Sequencing-based typing reveals new insight in HLA-DPA1 polymorphism."; RL Tissue Antigens 45:57-62(1995). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-117 (ALLELE DPA1*02:01). RX PubMed=11019928; DOI=10.1034/j.1399-0039.2000.560219.x; RA McDaniel D.O., Nguyen C., McDaniel L.S.; RT "A new HLA-DPA1 allele, DPA1*02016, identified in African-American RT population."; RL Tissue Antigens 56:197-198(2000). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*03:03). RX PubMed=15663751; DOI=10.1111/j.1399-0039.2005.00339.x; RA Luo M., Bamforth J., Gill K., Cohen C., Brunham R.C., Plummer F.A.; RT "High-resolution sequence-based DPA1 typing identified two novel DPA1 RT alleles, DPA1*010303 and DPA1*0303, from a Kenyan population."; RL Tissue Antigens 65:120-122(2005). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*01:06). RX PubMed=18838095; DOI=10.1016/j.humimm.2008.09.001; RA Peterson T.A., Luo M., Mao X., Brunham R.C., Plummer F.A.; RT "Identification of a novel DPA1 allele, DPA1*010602, in an East African RT population."; RL Hum. Immunol. 69:885-886(2008). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELES DPA1*01:03 AND RP DPA1*01:10). RX PubMed=18380777; DOI=10.1111/j.1399-0039.2008.01035.x; RA Lee K.W.; RT "Description of two novel HLA-DPA1 alleles: DPA1*0110 and DPA1*010304."; RL Tissue Antigens 71:575-577(2008). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*02:04). RX PubMed=18489436; DOI=10.1111/j.1399-0039.2008.01046.x; RA Zhao H., Dai W.-J., He Y.-M., Zhu F.-M., Yan L.-X.; RT "A novel HLA-DPA1*0204 allele was identified in a Chinese individual."; RL Tissue Antigens 71:577-578(2008). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*01:06). RA Steiner L., Begovich A., Suraj V.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*01:08). RA Grams S.E., Begovich A., Mangaccat J.; RT "One new DPA1 Allele."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*01:09). RA Bassinger S., Wu J., Williams T.M.; RT "Novel human HLA-DPA1 allele identified in potential bone marrow donors."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-115 (ALLELE DPA1*01:07). RA Varney M.D., Gavrilidis A., Abbott W.; RT "DPA1 polymorphism in Polynesians."; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-115 (ALLELE DPA1*01:05). RX PubMed=8988544; DOI=10.1111/j.1399-0039.1996.tb02675.x; RA May J., Krestchmer C., Schnittger L., Striecker R., Kremoner P.G., RA Meyer C.G.; RT "DPA1*0105, a novel DPA1 variant in a negrois population."; RL Tissue Antigens 48:593-594(1996). RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-210 (ALLELES DPA1*01:04; RP DPA1*02:02; DPA1*03:01 AND DPA1*04:01). RX PubMed=7806277; DOI=10.1007/bf00188437; RA Rozemuller E.H., Versluis L.F., Bouwens A.G., Tilanus M.G.; RT "Exon 2, 3, and 4 polymorphism of HLA-DPA1."; RL Immunogenetics 41:53-53(1995). RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 178-209 (ALLELE DPA1*01:03). RX PubMed=6300884; DOI=10.1073/pnas.80.7.1972; RA Trowsdale J., Lee J., Carey J., Grosveld F., Bodmer J., Bodmer W.; RT "Sequences related to HLA-DR alpha chain on human chromosome 6: restriction RT enzyme polymorphism detected with DC alpha chain probes."; RL Proc. Natl. Acad. Sci. U.S.A. 80:1972-1976(1983). RN [23] RP REVIEW. RX PubMed=8598037; DOI=10.1016/s0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [24] RP REVIEW. RX PubMed=11684289; DOI=10.1016/s0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most out RT of them."; RL Mol. Immunol. 38:329-346(2001). RN [25] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen presentation."; RL EMBO J. 27:1-5(2008). RN [26] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [27] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [28] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [29] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-149. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents them on CC the cell surface for recognition by the CD4 T-cells. The peptide CC binding cleft accommodates peptides of 10-30 residues. The peptides CC presented by MHC class II molecules are generated mostly by degradation CC of proteins that access the endocytic route, where they are processed CC by lysosomal proteases and other hydrolases. Exogenous antigens that CC have been endocytosed by the APC are thus readily available for CC presentation via MHC II molecules, and for this reason this antigen CC presentation pathway is usually referred to as exogenous. As membrane CC proteins on their way to degradation in lysosomes as part of their CC normal turn-over are also contained in the endosomal/lysosomal CC compartments, exogenous antigens must compete with those derived from CC endogenous components. Autophagy is also a source of endogenous CC peptides, autophagosomes constitutively fuse with MHC class II loading CC compartments. In addition to APCs, other cells of the gastrointestinal CC tract, such as epithelial cells, express MHC class II molecules and CC CD74 and act as APCs, which is an unusual trait of the GI tract. To CC produce a MHC class II molecule that presents an antigen, three MHC CC class II molecules (heterodimers of an alpha and a beta chain) CC associate with a CD74 trimer in the ER to form a heterononamer. Soon CC after the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving a CC small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM CC stabilizes MHC class II molecules until primary high affinity antigenic CC peptides are bound. The MHC II molecule bound to a peptide is then CC transported to the cell membrane surface. In B-cells, the interaction CC between HLA-DM and MHC class II molecules is regulated by HLA-DO. CC Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal CC microenvironment has been implicated in the regulation of antigen CC loading into MHC II molecules, increased acidification produces CC increased proteolysis and efficient peptide loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred as CC MHC class II molecule. In the endoplasmic reticulum (ER) it forms a CC heterononamer; 3 MHC class II molecules bind to a CD74 homotrimer (also CC known as invariant chain or HLA class II histocompatibility antigen CC gamma chain). In the endosomal/lysosomal system; CD74 undergoes CC sequential degradation by various proteases; leaving a small fragment CC termed CLIP on each MHC class II molecule. MHC class II molecule CC interacts with HLA_DM, and HLA_DO in B-cells, in order to release CLIP CC and facilitate the binding of antigenic peptides. CC -!- INTERACTION: CC P20036; Q12772: SREBF2; NbExp=3; IntAct=EBI-2802853, EBI-465059; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I membrane CC protein. Golgi apparatus, trans-Golgi network membrane; Single-pass CC type I membrane protein. Endosome membrane; Single-pass type I membrane CC protein. Lysosome membrane; Single-pass type I membrane protein. CC Note=The MHC class II complex transits through a number of CC intracellular compartments in the endocytic pathway until it reaches CC the cell membrane for antigen presentation. CC -!- POLYMORPHISM: The following alleles of DPA1 are known: DPA1*01:03, CC DPA1*01:04, DPA1*01:05, DPA1*01:06, DPA1*01:07, DPA1*01:08, DPA1*01:09, CC DPA1*01:10, DPA1*02:01, DPA1*02:02, DPA1*02:03, DPA1*02:04, DPA1*03:01, CC DPA1*03:02, DPA1*03:03, DPA1*04:01 The sequence shown is that of CC DPA1*01:03. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC64233.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAD42927.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; X03100; CAA26887.1; -; Genomic_DNA. DR EMBL; M27487; AAA63220.1; -; mRNA. DR EMBL; AK292709; BAF85398.1; -; mRNA. DR EMBL; AL645931; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL805913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX120009; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX005422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759795; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR847849; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759904; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR762479; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03669.1; -; Genomic_DNA. DR EMBL; X00457; CAA25143.1; -; mRNA. DR EMBL; Z48473; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF013767; AAC64233.1; ALT_SEQ; Genomic_DNA. DR EMBL; X78199; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X82393; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X82394; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X78198; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X82391; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X79475; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X79477; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X79479; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X79481; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF165160; AAD47826.1; -; Genomic_DNA. DR EMBL; AY618553; AAT92097.1; -; Genomic_DNA. DR EMBL; EU729350; ACH88749.1; -; Genomic_DNA. DR EMBL; DQ274060; ABB88406.1; -; Genomic_DNA. DR EMBL; DQ274061; ABB88407.1; -; Genomic_DNA. DR EMBL; EU304462; ABY27081.1; -; Genomic_DNA. DR EMBL; U87556; AAB97110.1; -; Genomic_DNA. DR EMBL; AF346471; AAK27152.1; -; Genomic_DNA. DR EMBL; AY650051; AAT67468.1; -; Genomic_DNA. DR EMBL; AF076284; AAD42927.1; ALT_SEQ; Genomic_DNA. DR EMBL; X96984; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X80482; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X81347; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X81348; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; K00514; AAA59786.1; -; Genomic_DNA. DR CCDS; CCDS4764.1; -. DR PIR; A29313; HLHUSB. DR RefSeq; NP_001229453.1; NM_001242524.2. DR RefSeq; NP_001229454.1; NM_001242525.2. DR RefSeq; NP_001391949.1; NM_001405020.1. DR RefSeq; NP_291032.2; NM_033554.4. DR PDB; 3LQZ; X-ray; 3.25 A; A=32-212. DR PDB; 4P4K; X-ray; 2.80 A; A/E=32-214. DR PDB; 4P4R; X-ray; 3.00 A; A/C=32-214. DR PDB; 4P57; X-ray; 2.60 A; A/C=32-214. DR PDB; 4P5K; X-ray; 2.59 A; A/D=32-214. DR PDB; 4P5M; X-ray; 1.70 A; A/C/E/G=32-214. DR PDB; 7T2A; X-ray; 3.04 A; A/D=32-212. DR PDB; 7T2B; X-ray; 2.80 A; A/F/K/P=32-212. DR PDB; 7T2C; X-ray; 3.10 A; A=32-212. DR PDB; 7T2D; X-ray; 3.40 A; A/F/K/P=32-212. DR AlphaFoldDB; P20036; -. DR SMR; P20036; -. DR BioGRID; 109358; 127. DR FunCoup; P20036; 578. DR IntAct; P20036; 101. DR NDEx; IQUERY-CP-HLA-DPA1; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000393566; -. DR GlyConnect; P20036; 1 N-Linked glycan (1 site). DR GlyCosmos; P20036; 3 sites, 58 glycans. DR GlyGen; P20036; 3 sites, 60 N-linked glycans (2 sites). DR iPTMnet; P20036; -. DR PhosphoSitePlus; P20036; -. DR BioMuta; HLA-DPA1; -. DR DMDM; 122204; -. DR jPOST; P20036; -. DR MassIVE; P20036; -. DR PaxDb; 9606-ENSP00000393566; -. DR PeptideAtlas; P20036; -. DR ProteomicsDB; 53716; -. DR Antibodypedia; 45587; 342 antibodies from 35 providers. DR DNASU; 3113; -. DR Ensembl; ENST00000374808.6; ENSP00000363941.2; ENSG00000168384.11. DR Ensembl; ENST00000383224.6; ENSP00000372711.2; ENSG00000206291.10. DR Ensembl; ENST00000415247.6; ENSP00000405838.2; ENSG00000224103.7. DR Ensembl; ENST00000419277.5; ENSP00000393566.1; ENSG00000231389.9. DR Ensembl; ENST00000422504.5; ENSP00000406250.1; ENSG00000228163.8. DR Ensembl; ENST00000443117.5; ENSP00000397587.1; ENSG00000235844.8. DR Ensembl; ENST00000454805.5; ENSP00000397139.1; ENSG00000229685.8. DR Ensembl; ENST00000515317.5; ENSP00000427429.1; ENSG00000236177.9. DR Ensembl; ENST00000692443.1; ENSP00000509163.1; ENSG00000231389.9. DR Ensembl; ENST00000923943.1; ENSP00000594002.1; ENSG00000231389.9. DR GeneID; 3113; -. DR KEGG; hsa:3113; -. DR MANE-Select; ENST00000692443.1; ENSP00000509163.1; NM_033554.4; NP_291032.2. DR AGR; HGNC:4938; -. DR ClinPGx; PA35062; -. DR CTD; 3113; -. DR DisGeNET; 3113; -. DR GeneCards; HLA-DPA1; -. DR HGNC; HGNC:4938; HLA-DPA1. DR HPA; ENSG00000231389; Tissue enhanced (lung, lymphoid tissue). DR MalaCards; HLA-DPA1; -. DR MIM; 142880; gene. DR OpenTargets; ENSG00000231389; -. DR Orphanet; 900; Granulomatosis with polyangiitis. DR VEuPathDB; HostDB:ENSG00000231389; -. DR eggNOG; ENOG502RXYJ; Eukaryota. DR GeneTree; ENSGT00940000162498; -. DR HOGENOM; CLU_069380_0_0_1; -. DR InParanoid; P20036; -. DR OMA; ACIQHSN; -. DR PAN-GO; P20036; 9 GO annotations based on evolutionary models. DR PhylomeDB; P20036; -. DR PathwayCommons; P20036; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; Co-inhibition by PD-1. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR Reactome; R-HSA-9938027; Affinity selection of immunoglobulins. DR Reactome; R-HSA-9979719; Processing of antigen in germinal center B cells. DR SignaLink; P20036; -. DR SIGNOR; P20036; -. DR Agora; ENSG00000231389; -. DR BioGRID-ORCS; 3113; 10 hits in 1133 CRISPR screens. DR ChiTaRS; HLA-DPA1; human. DR EvolutionaryTrace; P20036; -. DR GenomeRNAi; 3113; -. DR Pharos; P20036; Tbio. DR PRO; PR:P20036; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P20036; protein. DR Bgee; ENSG00000231389; Expressed in monocyte and 100 other cell types or tissues. DR ExpressionAtlas; P20036; baseline and differential. DR GO; GO:0009986; C:cell surface; IMP:UniProtKB. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central. DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central. DR GO; GO:0032395; F:MHC class II receptor activity; NAS:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:UniProtKB. DR GO; GO:0071346; P:cellular response to type II interferon; IDA:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central. DR GO; GO:0050778; P:positive regulation of immune response; IBA:GO_Central. DR GO; GO:0050870; P:positive regulation of T cell activation; IMP:UniProtKB. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB. DR GO; GO:0032729; P:positive regulation of type II interferon production; IMP:UniProtKB. DR CDD; cd05767; IgC1_MHC_II_alpha; 1. DR FunFam; 2.60.40.10:FF:000280; HLA class II histocompatibility antigen, DR alpha chain; 1. DR FunFam; 3.10.320.10:FF:000002; HLA class II histocompatibility antigen, DR alpha chain; 1. DR Gene3D; 3.10.320.10; Class II Histocompatibility Antigen, M Beta Chain, Chain B, domain 1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR050160; MHC/Immunoglobulin. 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 PANTHER; PTHR19944:SF64; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP ALPHA 1 CHAIN; 1. DR PANTHER; PTHR19944; MHC CLASS II-RELATED; 1. 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; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Cell membrane; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Immunity; KW Lysosome; Membrane; MHC II; Proteomics identification; Reference proteome; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..28 FT CHAIN 29..260 FT /note="HLA class II histocompatibility antigen, DP alpha 1 FT chain" FT /id="PRO_0000018967" FT TOPO_DOM 29..222 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 223..245 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 246..260 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 118..210 FT /note="Ig-like C1-type" FT REGION 29..115 FT /note="Alpha-1" FT REGION 116..209 FT /note="Alpha-2" FT REGION 210..222 FT /note="Connecting peptide" FT CARBOHYD 109 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 149 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT DISULFID 138..194 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VARIANT 42 FT /note="A -> M (in allele DPA1*02:02, allele DPA1*02:04, FT allele DPA1*03:01, allele DPA1*03:02 and allele DPA1*03:03; FT requires 2 nucleotide substitutions; dbSNP:rs386699859)" FT /id="VAR_058832" FT VARIANT 42 FT /note="A -> T (in dbSNP:rs1126533)" FT /id="VAR_047683" FT VARIANT 42 FT /note="A -> V (in dbSNP:rs1126534)" FT /id="VAR_047684" FT VARIANT 49 FT /note="P -> T (in allele DPA1*04:01; dbSNP:rs2308907)" FT /id="VAR_058833" FT VARIANT 54 FT /note="M -> T (in allele DPA1*01:09; dbSNP:rs1042175)" FT /id="VAR_058834" FT VARIANT 59 FT /note="E -> D (in allele DPA1*01:04, allele DPA1*01:08, FT allele DPA1*03:03 and allele DPA1*04:01; dbSNP:rs2308910)" FT /id="VAR_058835" FT VARIANT 62 FT /note="M -> K (in dbSNP:rs2308912)" FT /id="VAR_058836" FT VARIANT 62 FT /note="M -> L (in dbSNP:rs2308911)" FT /id="VAR_047685" FT VARIANT 62 FT /note="M -> Q (in allele DPA1*01:06, allele DPA1*02:01, FT allele DPA1*02:02 and allele DPA1*02:04; requires 2 FT nucleotide substitutions; dbSNP:rs36013091)" FT /id="VAR_058850" FT VARIANT 74 FT /note="W -> C (in allele DPA1*01:10; dbSNP:rs72558171)" FT /id="VAR_058837" FT VARIANT 81 FT /note="Q -> R (in allele DPA1*01:08, allele DPA1*02:01, FT allele DPA1*02:02, allele DPA1*02:03, allele DPA1*02:04 and FT allele DPA1*04:01; dbSNP:rs1042178)" FT /id="VAR_047686" FT VARIANT 82 FT /note="A -> T (in allele DPA1*01:07; dbSNP:rs41543112)" FT /id="VAR_058838" FT VARIANT 97 FT /note="L -> S (in allele DPA1*03:01 and allele DPA1*03:03; FT dbSNP:rs2308917)" FT /id="VAR_047687" FT VARIANT 100 FT /note="N -> D (in allele DPA1*02:04; dbSNP:rs61759929)" FT /id="VAR_058839" FT VARIANT 103 FT /note="T -> I (in allele DPA1*04:01; dbSNP:rs41559316)" FT /id="VAR_058840" FT VARIANT 104 FT /note="L -> A (in allele DPA1*04:01; requires 2 nucleotide FT substitutions)" FT /id="VAR_058841" FT VARIANT 114 FT /note="T -> A (in allele DPA1*01:05, allele DPA1*02:01, FT allele DPA1*02:02, allele DPA1*02:03, allele DPA1*02:04 and FT allele DPA1*04:01; dbSNP:rs1126542)" FT /id="VAR_047688" FT VARIANT 127 FT /note="P -> A (in allele DPA1*04:01; dbSNP:rs41562016)" FT /id="VAR_058842" FT VARIANT 142 FT /note="K -> R (in allele DPA1*02:01 and allele DPA1*02:02; FT dbSNP:rs1042190)" FT /id="VAR_047689" FT VARIANT 158 FT /note="L -> P (in allele DPA1*02:01, allele DPA1*02:02 and FT allele DPA1*04:01; dbSNP:rs2308930)" FT /id="VAR_058843" FT VARIANT 191 FT /note="F -> V (in allele DPA1*02:01, allele DPA1*02:02 and FT allele DPA1*04:01; dbSNP:rs1042308)" FT /id="VAR_047690" FT VARIANT 221 FT /note="T -> A (in allele DPA1*04:01; dbSNP:rs17509489)" FT /id="VAR_058844" FT VARIANT 259 FT /note="T -> P (in allele DPA1*02:01, allele DPA1*02:02 and FT allele DPA1*04:01; dbSNP:rs1126769)" FT /id="VAR_058845" FT CONFLICT 237 FT /note="I -> F (in Ref. 7; CAA25143)" FT /evidence="ECO:0000305" FT STRAND 35..49 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 51..57 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 60..66 FT /evidence="ECO:0007829|PDB:4P5M" FT TURN 67..70 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 71..76 FT /evidence="ECO:0007829|PDB:4P5M" FT HELIX 77..82 FT /evidence="ECO:0007829|PDB:4P5M" FT HELIX 87..107 FT /evidence="ECO:0007829|PDB:4P5M" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 119..126 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 134..146 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 149..154 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 176..184 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 191..197 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:4P5M" FT STRAND 205..210 FT /evidence="ECO:0007829|PDB:4P5M" SQ SEQUENCE 260 AA; 29381 MW; 826174E963A8CB42 CRC64; MRPEDRMFHI RAVILRALSL AFLLSLRGAG AIKADHVSTY AAFVQTHRPT GEFMFEFDED EMFYVDLDKK ETVWHLEEFG QAFSFEAQGG LANIAILNNN LNTLIQRSNH TQATNDPPEV TVFPKEPVEL GQPNTLICHI DKFFPPVLNV TWLCNGELVT EGVAESLFLP RTDYSFHKFH YLTFVPSAED FYDCRVEHWG LDQPLLKHWE AQEPIQMPET TETVLCALGL VLGLVGIIVG TVLIIKSLRS GHDPRAQGTL //