DOB_HUMAN
ID DOB_HUMAN Reviewed; 273 AA.
AC P13765; B0V0Y0; Q29746; Q29825; Q6FHC2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=HLA class II histocompatibility antigen, DO beta chain;
DE AltName: Full=MHC class II antigen DOB;
DE Flags: Precursor;
GN Name=HLA-DOB;
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 [MRNA] (ALLELE DOB*01:01).
RX PubMed=2998758; DOI=10.1002/j.1460-2075.1985.tb04012.x;
RA Tonnelle C., Demars R., Long E.O.;
RT "DO beta: a new beta chain gene in HLA-D with a distinct regulation of
RT expression.";
RL EMBO J. 4:2839-2847(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DOB*01:01).
RX PubMed=2499532; DOI=10.1007/bf00375872;
RA Jonsson A.-K., Rask L.;
RT "Human class II DNA and DOB genes display low sequence variability.";
RL Immunogenetics 29:411-413(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DOB*01:01).
RX PubMed=1453454; DOI=10.1016/0022-2836(92)90832-5;
RA Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P., Trowsdale J.;
RT "DNA sequence analysis of 66 kb of the human MHC class II region encoding a
RT cluster of genes for antigen processing.";
RL J. Mol. Biol. 228:433-441(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-210.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-210.
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 MRNA] (ALLELE DOB*01:01).
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DOB*01:02).
RX PubMed=3036827; DOI=10.1016/s0021-9258(18)47481-9;
RA Servenius B., Rask L., Peterson P.A.;
RT "Class II genes of the human major histocompatibility complex. The DO beta
RT gene is a divergent member of the class II beta gene family.";
RL J. Biol. Chem. 262:8759-8766(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DOB*01:03).
RX PubMed=8568858; DOI=10.1006/jmbi.1996.0001;
RA Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., Hosking L.K.,
RA Jackson A., Kelly A., Newell W.R., Sanseau P., Radley E., Thorpe K.L.,
RA Trowsdale J.;
RT "Evolutionary dynamics of non-coding sequences within the class II region
RT of the human MHC.";
RL J. Mol. Biol. 255:1-13(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-273 (ALLELE DOB*01:04).
RX PubMed=12445321; DOI=10.1034/j.1399-0039.2002.590608.x;
RA Naruse T.K., Kawata H., Inoko H., Isshiki G., Yamano K., Hino M.,
RA Tatsumi N.;
RT "The HLA-DOB gene displays limited polymorphism with only one amino acid
RT substitution.";
RL Tissue Antigens 59:512-519(2002).
RN [10]
RP REVIEW.
RX PubMed=10837054; DOI=10.1146/annurev.immunol.18.1.113;
RA Alfonso C., Karlsson L.;
RT "Nonclassical MHC class II molecules.";
RL Annu. Rev. Immunol. 18:113-142(2000).
CC -!- FUNCTION: Important modulator in the HLA class II restricted antigen
CC presentation pathway by interaction with the HLA-DM molecule in B-
CC cells. Modifies peptide exchange activity of HLA-DM.
CC -!- SUBUNIT: Heterodimer of an alpha chain (DOA) and a beta chain (DOB).
CC Forms a heterotetrameric complex with an HLA-DM molecule during
CC intracellular transport in endosomal/lysosomal compartments in B-cells.
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Single-pass type I membrane
CC protein. Lysosome membrane; Single-pass type I membrane protein.
CC Note=Complexes with HLA-DM molecule during intracellular transport and
CC in endosomal/lysosomal compartments. Heterotetramerization is necessary
CC to exit the ER.
CC -!- POLYMORPHISM: The following alleles of DOB are known: DOB*01:01,
CC DOB*01:02, DOB*01:03 and DOB*01:04. The sequence shown is that of
CC DOB*01:01.
CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR EMBL; X03066; CAA26870.1; -; mRNA.
DR EMBL; M26040; AAA59718.1; -; mRNA.
DR EMBL; X66401; CAA47028.1; -; Genomic_DNA.
DR EMBL; CR541832; CAG46631.1; -; mRNA.
DR EMBL; CR788227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006097; AAH06097.1; -; mRNA.
DR EMBL; L29472; AAA59717.1; -; Genomic_DNA.
DR EMBL; X87344; CAA60789.1; -; Genomic_DNA.
DR EMBL; AB035252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS4754.1; -.
DR PIR; S27335; A24669.
DR RefSeq; NP_002111.1; NM_002120.3.
DR PDB; 4I0P; X-ray; 3.20 A; D/H=30-218.
DR PDBsum; 4I0P; -.
DR AlphaFoldDB; P13765; -.
DR SMR; P13765; -.
DR BioGRID; 109357; 3.
DR DIP; DIP-60117N; -.
DR IntAct; P13765; 3.
DR STRING; 9606.ENSP00000390020; -.
DR GlyGen; P13765; 1 site.
DR iPTMnet; P13765; -.
DR PhosphoSitePlus; P13765; -.
DR BioMuta; HLA-DOB; -.
DR DMDM; 122261; -.
DR jPOST; P13765; -.
DR MassIVE; P13765; -.
DR PaxDb; P13765; -.
DR PeptideAtlas; P13765; -.
DR PRIDE; P13765; -.
DR ProteomicsDB; 52985; -.
DR Antibodypedia; 34891; 194 antibodies from 24 providers.
DR DNASU; 3112; -.
DR Ensembl; ENST00000426644.6; ENSP00000395780.2; ENSG00000243612.5.
DR Ensembl; ENST00000438763.7; ENSP00000390020.2; ENSG00000241106.8.
DR Ensembl; ENST00000447178.6; ENSP00000405108.2; ENSG00000241386.6.
DR Ensembl; ENST00000454286.6; ENSP00000397268.2; ENSG00000243496.6.
DR Ensembl; ENST00000454969.6; ENSP00000410390.2; ENSG00000241910.5.
DR Ensembl; ENST00000456406.6; ENSP00000394783.2; ENSG00000239457.6.
DR Ensembl; ENST00000648009.1; ENSP00000496848.1; ENSG00000241106.8.
DR GeneID; 3112; -.
DR KEGG; hsa:3112; -.
DR MANE-Select; ENST00000438763.7; ENSP00000390020.2; NM_002120.4; NP_002111.1.
DR UCSC; uc011gkh.2; human.
DR CTD; 3112; -.
DR DisGeNET; 3112; -.
DR GeneCards; HLA-DOB; -.
DR HGNC; HGNC:4937; HLA-DOB.
DR HPA; ENSG00000241106; Group enriched (intestine, lymphoid tissue).
DR MIM; 142920; gene.
DR MIM; 600629; gene.
DR neXtProt; NX_P13765; -.
DR OpenTargets; ENSG00000241106; -.
DR PharmGKB; PA35061; -.
DR VEuPathDB; HostDB:ENSG00000241106; -.
DR eggNOG; ENOG502RWX2; Eukaryota.
DR GeneTree; ENSGT00940000162353; -.
DR InParanoid; P13765; -.
DR OMA; DIKITWF; -.
DR OrthoDB; 1249505at2759; -.
DR PhylomeDB; P13765; -.
DR TreeFam; TF336626; -.
DR PathwayCommons; P13765; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR SignaLink; P13765; -.
DR SIGNOR; P13765; -.
DR BioGRID-ORCS; 3112; 8 hits in 1074 CRISPR screens.
DR ChiTaRS; HLA-DOB; human.
DR GeneWiki; HLA-DOB; -.
DR GenomeRNAi; 3112; -.
DR Pharos; P13765; Tbio.
DR PRO; PR:P13765; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P13765; protein.
DR Bgee; ENSG00000241106; Expressed in lymph node and 93 other tissues.
DR ExpressionAtlas; P13765; baseline and differential.
DR Genevisible; P13765; HS.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB.
DR GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
DR GO; GO:0032395; F:MHC class II receptor activity; TAS: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; IBA:GO_Central.
DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IDA:UniProtKB.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
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; IPR000353; MHC_II_b_N.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00969; MHC_II_beta; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00921; MHC_II_beta; 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; Disulfide bond; Endosome; Glycoprotein;
KW Immunity; Lysosome; Membrane; MHC II; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT CHAIN 27..273
FT /note="HLA class II histocompatibility antigen, DO beta
FT chain"
FT /id="PRO_0000018963"
FT TOPO_DOM 27..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 123..213
FT /note="Ig-like C1-type"
FT REGION 27..120
FT /note="Beta-1"
FT REGION 121..214
FT /note="Beta-2"
FT REGION 215..224
FT /note="Connecting peptide"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 143..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 18
FT /note="R -> Q (in allele DOB*01:02; dbSNP:rs2071554)"
FT /id="VAR_016743"
FT VARIANT 210
FT /note="V -> I (in dbSNP:rs11575907)"
FT /evidence="ECO:0000269|PubMed:14574404, ECO:0000269|Ref.4"
FT /id="VAR_050363"
FT VARIANT 234
FT /note="L -> F (in allele DOB*01:04; dbSNP:rs2070121)"
FT /id="VAR_016745"
FT VARIANT 244
FT /note="V -> I (in allele DOB*01:03; dbSNP:rs2621330)"
FT /id="VAR_016744"
FT STRAND 34..44
FT /evidence="ECO:0007829|PDB:4I0P"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:4I0P"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:4I0P"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:4I0P"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4I0P"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:4I0P"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4I0P"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:4I0P"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:4I0P"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:4I0P"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4I0P"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4I0P"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:4I0P"
FT STRAND 139..151
FT /evidence="ECO:0007829|PDB:4I0P"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:4I0P"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:4I0P"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4I0P"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:4I0P"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:4I0P"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:4I0P"
SQ SEQUENCE 273 AA; 30822 MW; C06A1360DCC4AD26 CRC64;
MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL
EEYVRFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSRQA VDGVCRHNYR LGAPFTVGRK
VQPEVTVYPE RTPLLHQHNL LHCSVTGFYP GDIKIKWFLN GQEERAGVMS TGPIRNGDWT
FQTVVMLEMT PELGHVYTCL VDHSSLLSPV SVEWRAQSEY SWRKMLSGIA AFLLGLIFLL
VGIVIQLRAQ KGYVRTQMSG NEVSRAVLLP QSC
