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HLA class II histocompatibility antigen, DP alpha 1 chain (DP(W3)) (DP(W4)) (HLA-SB alpha chain) (MHC class II DP3-alpha) (MHC class II DPA1)

 DPA1_HUMAN              Reviewed;         260 AA.
P20036; A9YWH7; B9UKH4; O19722; O46883; P01905; P79554; Q2Q060;
Q2Q061; Q5EY03; Q5STP1; Q6DQK4; Q9BCQ1; Q9TPX3; Q9XS10;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
25-OCT-2017, entry version 157.
RecName: Full=HLA class II histocompatibility antigen, DP alpha 1 chain;
AltName: Full=DP(W3);
AltName: Full=DP(W4);
AltName: Full=HLA-SB alpha chain;
AltName: Full=MHC class II DP3-alpha;
AltName: Full=MHC class II DPA1;
Flags: Precursor;
Name=HLA-DPA1; Synonyms=HLA-DP1A, HLASB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DPA1*01:03).
PubMed=2997750; DOI=10.1093/nar/13.20.7515;
Lawrance S.K., Das H.K., Pan J., Weissman S.M.;
"The genomic organisation and nucleotide sequence of the HLA-SB(DP)
alpha gene.";
Nucleic Acids Res. 13:7515-7528(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DPA1*01:03).
PubMed=3036829;
Gustafsson K., Widmark E., Jonsson A.-K., Servenius B., Sachs D.H.,
Larhammar D., Rask L., Peterson P.A.;
"Class II genes of the human major histocompatibility complex.
Evolution of the DP region as deduced from nucleotide sequences of the
four genes.";
J. Biol. Chem. 262:8778-8786(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DPA1*01:03).
PubMed=2461352; DOI=10.1016/0198-8859(88)90016-X;
Young J.A., Lindsay J., Bodmer J.G., Trowsdale J.;
"Epitope recognition by a DP alpha chain-specific monoclonal antibody
(DP11.1) is influenced by the interaction between the DP alpha chain
and its polymorphic DP beta chain partner.";
Hum. Immunol. 23:37-44(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DPA1*01:03).
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 28-260 (ALLELE DPA1*01:03).
PubMed=6584734; DOI=10.1038/308327a0;
Auffray C., Lillie J.W., Arnot D., Grossberger D., Kappes D.,
Strominger J.L.;
"Isotypic and allotypic variation of human class II histocompatibility
antigen alpha-chain genes.";
Nature 308:327-333(1984).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-115 (ALLELE DPA1*02:03).
PubMed=9234495; DOI=10.1111/j.1399-0039.1997.tb02821.x;
Muntau B., Thye T., Pirmez C., Horstmann R.D.;
"A novel DPA1 allele (DPA1*0203) composed of known epitopes.";
Tissue Antigens 49:668-669(1997).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-115 (ALLELE DPA1*03:02).
PubMed=9694359; DOI=10.1111/j.1399-0039.1998.tb03009.x;
Steiner L.L., Cavalli A., Zimmerman P.A., Boatin B.A., Titanji V.P.,
Bradley J.E., Lucius R., Nutman T.B., Begovich A.B.;
"Three new DP alleles identified in sub-Saharan Africa: DPB1*7401,
DPA1*02013, and DPA1*0302.";
Tissue Antigens 51:653-657(1998).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-116 AND 211-260 (ALLELE
DPA1*01:04), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-229 (ALLELE
DPA1*02:01), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-116 AND 211-260
(ALLELE DPA1*02:02), AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-115
AND 211-260 (ALLELES DPA1*03:01 AND DPA1*401).
PubMed=7725312; DOI=10.1111/j.1399-0039.1995.tb02415.x;
Rozemuller E.H., Bouwens A.G., van Oort E., Versluis L.F., Marsh S.G.,
Bodmer J.G., Tilanus M.G.;
"Sequencing-based typing reveals new insight in HLA-DPA1
polymorphism.";
Tissue Antigens 45:57-62(1995).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-117 (ALLELE DPA1*02:01).
PubMed=11019928; DOI=10.1034/j.1399-0039.2000.560219.x;
McDaniel D.O., Nguyen C., McDaniel L.S.;
"A new HLA-DPA1 allele, DPA1*02016, identified in African-American
population.";
Tissue Antigens 56:197-198(2000).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*03:03).
PubMed=15663751; DOI=10.1111/j.1399-0039.2005.00339.x;
Luo M., Bamforth J., Gill K., Cohen C., Brunham R.C., Plummer F.A.;
"High-resolution sequence-based DPA1 typing identified two novel DPA1
alleles, DPA1*010303 and DPA1*0303, from a Kenyan population.";
Tissue Antigens 65:120-122(2005).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*01:06).
PubMed=18838095; DOI=10.1016/j.humimm.2008.09.001;
Peterson T.A., Luo M., Mao X., Brunham R.C., Plummer F.A.;
"Identification of a novel DPA1 allele, DPA1*010602, in an East
African population.";
Hum. Immunol. 69:885-886(2008).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELES DPA1*01:03 AND
DPA1*01:10).
PubMed=18380777; DOI=10.1111/j.1399-0039.2008.01035.x;
Lee K.W.;
"Description of two novel HLA-DPA1 alleles: DPA1*0110 and
DPA1*010304.";
Tissue Antigens 71:575-577(2008).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*02:04).
PubMed=18489436; DOI=10.1111/j.1399-0039.2008.01046.x;
Zhao H., Dai W.-J., He Y.-M., Zhu F.-M., Yan L.-X.;
"A novel HLA-DPA1*0204 allele was identified in a Chinese
individual.";
Tissue Antigens 71:577-578(2008).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*01:06).
Steiner L., Begovich A., Suraj V.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*01:08).
Grams S.E., Begovich A., Mangaccat J.;
"One new DPA1 Allele.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DPA1*01:09).
Bassinger S., Wu J., Williams T.M.;
"Novel human HLA-DPA1 allele identified in potential bone marrow
donors.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[19]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-115 (ALLELE DPA1*01:07).
Varney M.D., Gavrilidis A., Abbott W.;
"DPA1 polymorphism in Polynesians.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[20]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-115 (ALLELE DPA1*01:05).
PubMed=8988544; DOI=10.1111/j.1399-0039.1996.tb02675.x;
May J., Krestchmer C., Schnittger L., Striecker R., Kremoner P.G.,
Meyer C.G.;
"DPA1*0105, a novel DPA1 variant in a negrois population.";
Tissue Antigens 48:593-594(1996).
[21]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-210 (ALLELES DPA1*01:04;
DPA1*02:02; DPA1*03:01 AND DPA1*04:01).
PubMed=7806277; DOI=10.1007/BF00188437;
Rozemuller E.H., Versluis L.F., Bouwens A.G., Tilanus M.G.;
"Exon 2, 3, and 4 polymorphism of HLA-DPA1.";
Immunogenetics 41:53-53(1995).
[22]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 178-209 (ALLELE DPA1*01:03).
PubMed=6300884; DOI=10.1073/pnas.80.7.1972;
Trowsdale J., Lee J., Carey J., Grosveld F., Bodmer J., Bodmer W.;
"Sequences related to HLA-DR alpha chain on human chromosome 6:
restriction enzyme polymorphism detected with DC alpha chain probes.";
Proc. Natl. Acad. Sci. U.S.A. 80:1972-1976(1983).
[23]
REVIEW.
PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9;
Cresswell P.;
"Invariant chain structure and MHC class II function.";
Cell 84:505-507(1996).
[24]
REVIEW.
PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4;
Villadangos J.A.;
"Presentation of antigens by MHC class II molecules: getting the most
out of them.";
Mol. Immunol. 38:329-346(2001).
[25]
REVIEW.
PubMed=18046453; DOI=10.1038/sj.emboj.7601945;
Rocha N., Neefjes J.;
"MHC class II molecules on the move for successful antigen
presentation.";
EMBO J. 27:1-5(2008).
[26]
REVIEW.
PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005;
Menendez-Benito V., Neefjes J.;
"Autophagy in MHC class II presentation: sampling from within.";
Immunity 26:1-3(2007).
[27]
REVIEW.
PubMed=19092054; DOI=10.1242/jcs.035089;
Berger A.C., Roche P.A.;
"MHC class II transport at a glance.";
J. Cell Sci. 122:1-4(2009).
[28]
REVIEW.
PubMed=19533806; DOI=10.3748/wjg.15.2855;
Beswick E.J., Reyes V.E.;
"CD74 in antigen presentation, inflammation, and cancers of the
gastrointestinal tract.";
World J. Gastroenterol. 15:2855-2861(2009).
[29]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-149.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Binds peptides derived from antigens that access the
endocytic route of antigen presenting cells (APC) and presents
them on the cell surface for recognition by the CD4 T-cells. The
peptide binding cleft accommodates peptides of 10-30 residues. The
peptides presented by MHC class II molecules are generated mostly
by degradation of proteins that access the endocytic route, where
they are processed by lysosomal proteases and other hydrolases.
Exogenous antigens that have been endocytosed by the APC are thus
readily available for presentation via MHC II molecules, and for
this reason this antigen presentation pathway is usually referred
to as exogenous. As membrane proteins on their way to degradation
in lysosomes as part of their normal turn-over are also contained
in the endosomal/lysosomal compartments, exogenous antigens must
compete with those derived from endogenous components. Autophagy
is also a source of endogenous peptides, autophagosomes
constitutively fuse with MHC class II loading compartments. In
addition to APCs, other cells of the gastrointestinal tract, such
as epithelial cells, express MHC class II molecules and CD74 and
act as APCs, which is an unusual trait of the GI tract. To produce
a MHC class II molecule that presents an antigen, three MHC class
II molecules (heterodimers of an alpha and a beta chain) associate
with a CD74 trimer in the ER to form a heterononamer. Soon after
the entry of this complex into the endosomal/lysosomal system
where antigen processing occurs, CD74 undergoes a sequential
degradation by various proteases, including CTSS and CTSL, leaving
a small fragment termed CLIP (class-II-associated invariant chain
peptide). The removal of CLIP is facilitated by HLA-DM via direct
binding to the alpha-beta-CLIP complex so that CLIP is released.
HLA-DM stabilizes MHC class II molecules until primary high
affinity antigenic peptides are bound. The MHC II molecule bound
to a peptide is then transported to the cell membrane surface. In
B-cells, the interaction between HLA-DM and MHC class II molecules
is regulated by HLA-DO. Primary dendritic cells (DCs) also to
express HLA-DO. Lysosomal microenvironment has been implicated in
the regulation of antigen loading into MHC II molecules, increased
acidification produces increased proteolysis and efficient peptide
loading.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred
as MHC class II molecule. In the endoplasmic reticulum (ER) it
forms a heterononamer; 3 MHC class II molecules bind to a CD74
homotrimer (also known as invariant chain or HLA class II
histocompatibility antigen gamma chain). In the
endosomal/lysosomal system; CD74 undergoes sequential degradation
by various proteases; leaving a small fragment termed CLIP on each
MHC class II molecule. MHC class II molecule interacts with
HLA_DM, and HLA_DO in B-cells, in order to release CLIP and
facilitate the binding of antigenic peptides.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Endoplasmic reticulum membrane; Single-pass type I
membrane protein. Golgi apparatus, trans-Golgi network membrane;
Single-pass type I membrane protein. Endosome membrane; Single-
pass type I membrane protein. Lysosome membrane; Single-pass type
I membrane protein. Note=The MHC class II complex transits through
a number of intracellular compartments in the endocytic pathway
until it reaches the cell membrane for antigen presentation.
-!- POLYMORPHISM: The following alleles of DPA1 are known: DPA1*01:03,
DPA1*01:04, DPA1*01:05, DPA1*01:06, DPA1*01:07, DPA1*01:08,
DPA1*01:09, DPA1*01:10, DPA1*02:01, DPA1*02:02, DPA1*02:03,
DPA1*02:04, DPA1*03:01, DPA1*03:02, DPA1*03:03, DPA1*04:01 The
sequence shown is that of DPA1*01:03.
-!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC64233.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAD42927.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X03100; CAA26887.1; -; Genomic_DNA.
EMBL; M27487; AAA63220.1; -; mRNA.
EMBL; AK292709; BAF85398.1; -; mRNA.
EMBL; AL645931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL805913; CAI18549.1; -; Genomic_DNA.
EMBL; BX120009; CAM25981.1; -; Genomic_DNA.
EMBL; BX005422; CAM25981.1; JOINED; Genomic_DNA.
EMBL; BX005422; CAM26119.1; -; Genomic_DNA.
EMBL; BX120009; CAM26119.1; JOINED; Genomic_DNA.
EMBL; CR759829; CAQ07261.1; -; Genomic_DNA.
EMBL; CR762479; CAQ07261.1; JOINED; Genomic_DNA.
EMBL; CR759795; CAQ07433.1; -; Genomic_DNA.
EMBL; CR847849; CAQ07485.1; -; Genomic_DNA.
EMBL; CR759904; CAQ09865.1; -; Genomic_DNA.
EMBL; CR762479; CAQ10344.1; -; Genomic_DNA.
EMBL; CR759829; CAQ10344.1; JOINED; Genomic_DNA.
EMBL; CH471081; EAX03669.1; -; Genomic_DNA.
EMBL; X00457; CAA25143.1; -; mRNA.
EMBL; Z48473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF013767; AAC64233.1; ALT_SEQ; Genomic_DNA.
EMBL; X78199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X82393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X82394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X78198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X82391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X79475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X79477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X79479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X79481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF165160; AAD47826.1; -; Genomic_DNA.
EMBL; AY618553; AAT92097.1; -; Genomic_DNA.
EMBL; EU729350; ACH88749.1; -; Genomic_DNA.
EMBL; DQ274060; ABB88406.1; -; Genomic_DNA.
EMBL; DQ274061; ABB88407.1; -; Genomic_DNA.
EMBL; EU304462; ABY27081.1; -; Genomic_DNA.
EMBL; U87556; AAB97110.1; -; Genomic_DNA.
EMBL; AF346471; AAK27152.1; -; Genomic_DNA.
EMBL; AY650051; AAT67468.1; -; Genomic_DNA.
EMBL; AF076284; AAD42927.1; ALT_SEQ; Genomic_DNA.
EMBL; X96984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X80482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X81347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X81348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; K00514; AAA59786.1; -; Genomic_DNA.
CCDS; CCDS4764.1; -.
PIR; A29313; HLHUSB.
RefSeq; NP_001229453.1; NM_001242524.1.
RefSeq; NP_001229454.1; NM_001242525.1.
RefSeq; NP_291032.2; NM_033554.3.
UniGene; Hs.347270; -.
PDB; 3LQZ; X-ray; 3.25 A; A=32-212.
PDB; 4P4K; X-ray; 2.80 A; A/E=32-214.
PDB; 4P4R; X-ray; 3.00 A; A/C=32-214.
PDB; 4P57; X-ray; 2.60 A; A/C=32-214.
PDB; 4P5K; X-ray; 2.59 A; A/D=32-214.
PDB; 4P5M; X-ray; 1.70 A; A/C/E/G=32-214.
PDBsum; 3LQZ; -.
PDBsum; 4P4K; -.
PDBsum; 4P4R; -.
PDBsum; 4P57; -.
PDBsum; 4P5K; -.
PDBsum; 4P5M; -.
ProteinModelPortal; P20036; -.
SMR; P20036; -.
BioGrid; 109358; 101.
IntAct; P20036; 4.
MINT; MINT-1488672; -.
STRING; 9606.ENSP00000393566; -.
iPTMnet; P20036; -.
PhosphoSitePlus; P20036; -.
BioMuta; HLA-DPA1; -.
DMDM; 122204; -.
EPD; P20036; -.
PaxDb; P20036; -.
PeptideAtlas; P20036; -.
PRIDE; P20036; -.
DNASU; 3113; -.
Ensembl; ENST00000374808; ENSP00000363941; ENSG00000168384.
Ensembl; ENST00000383224; ENSP00000372711; ENSG00000206291.
Ensembl; ENST00000415247; ENSP00000405838; ENSG00000224103.
Ensembl; ENST00000419277; ENSP00000393566; ENSG00000231389.
Ensembl; ENST00000422504; ENSP00000406250; ENSG00000228163.
Ensembl; ENST00000443117; ENSP00000397587; ENSG00000235844.
Ensembl; ENST00000454805; ENSP00000397139; ENSG00000229685.
Ensembl; ENST00000515317; ENSP00000427429; ENSG00000236177.
GeneID; 3113; -.
KEGG; hsa:3113; -.
CTD; 3113; -.
DisGeNET; 3113; -.
EuPathDB; HostDB:ENSG00000231389.7; -.
GeneCards; HLA-DPA1; -.
HGNC; HGNC:4938; HLA-DPA1.
HPA; HPA017967; -.
MIM; 142880; gene.
neXtProt; NX_P20036; -.
OpenTargets; ENSG00000231389; -.
PharmGKB; PA35062; -.
eggNOG; ENOG410IZMF; Eukaryota.
eggNOG; ENOG410YHX9; LUCA.
GeneTree; ENSGT00900000140882; -.
HOVERGEN; HBG006862; -.
InParanoid; P20036; -.
KO; K06752; -.
OMA; DYSFHKF; -.
OrthoDB; EOG09370Q7A; -.
PhylomeDB; P20036; -.
TreeFam; TF333797; -.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-389948; PD-1 signaling.
Reactome; R-HSA-877300; Interferon gamma signaling.
SIGNOR; P20036; -.
ChiTaRS; HLA-DPA1; human.
EvolutionaryTrace; P20036; -.
GenomeRNAi; 3113; -.
PRO; PR:P20036; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000231389; -.
CleanEx; HS_HLA-DPA1; -.
ExpressionAtlas; P20036; baseline and differential.
Genevisible; P20036; HS.
GO; GO:0009986; C:cell surface; IMP:UniProtKB.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
GO; GO:0032395; F:MHC class II receptor activity; NAS:UniProtKB.
GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
GO; GO:0050870; P:positive regulation of T cell activation; IMP:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.320.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR014745; MHC_II_a/b_N.
InterPro; IPR001003; MHC_II_a_N.
Pfam; PF07654; C1-set; 1.
Pfam; PF00993; MHC_II_alpha; 1.
SMART; SM00407; IGc1; 1.
SMART; SM00920; MHC_II_alpha; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus;
Immunity; Lysosome; Membrane; MHC II; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 28
CHAIN 29 260 HLA class II histocompatibility antigen,
DP alpha 1 chain.
/FTId=PRO_0000018967.
TOPO_DOM 29 222 Extracellular. {ECO:0000255}.
TRANSMEM 223 245 Helical. {ECO:0000255}.
TOPO_DOM 246 260 Cytoplasmic. {ECO:0000255}.
DOMAIN 118 210 Ig-like C1-type.
REGION 29 115 Alpha-1.
REGION 116 209 Alpha-2.
REGION 210 222 Connecting peptide.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 149 149 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 138 194 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 42 42 A -> M (in allele DPA1*02:02, allele
DPA1*02:04, allele DPA1*03:01, allele
DPA1*03:02 and allele DPA1*03:03;
requires 2 nucleotide substitutions;
dbSNP:rs386699859).
/FTId=VAR_058832.
VARIANT 42 42 A -> T (in dbSNP:rs1126533).
/FTId=VAR_047683.
VARIANT 42 42 A -> V (in dbSNP:rs1126534).
/FTId=VAR_047684.
VARIANT 49 49 P -> T (in allele DPA1*04:01;
dbSNP:rs2308907).
/FTId=VAR_058833.
VARIANT 54 54 M -> T (in allele DPA1*01:09;
dbSNP:rs1042175).
/FTId=VAR_058834.
VARIANT 59 59 E -> D (in allele DPA1*01:04, allele
DPA1*01:08, allele DPA1*03:03 and allele
DPA1*04:01; dbSNP:rs2308910).
/FTId=VAR_058835.
VARIANT 62 62 M -> K (in dbSNP:rs2308912).
/FTId=VAR_058836.
VARIANT 62 62 M -> L (in dbSNP:rs2308911).
/FTId=VAR_047685.
VARIANT 62 62 M -> Q (in allele DPA1*01:06, allele
DPA1*02:01, allele DPA1*02:02 and allele
DPA1*02:04; requires 2 nucleotide
substitutions; dbSNP:rs36013091).
/FTId=VAR_058850.
VARIANT 74 74 W -> C (in allele DPA1*01:10;
dbSNP:rs72558171).
/FTId=VAR_058837.
VARIANT 81 81 Q -> R (in allele DPA1*01:08, allele
DPA1*02:01, allele DPA1*02:02, allele
DPA1*02:03, allele DPA1*02:04 and allele
DPA1*04:01; dbSNP:rs1042178).
/FTId=VAR_047686.
VARIANT 82 82 A -> T (in allele DPA1*01:07;
dbSNP:rs41543112).
/FTId=VAR_058838.
VARIANT 97 97 L -> S (in allele DPA1*03:01 and allele
DPA1*03:03; dbSNP:rs2308917).
/FTId=VAR_047687.
VARIANT 100 100 N -> D (in allele DPA1*02:04;
dbSNP:rs61759929).
/FTId=VAR_058839.
VARIANT 103 103 T -> I (in allele DPA1*04:01;
dbSNP:rs41559316).
/FTId=VAR_058840.
VARIANT 104 104 L -> A (in allele DPA1*04:01; requires 2
nucleotide substitutions).
/FTId=VAR_058841.
VARIANT 114 114 T -> A (in allele DPA1*01:05, allele
DPA1*02:01, allele DPA1*02:02, allele
DPA1*02:03, allele DPA1*02:04 and allele
DPA1*04:01; dbSNP:rs1126542).
/FTId=VAR_047688.
VARIANT 127 127 P -> A (in allele DPA1*04:01;
dbSNP:rs41562016).
/FTId=VAR_058842.
VARIANT 142 142 K -> R (in allele DPA1*02:01 and allele
DPA1*02:02; dbSNP:rs1042190).
/FTId=VAR_047689.
VARIANT 158 158 L -> P (in allele DPA1*02:01, allele
DPA1*02:02 and allele DPA1*04:01;
dbSNP:rs2308930).
/FTId=VAR_058843.
VARIANT 191 191 F -> V (in allele DPA1*02:01, allele
DPA1*02:02 and allele DPA1*04:01;
dbSNP:rs1042308).
/FTId=VAR_047690.
VARIANT 221 221 T -> A (in allele DPA1*04:01;
dbSNP:rs17509489).
/FTId=VAR_058844.
VARIANT 259 259 T -> P (in allele DPA1*02:01, allele
DPA1*02:02 and allele DPA1*04:01;
dbSNP:rs1126769).
/FTId=VAR_058845.
CONFLICT 237 237 I -> F (in Ref. 7; CAA25143).
{ECO:0000305}.
STRAND 35 49 {ECO:0000244|PDB:4P5M}.
STRAND 51 57 {ECO:0000244|PDB:4P5M}.
STRAND 60 66 {ECO:0000244|PDB:4P5M}.
TURN 67 70 {ECO:0000244|PDB:4P5M}.
STRAND 71 76 {ECO:0000244|PDB:4P5M}.
HELIX 77 82 {ECO:0000244|PDB:4P5M}.
HELIX 87 107 {ECO:0000244|PDB:4P5M}.
STRAND 119 126 {ECO:0000244|PDB:4P5M}.
STRAND 134 146 {ECO:0000244|PDB:4P5M}.
STRAND 149 154 {ECO:0000244|PDB:4P5M}.
STRAND 157 159 {ECO:0000244|PDB:4P5M}.
STRAND 161 165 {ECO:0000244|PDB:4P5M}.
STRAND 176 184 {ECO:0000244|PDB:4P5M}.
STRAND 191 197 {ECO:0000244|PDB:4P5M}.
STRAND 201 203 {ECO:0000244|PDB:4P5M}.
STRAND 205 210 {ECO:0000244|PDB:4P5M}.
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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