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HLA class II histocompatibility antigen, DO alpha chain (MHC DN-alpha) (MHC DZ alpha) (MHC class II antigen DOA)

 DOA_HUMAN               Reviewed;         250 AA.
P06340; Q58HU0; Q58HU1; Q5STC7; Q9TQC6; Q9TQC7; Q9TQC8; Q9TQC9;
Q9TQD0; Q9TQD1; Q9TQD2; Q9TQD3;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
28-FEB-2018, entry version 156.
RecName: Full=HLA class II histocompatibility antigen, DO alpha chain;
AltName: Full=MHC DN-alpha;
AltName: Full=MHC DZ alpha;
AltName: Full=MHC class II antigen DOA;
Flags: Precursor;
Name=HLA-DOA; Synonyms=HLA-DNA, HLA-DZA;
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 DOA*01:01).
PubMed=3000765;
Trowsdale J., Kelly A.;
"The human HLA class II alpha chain gene DZ alpha is distinct from
genes in the DP, DQ and DR subregions.";
EMBO J. 4:2231-2237(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DOA*01:01).
PubMed=2499532; DOI=10.1007/BF00375872;
Jonsson A.-K., Rask L.;
"Human class II DNA and DOB genes display low sequence variability.";
Immunogenetics 29:411-413(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DOA*01:01).
PubMed=2370084; DOI=10.1007/BF02115015;
Young J.A., Trowsdale J.;
"The HLA-DNA (DZA) gene is correctly expressed as a 1.1 kb mature mRNA
transcript.";
Immunogenetics 31:386-388(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DOA*01:01; DOA*01:02 AND
DOA*01:03).
PubMed=16101837; DOI=10.1111/j.1399-0039.2005.00446.x;
Moon S.-M., Gu H., Ryu H.-J., Kim J.-J., Kim H.-T., Han B.G., Kimm K.,
Lee J.-K., Oh B.;
"Identification of four novel HLA-DOA alleles, DOA*010106, DOA*0102,
DOA*0103, and DOA*0104N, by sequence-based typing.";
Tissue Antigens 66:242-245(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DOA*01:01).
TISSUE=Lung;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DOA*01:01).
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DOA*01:01).
Mural R.J., Istrail S., Sutton G.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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DOA*01:01).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-250 (ALLELE DOA*01:01).
PubMed=10323340; DOI=10.1034/j.1399-0039.1999.530406.x;
Naruse T.K., Kawata H., Anzai T., Takashige N., Kagiya M., Nose Y.,
Nabeya N., Isshiki G., Tatsumi N., Inoko H.;
"Limited polymorphism in the HLA-DOA gene.";
Tissue Antigens 53:359-365(1999).
[10]
REVIEW.
PubMed=10837054; DOI=10.1146/annurev.immunol.18.1.113;
Alfonso C., Karlsson L.;
"Nonclassical MHC class II molecules.";
Annu. Rev. Immunol. 18:113-142(2000).
-!- FUNCTION: Important modulator in the HLA class II restricted
antigen presentation pathway by interaction with the HLA-DM
molecule in B-cells. Modifies peptide exchange activity of HLA-DM.
-!- SUBUNIT: Heterodimer of an alpha chain (DOA) and a beta chain
(DOB). Forms a heterotetrameric complex with an HLA-DM molecule
during intracellular transport in endosomal/lysosomal compartments
in B-cells.
-!- INTERACTION:
Q04864:REL; NbExp=3; IntAct=EBI-10194851, EBI-307352;
-!- SUBCELLULAR LOCATION: Endosome membrane; Single-pass type I
membrane protein. Lysosome membrane; Single-pass type I membrane
protein. Note=Complexes with HLA-DM molecule during intracellular
transport and in endosomal/lysosomal compartments.
Heterotetramerization is necessary to exit the ER.
-!- POLYMORPHISM: The following alleles of DOA are known: DOA*01:01,
DOA*01:02 and DOA*01:03. The sequence shown is that of DOA*01:01.
-!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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EMBL; X02882; CAA26635.1; -; Genomic_DNA.
EMBL; M26039; AAA59716.1; -; mRNA.
EMBL; M31525; AAA60075.1; -; mRNA.
EMBL; AY947479; AAX49509.1; -; mRNA.
EMBL; AY947480; AAX49510.1; -; mRNA.
EMBL; AY947481; AAX49511.1; -; mRNA.
EMBL; AK290714; BAF83403.1; -; mRNA.
EMBL; AK313551; BAG36327.1; -; mRNA.
EMBL; Z81310; CAB03594.1; -; Genomic_DNA.
EMBL; AL662845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL645931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL805913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX005422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR936909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03668.1; -; Genomic_DNA.
EMBL; BC013183; AAH13183.1; -; mRNA.
EMBL; AB005991; BAA81787.1; -; Genomic_DNA.
EMBL; AB005992; BAA81788.1; -; Genomic_DNA.
EMBL; AB005993; BAA81789.1; -; Genomic_DNA.
EMBL; AB005994; BAA81790.1; -; Genomic_DNA.
EMBL; AB005995; BAA81791.1; -; Genomic_DNA.
EMBL; AB005996; BAA81792.1; -; Genomic_DNA.
EMBL; AB005997; BAA81793.1; -; Genomic_DNA.
EMBL; AB005998; BAA81794.1; -; Genomic_DNA.
CCDS; CCDS4763.1; -.
PIR; A02216; HLHUDZ.
RefSeq; NP_002110.1; NM_002119.3.
UniGene; Hs.631991; -.
PDB; 4I0P; X-ray; 3.20 A; C/G=27-207.
PDBsum; 4I0P; -.
ProteinModelPortal; P06340; -.
SMR; P06340; -.
BioGrid; 109356; 3.
DIP; DIP-60116N; -.
IntAct; P06340; 4.
STRING; 9606.ENSP00000229829; -.
iPTMnet; P06340; -.
PhosphoSitePlus; P06340; -.
BioMuta; HLA-DOA; -.
DMDM; 122210; -.
EPD; P06340; -.
PaxDb; P06340; -.
PeptideAtlas; P06340; -.
PRIDE; P06340; -.
DNASU; 3111; -.
Ensembl; ENST00000229829; ENSP00000229829; ENSG00000204252.
Ensembl; ENST00000383226; ENSP00000372713; ENSG00000206292.
Ensembl; ENST00000426070; ENSP00000401504; ENSG00000231558.
Ensembl; ENST00000426685; ENSP00000397945; ENSG00000232957.
Ensembl; ENST00000434335; ENSP00000416448; ENSG00000232962.
Ensembl; ENST00000438987; ENSP00000395737; ENSG00000230141.
Ensembl; ENST00000452598; ENSP00000398819; ENSG00000235744.
GeneID; 3111; -.
KEGG; hsa:3111; -.
CTD; 3111; -.
DisGeNET; 3111; -.
EuPathDB; HostDB:ENSG00000204252.12; -.
GeneCards; HLA-DOA; -.
HGNC; HGNC:4936; HLA-DOA.
HPA; HPA045038; -.
MIM; 142930; gene.
neXtProt; NX_P06340; -.
OpenTargets; ENSG00000204252; -.
PharmGKB; PA35060; -.
eggNOG; ENOG410IM01; Eukaryota.
eggNOG; ENOG4111C4S; LUCA.
GeneTree; ENSGT00900000140882; -.
HOVERGEN; HBG006862; -.
InParanoid; P06340; -.
KO; K06752; -.
OMA; DHMGSYG; -.
OrthoDB; EOG093711AM; -.
PhylomeDB; P06340; -.
TreeFam; TF333797; -.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
SIGNOR; P06340; -.
ChiTaRS; HLA-DOA; human.
GeneWiki; HLA-DOA; -.
GenomeRNAi; 3111; -.
PRO; PR:P06340; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204252; -.
ExpressionAtlas; P06340; baseline and differential.
Genevisible; P06340; HS.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:ProtInc.
GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IDA:UniProtKB.
GO; GO:0045580; P:regulation of T cell differentiation; IEA:Ensembl.
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; Complete proteome; Disulfide bond; Endosome;
Glycoprotein; Immunity; Lysosome; Membrane; MHC II; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 250 HLA class II histocompatibility antigen,
DO alpha chain.
/FTId=PRO_0000018962.
TOPO_DOM 26 217 Extracellular. {ECO:0000255}.
TRANSMEM 218 240 Helical. {ECO:0000255}.
TOPO_DOM 241 250 Cytoplasmic. {ECO:0000255}.
DOMAIN 113 205 Ig-like C1-type.
REGION 26 110 Alpha-1.
REGION 111 204 Alpha-2.
REGION 205 217 Connecting peptide.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 133 189 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 99 99 L -> V (in allele DOA*01:03;
dbSNP:rs41542323).
/FTId=VAR_058126.
VARIANT 105 105 R -> C (in allele DOA*01:02;
dbSNP:rs11575906).
/FTId=VAR_058127.
STRAND 29 40 {ECO:0000244|PDB:4I0P}.
HELIX 42 44 {ECO:0000244|PDB:4I0P}.
STRAND 45 52 {ECO:0000244|PDB:4I0P}.
STRAND 55 61 {ECO:0000244|PDB:4I0P}.
TURN 62 65 {ECO:0000244|PDB:4I0P}.
STRAND 66 71 {ECO:0000244|PDB:4I0P}.
HELIX 72 74 {ECO:0000244|PDB:4I0P}.
STRAND 77 80 {ECO:0000244|PDB:4I0P}.
HELIX 87 94 {ECO:0000244|PDB:4I0P}.
HELIX 96 102 {ECO:0000244|PDB:4I0P}.
STRAND 114 121 {ECO:0000244|PDB:4I0P}.
STRAND 129 141 {ECO:0000244|PDB:4I0P}.
STRAND 144 149 {ECO:0000244|PDB:4I0P}.
STRAND 152 154 {ECO:0000244|PDB:4I0P}.
STRAND 171 179 {ECO:0000244|PDB:4I0P}.
STRAND 187 192 {ECO:0000244|PDB:4I0P}.
STRAND 196 198 {ECO:0000244|PDB:4I0P}.
STRAND 200 204 {ECO:0000244|PDB:4I0P}.
SEQUENCE 250 AA; 27599 MW; FA9482197A02AC85 CRC64;
MALRAGLVLG FHTLMTLLSP QEAGATKADH MGSYGPAFYQ SYGASGQFTH EFDEEQLFSV
DLKKSEAVWR LPEFGDFARF DPQGGLAGIA AIKAHLDILV ERSNRSRAIN VPPRVTVLPK
SRVELGQPNI LICIVDNIFP PVINITWLRN GQTVTEGVAQ TSFYSQPDHL FRKFHYLPFV
PSAEDVYDCQ VEHWGLDAPL LRHWELQVPI PPPDAMETLV CALGLAIGLV GFLVGTVLII
MGTYVSSVPR


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