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Database: UniProt
Entry: P20036
LinkDB: P20036
Original site: P20036 
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   07-APR-2021, entry version 183.
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;
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   -!- 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};
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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_001242524.1.
DR   RefSeq; NP_001229454.1; NM_001242525.1.
DR   RefSeq; NP_291032.2; NM_033554.3.
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   PDBsum; 3LQZ; -.
DR   PDBsum; 4P4K; -.
DR   PDBsum; 4P4R; -.
DR   PDBsum; 4P57; -.
DR   PDBsum; 4P5K; -.
DR   PDBsum; 4P5M; -.
DR   SMR; P20036; -.
DR   BioGRID; 109358; 104.
DR   IntAct; P20036; 67.
DR   MINT; P20036; -.
DR   STRING; 9606.ENSP00000393566; -.
DR   GlyConnect; 1365; 1 N-Linked glycan (1 site).
DR   GlyGen; P20036; 3 sites.
DR   iPTMnet; P20036; -.
DR   PhosphoSitePlus; P20036; -.
DR   BioMuta; HLA-DPA1; -.
DR   DMDM; 122204; -.
DR   jPOST; P20036; -.
DR   MassIVE; P20036; -.
DR   PaxDb; P20036; -.
DR   PeptideAtlas; P20036; -.
DR   PRIDE; P20036; -.
DR   ProteomicsDB; 53716; -.
DR   Antibodypedia; 45587; 305 antibodies.
DR   DNASU; 3113; -.
DR   Ensembl; ENST00000374808; ENSP00000363941; ENSG00000168384.
DR   Ensembl; ENST00000383224; ENSP00000372711; ENSG00000206291.
DR   Ensembl; ENST00000415247; ENSP00000405838; ENSG00000224103.
DR   Ensembl; ENST00000419277; ENSP00000393566; ENSG00000231389.
DR   Ensembl; ENST00000422504; ENSP00000406250; ENSG00000228163.
DR   Ensembl; ENST00000443117; ENSP00000397587; ENSG00000235844.
DR   Ensembl; ENST00000454805; ENSP00000397139; ENSG00000229685.
DR   Ensembl; ENST00000515317; ENSP00000427429; ENSG00000236177.
DR   GeneID; 3113; -.
DR   KEGG; hsa:3113; -.
DR   CTD; 3113; -.
DR   DisGeNET; 3113; -.
DR   GeneCards; HLA-DPA1; -.
DR   HGNC; HGNC:4938; HLA-DPA1.
DR   HPA; ENSG00000231389; Tissue enhanced (blood).
DR   MalaCards; HLA-DPA1; -.
DR   MIM; 142880; gene.
DR   neXtProt; NX_P20036; -.
DR   NIAGADS; ENSG00000231389; -.
DR   OpenTargets; ENSG00000231389; -.
DR   PharmGKB; PA35062; -.
DR   VEuPathDB; HostDB:ENSG00000231389.7; -.
DR   eggNOG; ENOG502RXYJ; Eukaryota.
DR   GeneTree; ENSGT00940000162498; -.
DR   HOGENOM; CLU_069380_0_0_1; -.
DR   InParanoid; P20036; -.
DR   OMA; TVWHLPE; -.
DR   OrthoDB; 1132781at2759; -.
DR   PhylomeDB; P20036; -.
DR   TreeFam; TF333797; -.
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; PD-1 signaling.
DR   Reactome; R-HSA-877300; Interferon gamma signaling.
DR   SIGNOR; P20036; -.
DR   BioGRID-ORCS; 3113; 4 hits in 972 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 visceral pleura and 246 other tissues.
DR   ExpressionAtlas; P20036; baseline and differential.
DR   Genevisible; P20036; HS.
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:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
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:0032395; F:MHC class II receptor activity; NAS:UniProtKB.
DR   GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
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 interferon-gamma; IDA:UniProtKB.
DR   GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR   GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
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:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
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; Adaptive immunity; Cell membrane; Disulfide bond;
KW   Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Immunity;
KW   Lysosome; Membrane; MHC II; Reference proteome; Signal; Transmembrane;
KW   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:0007744|PDB:4P5M"
FT   STRAND          51..57
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   STRAND          60..66
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   TURN            67..70
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   STRAND          71..76
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   HELIX           77..82
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   HELIX           87..107
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   STRAND          119..126
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   STRAND          134..146
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   STRAND          149..154
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   STRAND          157..159
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   STRAND          161..165
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   STRAND          176..184
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   STRAND          191..197
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   STRAND          201..203
FT                   /evidence="ECO:0007744|PDB:4P5M"
FT   STRAND          205..210
FT                   /evidence="ECO:0007744|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
//
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