DRB3_HUMAN
ID DRB3_HUMAN Reviewed; 266 AA.
AC P79483; A0ZXY9; A7MA46; B5AU12; B5AU13; B5AU14; B8YAC6; C6H115; C6H116;
AC O02875; O19590; O46701; O46794; O78049; O78162; P01913; P79663; Q29721;
AC Q29809; Q2PPD0; Q30144; Q507L8; Q5SP44; Q5STE0; Q6YJU6; Q70M87; Q7YQ62;
AC Q860I9; Q8SP69; Q8WLT7; Q8WLT8; Q95359; Q95HM8; Q95IE5; Q96H16; Q9BCP3;
AC Q9BD18; Q9MYA4; Q9MYH3; Q9MYH4; Q9TP01; Q9TP02; Q9TPB5; Q9TQ21; Q9UIN3;
AC Q9UIN5;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=HLA class II histocompatibility antigen, DR beta 3 chain;
DE AltName: Full=MHC class II antigen DRB3;
DE Flags: Precursor;
GN Name=HLA-DRB3;
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 DRB3*02:01).
RX PubMed=11894954; DOI=10.1002/j.1460-2075.1983.tb01435.x;
RA Long E.O., Wake C.T., Gorski J., Mach B.;
RT "Complete sequence of an HLA-DR beta chain deduced from a cDNA clone and
RT identification of multiple non-allelic DR beta chain genes.";
RL EMBO J. 2:389-394(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB3*01:01).
RX PubMed=3459965; DOI=10.1038/322067a0;
RA Gorski J., Mach B.;
RT "Polymorphism of human Ia antigens: gene conversion between two DR beta
RT loci results in a new HLA-D/DR specificity.";
RL Nature 322:67-70(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB3*01:01).
RC TISSUE=Blood;
RX PubMed=9234492; DOI=10.1111/j.1399-0039.1997.tb02818.x;
RA Martinez-Quiles N., Martin-Villa J.M., Martinez-Laso J., Perez-Blas M.,
RA Ferre-Lopez S., Moreno-Pelayo M.A., Alvarez-Tejado M., Arnaiz-Villena A.;
RT "Description of two new HLA-DRB alleles (DRB1*0310 and DRB3*01012) found in
RT a Spanish infant.";
RL Tissue Antigens 49:658-661(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB3*01:01), AND NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 35-119 (ALLELE DRB3*01:04).
RC TISSUE=Blood;
RX PubMed=10902611; DOI=10.1034/j.1399-0039.2000.550606.x;
RA Coquillard G.J., Tang T.F., Steiner N., Perlee L., Ng J., Hartzman R.J.,
RA Hurley C.K.;
RT "DRB3 alleles with variations in the annealing sites of commonly used
RT amplification primers.";
RL Tissue Antigens 55:558-563(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB3*01:01).
RA Kim K.H., Kang J.H., Maeng C.Y., Han H., Park J.H., Hahm K.S., Kim K.L.;
RT "Cloning and nucleotide sequence analysis of HLA-DRB3*01012 from EBV-
RT transformed Korean B-cell line by sequence based typing.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB3*03:01).
RA Spierings E., Zegveld S.T., Goulmy E.;
RT "HLA-DRB3*03011 sequence complete mRNA.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB3*02:01).
RA Mach B.F., Long E.O., Wake C.T.;
RT "DNA sequences coding for the DR beta-chain locus of the human lymphocyte
RT antigen complex and polypeptides, diagnostic typing processes and products
RT related thereto.";
RL Patent number EP0103960, 28-MAR-1984.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES DRB3*01:01 AND
RP DRB3*02:02).
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DRB3*01:01 AND DRB3*02:02).
RC TISSUE=Brain;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB3*02:01).
RX PubMed=6414998; DOI=10.1016/0198-8859(83)90089-7;
RA Long E.O., Gorski J., Rollini P., Wake C.T., Strubin M.,
RA Rabourdin-Combe C., Mach B.;
RT "Molecular analysis of the genes for human class II antigens of the major
RT histocompatibility complex.";
RL Hum. Immunol. 8:113-121(1983).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB3*02:01).
RX PubMed=3476943; DOI=10.1073/pnas.84.17.6234;
RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., McDevitt H.O.;
RT "Allelic variation in the DR subregion of the human major
RT histocompatibility complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELES DRB3*02:10 AND DRB3*02:11).
RX PubMed=11098940; DOI=10.1034/j.1399-0039.2000.560412.x;
RA Balas A., Santos S., Aviles M.J., Garcia-Sanchez F., Lillo R.,
RA Vicario J.L.;
RT "Identification by sequencing based typing and complete coding region
RT analysis of three new HLA class II alleles: DRB3*0210, DRB3*0211 and
RT DQB1*0310.";
RL Tissue Antigens 56:380-384(2000).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-217 (ALLELE DRB3*02:24).
RA Westerink N., Bacelar M., Arts-Hilkes Y., Mulder W., Rozemuller E.H.;
RT "A new HLA-DRB3*02 allele identified by sequencing based typing.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-124 (ALLELE DRB3*02:18).
RX PubMed=15140047; DOI=10.1111/j.0001-2815.2004.00196.x;
RA Balas A., Aviles M.J., Lillo R., Alonso-Nieto M., Zarapuz L.,
RA Garcia-Villaescusa R., Garcia-Sanchez F., Vicario J.L.;
RT "Sequencing of two new HLA class II alleles: DRB3*0218 and DQB1*030202.";
RL Tissue Antigens 63:614-616(2004).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:09).
RX PubMed=10958362; DOI=10.1034/j.1399-0039.2000.560113.x;
RA Morabito A., Pera C., Longo A., Delfino L., Ferrara G.B.;
RT "Identification of a new DRB3*02 allelic variant (DRB3*0209) by high-
RT resolution sequence-based typing.";
RL Tissue Antigens 56:90-94(2000).
RN [16]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*01:05).
RX PubMed=11972885; DOI=10.1034/j.1399-0039.2002.590115.x;
RA Tang T.F., Lin Y.-S., Robbins F.M., Li L., Sintasath D., Coquillard G.,
RA Huang A., Heine U., Ng J., Hartzman R.J., Hurley C.K.;
RT "Description of fourteen new DRB alleles found in a stem cell donor
RT registry.";
RL Tissue Antigens 59:63-65(2002).
RN [17]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:19).
RX PubMed=15496209; DOI=10.1111/j.1399-0039.2004.00296.x;
RA Dubois V., Favre-Victoire I., Gebuhrer L.;
RT "Three new DRB alleles routinely identified by sequence-based typing:
RT DRB1*010103, DRB1*0326 and DRB3*0219.";
RL Tissue Antigens 64:621-623(2004).
RN [18]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:23).
RC TISSUE=Peripheral blood;
RX PubMed=18764810; DOI=10.1111/j.1399-0039.2008.01124.x;
RA Danzer M., Polin H., Hofer K., Proll J., Gabriel C.;
RT "Characterisation of two novel HLA alleles, HLA-Cw*0429 and HLA-
RT DRB3*0223.";
RL Tissue Antigens 72:498-499(2008).
RN [19]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB3*01:01; DRB3*01:12
RP AND DRB3*01:13).
RX PubMed=19000136; DOI=10.1111/j.1399-0039.2008.01158.x;
RA Lee K.W., Jung Y.A.;
RT "Description of three novel HLA-DRB3 alleles: DRB3*010105, DRB3*0112 and
RT DRB3*0113.";
RL Tissue Antigens 73:83-84(2009).
RN [20]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:04).
RA Keller E.;
RT "New DRB3*02 variant.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [21]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB3*02:12 AND
RP DRB3*02:13).
RA Greville W.D., Ng G., Kennedy A., Dunckley H.;
RT "An HLA-DRB3 allele detected by SBT.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [22]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:14).
RA Moine A.;
RT "A new HLA DRB3* allele very similar to DRB3*02021 and DRB3*0212 alleles.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [23]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:15).
RA Varney M.;
RT "A novel DRB3 allele.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [24]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:16).
RA Avergas C.U., Iglehart B.A., Leffell M.S.;
RT "Identification of a novel DRB3*0216 allele.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [25]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:17).
RA Hogbin J.-P., Chapman G., Greville W.D.;
RT "Novel HLA-DRB3 allele revealed by sequencing based typing.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [26]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*01:11).
RA Perasaari J., Egle Jansson I., Partanen J., Bengtsson M.;
RT "Description of a new DRB3* allele.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [27]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:20).
RA Colombini I., Malagoli A., Carella G.;
RT "New HLA-DRB3*02 allele.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [28]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:21).
RA Garino E., Berrino M., Bertinetto F., Brancatello F., Caropreso P.,
RA Chidichimo R., Frisaldi E., Mazzola G., Panniello M., Tondat F.,
RA Locatelli F., Amoroso A.;
RT "New HLA-DRB3*02 allelic variant identified by high resolution sequence-
RT based typing.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [29]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB3*02:22).
RA Dormoy A., Froelich N.;
RT "The DRB3 new allele is identical to the current HLA-DRB3*020201 allele
RT except a point substitution at codon 74 where a G is found in place of A.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [30]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:25).
RC TISSUE=Peripheral blood;
RA Dormoy A., Derin R., Jollet I., Weschler B., Leisenbach R.;
RT "The new DRB3 allele is identical to the DRB3*020201 allele except a
RT mutation at position 266 leading to the change of the amino acid 65 (Tyr
RT (TAC) -> Ser(TCC).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [31]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*01:14).
RA Garritsen H.S.P., Fae I., Legath N., Hannig H., Fischer G.F.;
RT "Identification of a novel HLA-DRB3*01 allele containing a DRB1 sequence
RT motive by micro-TGGE and confirmed by cloning and direct sequencing.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [32]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB3*02:02).
RA Greville W.D., Ng G., Kennedy A., Dunckley H.;
RT "New HLA class II (DRB3) allele detected by sequencing-based typing.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [33]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB3*01:08).
RC TISSUE=Bone marrow;
RA Loeliger C.;
RT "Description of a new HLA-DRB3 allele in a Spanish bone marrow donor.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [34]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB3*01:09).
RA Li L., Hurley C.K.;
RT "Novel HLA*DRB3 allele.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [35]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DRB3*02:05).
RX PubMed=9162096; DOI=10.1007/s002510050248;
RA Robbins F., Hurley C.K., Tang T., Yao H., Lin Y.S., Wade J., Goeken N.,
RA Hartzman R.J.;
RT "Diversity associated with the second expressed HLA-DRB locus in the human
RT population.";
RL Immunogenetics 46:104-110(1997).
RN [36]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-117 (ALLELE DRB3*01:03).
RA Olerup O.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [37]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB3*02:06).
RX PubMed=9243765; DOI=10.1111/j.1399-0039.1997.tb02843.x;
RA Hashemi-Tavoularis S., Couture C., Buyse I.M.;
RT "Identification of new DRB1*01 (DRB1*01022), DRB1*14 (DRB1*1428) and DRB3*
RT (DRB3*0206) alleles.";
RL Tissue Antigens 50:89-93(1997).
RN [38]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELES DRB3*02:08 AND
RP DRB3*03:02).
RC TISSUE=Blood;
RX PubMed=9802612; DOI=10.1111/j.1399-0039.1998.tb03047.x;
RA Hashemi-tavoularis S., Ouellet S., Sengar D.P.S., Buyse I.M.;
RT "A novel DRB3 allele (DRB3*0208), a new allelic variant of DRB1*1502
RT (DRB1*15023) and two new DQB1 (DQB1*03012 and DQB1*0614) alleles.";
RL Tissue Antigens 52:294-299(1998).
RN [39]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELES DRB3*01:06 AND
RP DRB3*01:07).
RC TISSUE=Peripheral blood;
RX PubMed=11380956; DOI=10.1034/j.1399-0039.2001.570420.x;
RA Tavoularis S., Ouellet S., Stephens S.;
RT "Identification of three new DRB3* (DRB3*0106, DRB3*0107 and DRB3*02022)
RT alleles.";
RL Tissue Antigens 57:390-393(2001).
RN [40]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB3*01:10).
RC TISSUE=Peripheral blood;
RX PubMed=15104685; DOI=10.1111/j.0001-2815.2004.00186.x;
RA Tavoularis S., Couture C., Ribeiro-Barros E.;
RT "Identification of three novel alleles: DRB3*0110, DRB1*1140, and
RT DRB1*140102.";
RL Tissue Antigens 63:496-500(2004).
RN [41]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-119 (ALLELE DRB3*03:03).
RX PubMed=10599892; DOI=10.1034/j.1399-0039.1999.540510.x;
RA Panigoro R., Greville W.D., Kennedy A., Trejaut J., Dunckley H.;
RT "New HLA class II alleles in the Indonesian population.";
RL Tissue Antigens 54:521-523(1999).
RN [42]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-117 (ALLELE DRB3*01:02).
RX PubMed=9234494; DOI=10.1111/j.1399-0039.1997.tb02820.x;
RA Guttridge M.G., Hudson L., Williams H., Dunn P., Duy S., Darke C.;
RT "Identification and nucleotide sequence of two novel DRB3 alleles,
RT DRB3*0102 and DRB3*010133.";
RL Tissue Antigens 49:665-667(1997).
RN [43]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (ALLELE DRB3*02:07).
RX PubMed=9389331; DOI=10.1111/j.1399-0039.1997.tb02912.x;
RA Voorter C.E., Hentges F., van den Berg-Loonen E.M.;
RT "Identification of a new DRB3*02 allele (DRB3*0207) by sequence-based
RT typing.";
RL Tissue Antigens 50:552-554(1997).
RN [44]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (ALLELE DRB3*02:03).
RA Anholts J.D.H., Verduijn W., Schreuder G.M.T.;
RT "Five new DRB1 alleles found during routine DRB oligotyping.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [45]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-120 (ALLELE DRB3*02:02).
RA Eberle M., Asu U., Taylor M., Hunter J.B., Fuller T.C., Maurer D.;
RT "Identification of a putative DR8 founder haplotype containing a novel
RT DRB1*0801 allele.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [46]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-217 (ALLELE DRB3*01:01/DRB3*01:02).
RX PubMed=2471740;
RA Gorski J.;
RT "HLA-DR beta-chain polymorphism. Second domain polymorphism reflects
RT evolutionary relatedness of alleles and may explain public serologic
RT epitopes.";
RL J. Immunol. 143:329-333(1989).
RN [47]
RP FUNCTION (ALLELES DRB3*01:01; DRB3*02:02 AND DRB3*03:01).
RX PubMed=2788702; DOI=10.1084/jem.170.3.1027;
RA Gorski J., Irle C., Mickelson E.M., Sheehy M.J., Termijtelen A., Ucla C.,
RA Mach B.;
RT "Correlation of structure with T cell responses of the three members of the
RT HLA-DRw52 allelic series.";
RL J. Exp. Med. 170:1027-1032(1989).
RN [48]
RP FUNCTION (ALLELE DRB3*01:01).
RX PubMed=2463305;
RA Demotz S., Lanzavecchia A., Eisel U., Niemann H., Widmann C., Corradin G.;
RT "Delineation of several DR-restricted tetanus toxin T cell epitopes.";
RL J. Immunol. 142:394-402(1989).
RN [49]
RP ASSOCIATION OF ALLELE DRB3*03:01 WITH HLA-IDENTICAL SEX-MISMATCHED GRAFT
RP REJECTION, AND POLYMORPHISM.
RX PubMed=12944060; DOI=10.1016/s0140-6736(03)14191-8;
RA Spierings E., Vermeulen C.J., Vogt M.H., Doerner L.E., Falkenburg J.H.,
RA Mutis T., Goulmy E.;
RT "Identification of HLA class II-restricted H-Y-specific T-helper epitope
RT evoking CD4+ T-helper cells in H-Y-mismatched transplantation.";
RL Lancet 362:610-615(2003).
RN [50]
RP FUNCTION (ALLELE DRB3*03:01).
RX PubMed=16148104; DOI=10.4049/jimmunol.175.6.3603;
RA Schulze zur Wiesch J., Lauer G.M., Day C.L., Kim A.Y., Ouchi K.,
RA Duncan J.E., Wurcel A.G., Timm J., Jones A.M., Mothe B., Allen T.M.,
RA McGovern B., Lewis-Ximenez L., Sidney J., Sette A., Chung R.T.,
RA Walker B.D.;
RT "Broad repertoire of the CD4+ Th cell response in spontaneously controlled
RT hepatitis C virus infection includes dominant and highly promiscuous
RT epitopes.";
RL J. Immunol. 175:3603-3613(2005).
RN [51]
RP UBIQUITINATION BY MARCHF1, AND SUBCELLULAR LOCATION.
RX PubMed=18305173; DOI=10.1073/pnas.0708874105;
RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., Pierre P.,
RA Gatti E.;
RT "MHC class II stabilization at the surface of human dendritic cells is the
RT result of maturation-dependent MARCH I down-regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008).
RN [52]
RP IDENTIFICATION OF THE ALLOANTIGEN HPA-1A BY MASS SPECTROMETRY, ASSOCIATION
RP TO ALLELE HLA-DRB3*01:01, AND POLYMORPHISM.
RX PubMed=19494351; DOI=10.1182/blood-2009-04-211839;
RA Anani Sarab G., Moss M., Barker R.N., Urbaniak S.J.;
RT "Naturally processed peptides spanning the HPA-1a polymorphism are
RT efficiently generated and displayed from platelet glycoprotein by HLA-
RT DRB3*0101-positive antigen-presenting cells.";
RL Blood 114:1954-1957(2009).
RN [53]
RP ASSOCIATION OF ALLELES DRB3*01:01 AND DRB3*02:02 WITH GRAFT-VERSUS-LEUKEMIA
RP EFFECT, AND POLYMORPHISM.
RX PubMed=19706888; DOI=10.1182/blood-2009-03-208017;
RA Stumpf A.N., van der Meijden E.D., van Bergen C.A., Willemze R.,
RA Falkenburg J.H., Griffioen M.;
RT "Identification of 4 new HLA-DR-restricted minor histocompatibility
RT antigens as hematopoietic targets in antitumor immunity.";
RL Blood 114:3684-3692(2009).
RN [54]
RP FUNCTION (ALLELE DRB3*02:02), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19531622; DOI=10.1158/1078-0432.ccr-09-0582;
RA Bioley G., Dousset C., Yeh A., Dupont B., Bhardwaj N., Mears G., Old L.J.,
RA Ayyoub M., Valmori D.;
RT "Vaccination with recombinant NY-ESO-1 protein elicits immunodominant HLA-
RT DR52b-restricted CD4+ T cell responses with a conserved T cell receptor
RT repertoire.";
RL Clin. Cancer Res. 15:4467-4474(2009).
RN [55]
RP ASSOCIATION OF ALLELE DRB3*01:01 WITH NEONATAL ALLOIMMUNE THROMBOCYTOPENIA,
RP AND POLYMORPHISM.
RX PubMed=19535639; DOI=10.4049/jimmunol.0801473;
RA Rayment R., Kooij T.W., Zhang W., Siebold C., Murphy M.F., Allen D.,
RA Willcox N., Roberts D.J.;
RT "Evidence for the specificity for platelet HPA-1a alloepitope and the
RT presenting HLA-DR52a of diverse antigen-specific helper T cell clones from
RT alloimmunized mothers.";
RL J. Immunol. 183:677-686(2009).
RN [56]
RP FUNCTION (ALLELES DRB3*01:01 AND DRB3*02:02), TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19830726; DOI=10.1002/eji.200939225;
RA Faner R., James E., Huston L., Pujol-Borrel R., Kwok W.W., Juan M.;
RT "Reassessing the role of HLA-DRB3 T-cell responses: evidence for
RT significant expression and complementary antigen presentation.";
RL Eur. J. Immunol. 40:91-102(2010).
RN [57]
RP FUNCTION (ALLELE DRB3*02:02).
RX PubMed=20368442; DOI=10.1073/pnas.1001322107;
RA Ayyoub M., Dojcinovic D., Pignon P., Raimbaud I., Schmidt J., Luescher I.,
RA Valmori D.;
RT "Monitoring of NY-ESO-1 specific CD4+ T cells using molecularly defined MHC
RT class II/His-tag-peptide tetramers.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7437-7442(2010).
RN [58]
RP FUNCTION (ALLELE DRB3*02:02).
RX PubMed=23569328; DOI=10.1084/jem.20121437;
RA Long H.M., Chagoury O.L., Leese A.M., Ryan G.B., James E., Morton L.T.,
RA Abbott R.J., Sabbah S., Kwok W., Rickinson A.B.;
RT "MHC II tetramers visualize human CD4+ T cell responses to Epstein-Barr
RT virus infection and demonstrate atypical kinetics of the nuclear antigen
RT EBNA1 response.";
RL J. Exp. Med. 210:933-949(2013).
RN [59]
RP FUNCTION (ALLELE DRB3*02:02).
RX PubMed=22929521; DOI=10.1038/leu.2012.248;
RA Anguille S., Fujiki F., Smits E.L., Oji Y., Lion E., Oka Y., Berneman Z.N.,
RA Sugiyama H.;
RT "Identification of a Wilms' tumor 1-derived immunogenic CD4(+) T-cell
RT epitope that is recognized in the context of common Caucasian HLA-DR
RT haplotypes.";
RL Leukemia 27:748-750(2013).
RN [60]
RP FUNCTION (ALLELE DRB3*02:02).
RX PubMed=30282837; DOI=10.1172/jci.insight.122467;
RA Yossef R., Tran E., Deniger D.C., Gros A., Pasetto A., Parkhurst M.R.,
RA Gartner J.J., Prickett T.D., Cafri G., Robbins P.F., Rosenberg S.A.;
RT "Enhanced detection of neoantigen-reactive T cells targeting unique and
RT shared oncogenes for personalized cancer immunotherapy.";
RL JCI Insight 3:0-0(2018).
RN [61]
RP FUNCTION (ALLELE DRB3*01:01 AND DRB3*02:02).
RX PubMed=31020640; DOI=10.1002/eji.201948126;
RA Becerra-Artiles A., Cruz J., Leszyk J.D., Sidney J., Sette A.,
RA Shaffer S.A., Stern L.J.;
RT "Naturally processed HLA-DR3-restricted HHV-6B peptides are recognized
RT broadly with polyfunctional and cytotoxic CD4 T-cell responses.";
RL Eur. J. Immunol. 49:1167-1185(2019).
RN [62]
RP FUNCTION (ALLELE DRB3*02:02).
RX PubMed=31333679; DOI=10.3389/fimmu.2019.01568;
RA Grifoni A., Moore E., Voic H., Sidney J., Phillips E., Jadi R., Mallal S.,
RA De Silva A.D., De Silva A.M., Peters B., Weiskopf D., Sette A.;
RT "Characterization of Magnitude and Antigen Specificity of HLA-DP, DQ, and
RT DRB3/4/5 Restricted DENV-Specific CD4+ T Cell Responses.";
RL Front. Immunol. 10:1568-1568(2019).
RN [63]
RP FUNCTION (ALLELE DRB3*02:02).
RX PubMed=31308093; DOI=10.4049/jimmunol.1900377;
RA Meckiff B.J., Ladell K., McLaren J.E., Ryan G.B., Leese A.M., James E.A.,
RA Price D.A., Long H.M.;
RT "Primary EBV Infection Induces an Acute Wave of Activated Antigen-Specific
RT Cytotoxic CD4+ T Cells.";
RL J. Immunol. 203:1276-1287(2019).
RN [64]
RP FUNCTION (ALLELE DRB3*03:01).
RX PubMed=32341563; DOI=10.1038/s41587-020-0505-4;
RA Huang H., Wang C., Rubelt F., Scriba T.J., Davis M.M.;
RT "Analyzing the Mycobacterium tuberculosis immune response by T-cell
RT receptor clustering with GLIPH2 and genome-wide antigen screening.";
RL Nat. Biotechnol. 38:1194-1202(2020).
RN [65]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 30-219 (ALLELE DRB3*01:01) IN
RP COMPLEX WITH HLA-DRA AND ITGB3 PEPTIDE (ALLOANTIGEN HPA-1A), SUBUNIT,
RP DOMAIN, AND DISULFIDE BOND.
RX PubMed=17583734; DOI=10.1016/j.jmb.2007.05.025;
RA Parry C.S., Gorski J., Stern L.J.;
RT "Crystallographic structure of the human leukocyte antigen DRA, DRB3*0101:
RT models of a directional alloimmune response and autoimmunity.";
RL J. Mol. Biol. 371:435-446(2007).
RN [66]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-219 (ALLELE DRB3*03:01) IN
RP COMPLEX WITH OF HLA-DRA AND EEF1A2 PEPTIDE, SUBUNIT, DOMAIN, GLYCOSYLATION
RP AT ASN-48, AND DISULFIDE BOND.
RX PubMed=18697946; DOI=10.1073/pnas.0805810105;
RA Dai S., Crawford F., Marrack P., Kappler J.W.;
RT "The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11893-11897(2008).
RN [67]
RP POLYMORPHISM.
RX PubMed=23510415; DOI=10.1111/tan.12093;
RA Mack S.J., Cano P., Hollenbach J.A., He J., Hurley C.K., Middleton D.,
RA Moraes M.E., Pereira S.E., Kempenich J.H., Reed E.F., Setterholm M.,
RA Smith A.G., Tilanus M.G., Torres M., Varney M.D., Voorter C.E.,
RA Fischer G.F., Fleischhauer K., Goodridge D., Klitz W., Little A.M.,
RA Maiers M., Marsh S.G., Mueller C.R., Noreen H., Rozemuller E.H.,
RA Sanchez-Mazas A., Senitzer D., Trachtenberg E., Fernandez-Vina M.;
RT "Common and well-documented HLA alleles: 2012 update to the CWD
RT catalogue.";
RL Tissue Antigens 81:194-203(2013).
CC -!- FUNCTION: A beta chain of antigen-presenting major histocompatibility
CC complex class II (MHCII) molecule. In complex with the alpha chain HLA-
CC DRA, displays antigenic peptides on professional antigen presenting
CC cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on
CC HLA-DRB3-restricted CD4-positive T cells. This guides antigen-specific
CC T-helper effector functions, both antibody-mediated immune response and
CC macrophage activation, to ultimately eliminate the infectious agents
CC and transformed cells. Typically presents extracellular peptide
CC antigens of 10 to 30 amino acids that arise from proteolysis of
CC endocytosed antigens in lysosomes (PubMed:2788702, PubMed:2463305,
CC PubMed:16148104, PubMed:19531622, PubMed:20368442, PubMed:19830726,
CC PubMed:23569328, PubMed:22929521, PubMed:30282837, PubMed:31020640,
CC PubMed:31333679, PubMed:31308093). In the tumor microenvironment,
CC presents antigenic peptides that are primarily generated in tumor-
CC resident APCs likely via phagocytosis of apoptotic tumor cells or
CC macropinocytosis of secreted tumor proteins (By similarity). Presents
CC peptides derived from intracellular proteins that are trapped in
CC autolysosomes after macroautophagy, a mechanism especially relevant for
CC T cell selection in the thymus and central immune tolerance (By
CC similarity). The selection of the immunodominant epitopes follows two
CC processing modes: 'bind first, cut/trim later' for pathogen-derived
CC antigenic peptides and 'cut first, bind later' for autoantigens/self-
CC peptides. The anchor residue at position 1 of the peptide N-terminus,
CC usually a large hydrophobic residue, is essential for high affinity
CC interaction with MHCII molecules (By similarity).
CC {ECO:0000250|UniProtKB:P01911, ECO:0000269|PubMed:16148104,
CC ECO:0000269|PubMed:19531622, ECO:0000269|PubMed:19830726,
CC ECO:0000269|PubMed:20368442, ECO:0000269|PubMed:22929521,
CC ECO:0000269|PubMed:23569328, ECO:0000269|PubMed:2463305,
CC ECO:0000269|PubMed:2788702, ECO:0000269|PubMed:30282837,
CC ECO:0000269|PubMed:31020640, ECO:0000269|PubMed:31308093,
CC ECO:0000269|PubMed:31333679}.
CC -!- FUNCTION: ALLELE DRB3*01:01: Exclusively presents several immunogenic
CC epitopes derived from C. tetani neurotoxin tetX, playing a significant
CC role in immune recognition and long-term protection (PubMed:19830726,
CC PubMed:2788702, PubMed:2463305). Presents viral epitopes derived from
CC HHV-6B U11, TRX2/U56 and U85 antigens to polyfunctional CD4-positive T
CC cells with cytotoxic activity implicated in control of HHV-6B infection
CC (PubMed:31020640). {ECO:0000269|PubMed:19830726,
CC ECO:0000269|PubMed:2463305, ECO:0000269|PubMed:2788702,
CC ECO:0000269|PubMed:31020640}.
CC -!- FUNCTION: ALLELE DRB3*02:02 Exclusively presents several immunogenic
CC epitopes derived from C. tetani neurotoxin tetX, playing a significant
CC role in immune recognition and long-term protection (PubMed:19830726,
CC PubMed:2788702). Upon EBV infection, presents to CD4-positive T cells
CC latent antigen EBNA2 (PRSPTVFYNIPPMPLPPSQL) and lytic antigen BZLF1
CC (LTAYHVSTAPTGSWF) peptides, driving oligoclonal expansion and selection
CC of virus-specific memory T cell subsets with cytotoxic potential to
CC directly eliminate virus-infected B cells (PubMed:31308093,
CC PubMed:23569328). Presents viral epitopes derived from HHV-6B U11,
CC gB/U39 and gH/U48 antigens to polyfunctional CD4-positive T cells with
CC cytotoxic activity implicated in control of HHV-6B infection
CC (PubMed:31020640). Plays a minor role in CD4-positive T cell immune
CC response against Dengue virus by presenting conserved peptides from
CC capsid and non-structural NS3 proteins (PubMed:31333679). Displays
CC peptides derived from IAV matrix protein M, implying a role in
CC protection against IAV infection (PubMed:19830726). In the context of
CC tumor immunesurveillance, may present to T-helper 1 cells an
CC immunogenic epitope derived from tumor-associated antigen WT1
CC (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity
CC in a wide range of solid and hematological malignancies
CC (PubMed:22929521). Presents to Vbeta2-positive T-helper 1 cells
CC specifically an immunodominant peptide derived from tumor antigen
CC CTAG1A/NY-ESO-1(PGVLLKEFTVSGNILTIRLTAADHR) and confers protective
CC memory response (PubMed:19531622, PubMed:20368442). In metastatic
CC epithelial tumors, presents to intratumoral CD4-positive T cells a TP53
CC neoantigen (HYNYMCNSSCMGSMNRRPILTIITL) carrying G245S hotspot driver
CC mutation and may mediate tumor regression (PubMed:30282837).
CC {ECO:0000269|PubMed:19531622, ECO:0000269|PubMed:19830726,
CC ECO:0000269|PubMed:20368442, ECO:0000269|PubMed:22929521,
CC ECO:0000269|PubMed:23569328, ECO:0000269|PubMed:2788702,
CC ECO:0000269|PubMed:30282837, ECO:0000269|PubMed:31020640,
CC ECO:0000269|PubMed:31308093, ECO:0000269|PubMed:31333679}.
CC -!- FUNCTION: ALLELE DRB3*03:01: Presents a series of conserved peptides
CC derived from the M. tuberculosis PPE family of proteins, in particular
CC PPE29 and PPE33, known to be highly immunogenic (PubMed:32341563).
CC Presents immunogenic epitopes derived from C. tetani neurotoxin tetX,
CC playing a role in immune recognition and long-term protection
CC (PubMed:2788702). Displays immunodominant viral peptides from HCV non-
CC structural protein NS2, as part of a broad range T-helper response to
CC resolve infection (PubMed:16148104). {ECO:0000269|PubMed:16148104,
CC ECO:0000269|PubMed:2788702, ECO:0000269|PubMed:32341563}.
CC -!- SUBUNIT: Heterotrimer that consists of an alpha chain HLA-DRA, a beta
CC chain HLA-DRB1 and a peptide (peptide-MHCII) (PubMed:17583734,
CC PubMed:18697946). Newly synthesized alpha and beta chains forms a
CC heterodimer (MHCII) that associates with the CD74/invariant chain (Ii)
CC in the endoplasmic reticulum (ER). Ii is a trimer composed of three
CC subunits and each subunit interacts with one MHCII dimer, blocking the
CC peptide-binding cleft. As a result, MHCII molecules cannot bind
CC peptides present in the ER (By similarity). The complex of MHCII and
CC CD74/Ii is transported in vesicles from ER to Golgi to lysosomes, where
CC it encounters antigenic peptides generated via proteolysis of
CC endocytosed antigens. MHCII dimers are dissociated from CD74/Ii by the
CC combined action of proteolysis and HLA-DM (By similarity). Lysosomal
CC enzymes such as cathepsin, degrade CD74/Ii leaving a 24 amino acid
CC remnant called class II-associated Ii or CLIP. Interacts (via the
CC peptide binding cleft) with CLIP; this interaction inhibits antigen
CC peptide binding before entry in the endosomal compartment. The
CC displacement of CLIP and replacement by a high affinity peptide in
CC lysosomes is performed by HLA-DM heterodimer. HLA-DM catalyzes CLIP
CC dissociation from MHCII, stabilizes empty MHCII and mediates the
CC selection of high affinity peptides (By similarity). Interacts with
CC HLA-DM heterodimer; this interaction is direct (By similarity).
CC Interacts with TCR (via CDR3) (By similarity). Interacts (via beta-2
CC domain) with CD4 coreceptor (via Ig-like V-type domain); this
CC interaction is of exceptionally low affinity yet necessary for optimal
CC recognition of antigenic peptides (By similarity).
CC {ECO:0000250|UniProtKB:P01911, ECO:0000269|PubMed:17583734,
CC ECO:0000269|PubMed:18697946}.
CC -!- INTERACTION:
CC P79483; P27797: CALR; NbExp=3; IntAct=EBI-3910269, EBI-1049597;
CC P79483; P36957: DLST; NbExp=3; IntAct=EBI-3910269, EBI-351007;
CC P79483; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-3910269, EBI-1055945;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173,
CC ECO:0000269|PubMed:19531622, ECO:0000269|PubMed:19830726}; Single-pass
CC type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:18305173}; Single-
CC pass type I membrane protein {ECO:0000255}. Late endosome membrane
CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
CC {ECO:0000255}. Autolysosome membrane {ECO:0000250|UniProtKB:P01911};
CC Single-pass type I membrane protein {ECO:0000255}. Note=The MHC class
CC II complex transits through a number of intracellular compartments in
CC the endocytic pathway until it reaches the cell membrane for antigen
CC presentation (PubMed:18305173). Component of immunological synapses at
CC the interface between T cell and APC. {ECO:0000250|UniProtKB:P01911}.
CC -!- TISSUE SPECIFICITY: Expressed in professional APCs:
CC monocyte/macrophages, dendritic cells and B cells (at protein level).
CC {ECO:0000269|PubMed:19531622, ECO:0000269|PubMed:19830726}.
CC -!- DOMAIN: The beta-1 domain is a structural part of the peptide-binding
CC cleft. It contains one alpha helix and 4 beta sheets, respectively
CC forming part of the wall and the floor of the peptide-binding cleft.
CC The other 4 beta sheets of the floor and the second alpha helix wall is
CC formed by the alpha-1 domain of HLA-DRA. Forms hydrogen bonds with the
CC peptide main chain via conserved amino acid in most HLA-DRB molecules.
CC The polymorphic residues accomodate the side chains of the peptide
CC conferring peptide specificity to distinct HLA-DRB3 alleles
CC (PubMed:17583734, PubMed:18697946). The peptide-bound beta-1 domain
CC forms hydrogen bonds with CDR2 and CDR3 alpha-domains of TCR (By
CC similarity). {ECO:0000250|UniProtKB:P01911,
CC ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:18697946}.
CC -!- DOMAIN: The beta-2 Ig-like domain mediates the interaction with CD4
CC coreceptor. {ECO:0000250|UniProtKB:P01911}.
CC -!- PTM: Ubiquitinated by MARCHF1 and MARCHF8 at Lys-254 leading to sorting
CC into the endosome system and down-regulation of MHC class II.
CC {ECO:0000305|PubMed:18305173}.
CC -!- POLYMORPHISM: Highly polymorphic. Polymorphic residues encode for the
CC beta-1 domain of the peptide-binding cleft, where they contribute to
CC variations in peptide binding and TCR recognition among different
CC alleles. The sequence shown is that of DRB3*01:01. The sequences of
CC common representative alleles of serologically distinct allele groups
CC as defined in the catalog of common and well-documented HLA alleles,
CC are described as variants of DRB3*01:01. The most frequent alleles in
CC human population are DRB3*01:01 (DR52a), DRB3*02:02 (DR52b) and
CC DRB3*03:01 (DR52c) (PubMed:23510415). Allele DRB3*01:01 belongs to an
CC ancestral haplotype and is associated with autoimmune diseases that are
CC linked to antigen presentation. It is found in more than 95% of the
CC homozygous HPA-1B mothers that produce anti-HPA-1A antibodies, leading
CC to neonatal alloimmune thrombocytopenia (NAIT) (PubMed:19494351,
CC PubMed:19535639). In the context of hematological malignancy and T cell
CC transplantation, alleles DRB3*01:01 and DRB3*02:02 present minor
CC histocompatibility antigens derived respectively from host PTK2B and
CC MR1 proteins, contributing to T cell-mediated graft-versus-leukemia
CC effect and complete remission (PubMed:19706888). Allele DRB3*03:01
CC plays an important role in the outcome of HLA-identical sex-mismatched
CC organ transplantation. Presents to T-helper cells a minor
CC histocompatibility antigen encoded by the Y chromosome RPS4Y1
CC (VIKVNDTVQI), leading to the maturation of dendritic cells and
CC expansion of antigen-specific cytotoxic T cells, ultimately triggering
CC transplant rejection (PubMed:12944060). {ECO:0000269|PubMed:12944060,
CC ECO:0000269|PubMed:19494351, ECO:0000269|PubMed:19535639,
CC ECO:0000269|PubMed:19706888, ECO:0000269|PubMed:23510415}.
CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
CC -!- CAUTION: HLA-DRB3, HLA-DRB4 and HLA-DRB5 may represent a unique gene.
CC {ECO:0000305}.
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DR EMBL; V00522; CAA23781.1; -; mRNA.
DR EMBL; X04055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X04058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U66825; AAD43828.1; -; mRNA.
DR EMBL; AF026467; AAC05599.1; -; Genomic_DNA.
DR EMBL; AF199236; AAF13065.2; -; mRNA.
DR EMBL; U95819; AAD00819.1; -; mRNA.
DR EMBL; AY138123; AAN15205.1; -; mRNA.
DR EMBL; A06800; CAA00596.1; -; mRNA.
DR EMBL; AL662842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR788283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z84814; CAB06607.1; -; Genomic_DNA.
DR EMBL; BC008987; AAH08987.1; -; mRNA.
DR EMBL; BC106057; AAI06058.1; -; mRNA.
DR EMBL; M17380; AAA59804.1; -; mRNA.
DR EMBL; AF192258; AAF26358.1; -; mRNA.
DR EMBL; AF192259; AAF26359.1; -; mRNA.
DR EMBL; FJ515276; ACL50609.1; -; Genomic_DNA.
DR EMBL; AY291205; AAP43643.1; -; Genomic_DNA.
DR EMBL; AF148518; AAF67837.1; -; Genomic_DNA.
DR EMBL; AF081677; AAC32202.1; -; Genomic_DNA.
DR EMBL; AY271986; AAP23230.1; -; Genomic_DNA.
DR EMBL; AM747470; CAO00528.1; -; Genomic_DNA.
DR EMBL; EU873151; ACF33221.1; -; Genomic_DNA.
DR EMBL; EU873152; ACF33222.1; -; Genomic_DNA.
DR EMBL; EU873153; ACF33223.1; -; Genomic_DNA.
DR EMBL; X91639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF208484; AAF23165.1; -; Genomic_DNA.
DR EMBL; AF208485; AAF23166.1; -; Genomic_DNA.
DR EMBL; AJ290395; CAC27417.1; -; Genomic_DNA.
DR EMBL; AF427138; AAL26538.1; -; Genomic_DNA.
DR EMBL; AF455114; AAL57866.1; -; Genomic_DNA.
DR EMBL; AF461431; AAL66370.1; -; Genomic_DNA.
DR EMBL; AJ564210; CAD91915.2; -; Genomic_DNA.
DR EMBL; AY958608; AAY28717.1; -; Genomic_DNA.
DR EMBL; DQ311653; ABC33924.1; -; Genomic_DNA.
DR EMBL; AM413002; CAL85628.1; -; Genomic_DNA.
DR EMBL; FN424163; CAZ66795.1; -; Genomic_DNA.
DR EMBL; FN424162; CAZ66766.1; -; Genomic_DNA.
DR EMBL; AF177216; AAD53911.1; -; Genomic_DNA.
DR EMBL; AF361865; AAK38297.1; -; Genomic_DNA.
DR EMBL; AY042679; AAK94514.1; -; Genomic_DNA.
DR EMBL; U36826; AAB63531.1; -; Genomic_DNA.
DR EMBL; U94590; AAB53324.1; -; Genomic_DNA.
DR EMBL; X95760; CAA65066.1; -; Genomic_DNA.
DR EMBL; Y13715; CAA74043.1; -; Genomic_DNA.
DR EMBL; AJ001255; CAA04629.1; -; Genomic_DNA.
DR EMBL; AJ242860; CAB62390.1; -; Genomic_DNA.
DR EMBL; AJ242862; CAB62392.1; -; Genomic_DNA.
DR EMBL; AJ315477; CAC86562.1; -; Genomic_DNA.
DR EMBL; AF028012; AAB94614.1; -; Genomic_DNA.
DR EMBL; Y08063; CAA69301.1; -; Genomic_DNA.
DR EMBL; Y10180; CAA71253.1; -; Genomic_DNA.
DR EMBL; X86977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF152845; AAD45286.1; -; Genomic_DNA.
DR PIR; B60748; B60748.
DR PIR; E28043; E28043.
DR PIR; I37469; HLHU5D.
DR PIR; PT0164; PT0164.
DR PIR; PT0165; PT0165.
DR PIR; PT0166; PT0166.
DR PIR; S03442; S03442.
DR RefSeq; NP_072049.2; NM_022555.3.
DR PDB; 2Q6W; X-ray; 2.25 A; B/E=30-219.
DR PDB; 3C5J; X-ray; 1.80 A; B=30-219.
DR PDB; 4H1L; X-ray; 3.30 A; B/E=33-219.
DR PDBsum; 2Q6W; -.
DR PDBsum; 3C5J; -.
DR PDBsum; 4H1L; -.
DR AlphaFoldDB; P79483; -.
DR SMR; P79483; -.
DR BioGRID; 109370; 101.
DR IntAct; P79483; 8.
DR BindingDB; P79483; -.
DR ChEMBL; CHEMBL3460; -.
DR DrugBank; DB05121; 1D09C3.
DR DrugBank; DB11294; Coccidioides immitis spherule.
DR GlyConnect; 1377; 1 N-Linked glycan (1 site).
DR GlyGen; P79483; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; P79483; -.
DR PhosphoSitePlus; P79483; -.
DR SwissPalm; P79483; -.
DR BioMuta; HLA-DRB3; -.
DR DMDM; 34395491; -.
DR jPOST; P79483; -.
DR MassIVE; P79483; -.
DR MaxQB; P79483; -.
DR PeptideAtlas; P79483; -.
DR PRIDE; P79483; -.
DR ProteomicsDB; 57661; -.
DR TopDownProteomics; P79483; -.
DR DNASU; 3125; -.
DR Ensembl; ENST00000307137.11; ENSP00000302517.7; ENSG00000196101.9.
DR Ensembl; ENST00000383126.7; ENSP00000372607.3; ENSG00000231679.7.
DR GeneID; 3125; -.
DR KEGG; hsa:3125; -.
DR UCSC; uc011fni.2; human.
DR CTD; 3125; -.
DR DisGeNET; 3125; -.
DR GeneCards; HLA-DRB3; -.
DR HGNC; HGNC:4951; HLA-DRB3.
DR MIM; 612735; gene.
DR neXtProt; NX_P79483; -.
DR PharmGKB; PA35074; -.
DR InParanoid; P79483; -.
DR OrthoDB; 1249505at2759; -.
DR PhylomeDB; P79483; -.
DR PathwayCommons; P79483; -.
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 SignaLink; P79483; -.
DR SIGNOR; P79483; -.
DR BioGRID-ORCS; 3125; 0 hits in 9 CRISPR screens.
DR EvolutionaryTrace; P79483; -.
DR GeneWiki; HLA-DRB3_(gene); -.
DR GenomeRNAi; 3125; -.
DR Pharos; P79483; Tchem.
DR PRO; PR:P79483; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P79483; protein.
DR Bgee; ENSG00000196101; Expressed in lung and 20 other tissues.
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: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:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042613; C:MHC class II protein complex; ISS:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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: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; IDA:UniProtKB.
DR GO; GO:0002469; P:myeloid dendritic cell antigen processing and presentation; IDA:UniProtKB.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR GO; GO:2000516; P:positive regulation of CD4-positive, alpha-beta T cell activation; IDA:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR GO; GO:0002842; P:positive regulation of T cell mediated immune response to tumor cell; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
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; Cell membrane; Cytoplasmic vesicle;
KW Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein; Immunity;
KW Lysosome; Membrane; MHC II; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..266
FT /note="HLA class II histocompatibility antigen, DR beta 3
FT chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000018956"
FT TOPO_DOM 30..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 126..214
FT /note="Ig-like C1-type"
FT REGION 30..124
FT /note="Beta-1"
FT REGION 125..227
FT /note="Beta-2"
FT SITE 40
FT /note="Self-peptide antigen"
FT /evidence="ECO:0000269|PubMed:17583734,
FT ECO:0007744|PDB:2Q6W"
FT SITE 90
FT /note="Self-peptide antigen"
FT /evidence="ECO:0000269|PubMed:17583734,
FT ECO:0007744|PDB:2Q6W"
FT SITE 100
FT /note="Self-peptide antigen"
FT /evidence="ECO:0000269|PubMed:17583734,
FT ECO:0007744|PDB:2Q6W"
FT SITE 110
FT /note="Self-peptide antigen"
FT /evidence="ECO:0000269|PubMed:17583734,
FT ECO:0007744|PDB:2Q6W"
FT SITE 111
FT /note="Self-peptide antigen"
FT /evidence="ECO:0000269|PubMed:17583734,
FT ECO:0007744|PDB:2Q6W"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18697946,
FT ECO:0007744|PDB:3C5J"
FT DISULFID 44..108
FT /evidence="ECO:0000269|PubMed:17583734,
FT ECO:0000269|PubMed:18697946, ECO:0007744|PDB:2Q6W,
FT ECO:0007744|PDB:3C5J"
FT DISULFID 146..202
FT /evidence="ECO:0000269|PubMed:17583734,
FT ECO:0000269|PubMed:18697946, ECO:0007744|PDB:2Q6W,
FT ECO:0007744|PDB:3C5J"
FT VARIANT 37
FT /note="L -> S (in allele DRB3*01:04)"
FT /id="VAR_060739"
FT VARIANT 38
FT /note="E -> Q (in allele DRB3*02:12; dbSNP:rs1071747)"
FT /id="VAR_060740"
FT VARIANT 39
FT /note="L -> Y (in allele DRB3*01:14; requires 2 nucleotide
FT substitutions)"
FT /id="VAR_060741"
FT VARIANT 40
FT /note="R -> C (in allele DRB3*01:02)"
FT /id="VAR_016686"
FT VARIANT 40
FT /note="R -> L (in allele DRB3*02:01, allele DRB3*02:02,
FT allele DRB3*02:03, allele DRB3*02:04, allele DRB3*02:05,
FT allele DRB3*02:06, allele DRB3*02:07, allele DRB3*02:08,
FT allele DRB3*02:09, allele DRB3*02:10, allele DRB3*02:11,
FT allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14,
FT allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17,
FT allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:20,
FT allele DRB3*02:21, allele DRB3*02:22, allele DRB3*02:23,
FT allele DRB3*02:24, allele DRB3*02:25, allele DRB3*03:01,
FT allele DRB3*03:02 and allele DRB3*03:03; dbSNP:rs1071748)"
FT /id="VAR_060742"
FT VARIANT 40
FT /note="R -> S (in allele DRB3*01:14; dbSNP:rs1136752)"
FT /id="VAR_060743"
FT VARIANT 41
FT /note="K -> T (in allele DRB3*01:14; dbSNP:rs200581589)"
FT /id="VAR_060744"
FT VARIANT 55
FT /note="Y -> F (in allele DRB3*01:09, allele DRB3*02:01,
FT allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04,
FT allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:07,
FT allele DRB3*02:08, allele DRB3*02:09, allele DRB3*02:10,
FT allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:14,
FT allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17,
FT allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:20,
FT allele DRB3*02:21, allele DRB3*02:22, allele DRB3*02:23,
FT allele DRB3*02:24, allele DRB3*02:25, allele DRB3*03:01,
FT allele DRB3*03:02 and allele DRB3*03:03;
FT dbSNP:rs147440497)"
FT /id="VAR_060746"
FT VARIANT 55
FT /note="Y -> L (in allele DRB3*02:13; requires 2 nucleotide
FT substitutions)"
FT /id="VAR_060745"
FT VARIANT 57
FT /note="D -> E (in allele DRB3*01:03, allele DRB3*01:09,
FT allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:03,
FT allele DRB3*02:04, allele DRB3*02:05, allele DRB3*02:06,
FT allele DRB3*02:07, allele DRB3*02:08, allele DRB3*02:09,
FT allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:12,
FT allele DRB3*02:13, allele DRB3*02:14, allele DRB3*02:15,
FT allele DRB3*02:16, allele DRB3*02:17, allele DRB3*02:18,
FT allele DRB3*02:19, allele DRB3*02:20, allele DRB3*02:21,
FT allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24,
FT allele DRB3*02:25, allele DRB3*03:01, allele DRB3*03:02 and
FT allele DRB3*03:03; dbSNP:rs202185589)"
FT /id="VAR_060747"
FT VARIANT 57
FT /note="D -> N (in allele DRB3*01:05; dbSNP:rs142793258)"
FT /id="VAR_060748"
FT VARIANT 58
FT /note="R -> I (in allele DRB3*01:11; dbSNP:rs1407020168)"
FT /id="VAR_060749"
FT VARIANT 59
FT /note="Y -> H (in allele DRB3*01:09, allele DRB3*02:01,
FT allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04,
FT allele DRB3*02:06, allele DRB3*02:07, allele DRB3*02:08,
FT allele DRB3*02:09, allele DRB3*02:10, allele DRB3*02:11,
FT allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14,
FT allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17,
FT allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:20,
FT allele DRB3*02:21, allele DRB3*02:22, allele DRB3*02:23,
FT allele DRB3*02:24, allele DRB3*02:25 and allele DRB3*03:02;
FT dbSNP:rs138849995)"
FT /id="VAR_060750"
FT VARIANT 66
FT /note="F -> L (in allele DRB3*01:13; dbSNP:rs707956)"
FT /id="VAR_060752"
FT VARIANT 66
FT /note="F -> N (in allele DRB3*01:08, allele DRB3*02:06 and
FT allele DRB3*02:20; requires 2 nucleotide substitutions)"
FT /id="VAR_060753"
FT VARIANT 66
FT /note="F -> S (in allele DRB3*02:03; dbSNP:rs200042906)"
FT /id="VAR_060751"
FT VARIANT 66
FT /note="F -> Y (in allele DRB3*01:07, allele DRB3*01:09,
FT allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:04,
FT allele DRB3*02:05, allele DRB3*02:07, allele DRB3*02:08,
FT allele DRB3*02:09, allele DRB3*02:10, allele DRB3*02:11,
FT allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14,
FT allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17,
FT allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:21,
FT allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24 and
FT allele DRB3*02:25; dbSNP:rs200042906)"
FT /id="VAR_060754"
FT VARIANT 67
FT /note="L -> A (in allele DRB3*01:07, allele DRB3*01:09,
FT allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:04,
FT allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:07,
FT allele DRB3*02:08, allele DRB3*02:09, allele DRB3*02:10,
FT allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:13,
FT allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:16,
FT allele DRB3*02:17, allele DRB3*02:18, allele DRB3*02:19,
FT allele DRB3*02:21, allele DRB3*02:22, allele DRB3*02:23,
FT allele DRB3*02:24 and allele DRB3*02:25; requires 2
FT nucleotide substitutions)"
FT /id="VAR_060755"
FT VARIANT 67
FT /note="L -> V (in allele DRB3*01:06, allele DRB3*01:08,
FT allele DRB3*02:03, allele DRB3*02:20, allele DRB3*03:01,
FT allele DRB3*03:02 and allele DRB3*03:03; dbSNP:rs1059580)"
FT /id="VAR_060756"
FT VARIANT 68
FT /note="R -> S (in allele DRB3*01:10; dbSNP:rs774894415)"
FT /id="VAR_060757"
FT VARIANT 80
FT /note="T -> R (in allele DRB3*01:07, allele DRB3*02:01,
FT allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04,
FT allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:07,
FT allele DRB3*02:08, allele DRB3*02:11, allele DRB3*02:12,
FT allele DRB3*02:13, allele DRB3*02:14, allele DRB3*02:15,
FT allele DRB3*02:16, allele DRB3*02:17, allele DRB3*02:18,
FT allele DRB3*02:19, allele DRB3*02:20, allele DRB3*02:21,
FT allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24 and
FT allele DRB3*02:25; dbSNP:rs79606458)"
FT /id="VAR_060758"
FT VARIANT 84
FT /note="R -> L (in allele DRB3*02:23)"
FT /id="VAR_060759"
FT VARIANT 86
FT /note="V -> A (in allele DRB3*02:16; dbSNP:rs144532965)"
FT /id="VAR_060760"
FT VARIANT 86
FT /note="V -> D (in allele DRB3*01:07, allele DRB3*02:01,
FT allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04,
FT allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:10,
FT allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:13,
FT allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:17,
FT allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:20,
FT allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24 and
FT allele DRB3*02:25; dbSNP:rs144532965)"
FT /id="VAR_060762"
FT VARIANT 86
FT /note="V -> S (in allele DRB3*02:08; requires 2 nucleotide
FT substitutions)"
FT /id="VAR_060761"
FT VARIANT 87
FT /note="A -> E (in allele DRB3*02:18)"
FT /id="VAR_060763"
FT VARIANT 89
FT /note="S -> H (in allele DRB3*02:16; requires 2 nucleotide
FT substitutions)"
FT /id="VAR_060764"
FT VARIANT 89
FT /note="S -> Y (in allele DRB3*01:07, allele DRB3*02:01,
FT allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04,
FT allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:07,
FT allele DRB3*02:08, allele DRB3*02:10, allele DRB3*02:11,
FT allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14,
FT allele DRB3*02:15, allele DRB3*02:17, allele DRB3*02:18,
FT allele DRB3*02:20, allele DRB3*02:22, allele DRB3*02:23 and
FT allele DRB3*02:24; dbSNP:rs41541218)"
FT /id="VAR_060765"
FT VARIANT 96
FT /note="L -> F (in allele DRB3*02:17; dbSNP:rs696318)"
FT /id="VAR_060766"
FT VARIANT 96
FT /note="L -> I (in allele DRB3*02:11; dbSNP:rs696318)"
FT /id="VAR_060767"
FT VARIANT 102
FT /note="G -> A (in dbSNP:rs17878857)"
FT /id="VAR_033396"
FT VARIANT 103
FT /note="R -> Q (in allele DRB3*01:07, allele DRB3*02:01,
FT allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:05,
FT allele DRB3*02:06, allele DRB3*02:07, allele DRB3*02:08,
FT allele DRB3*02:09, allele DRB3*02:10, allele DRB3*02:11,
FT allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14,
FT allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17,
FT allele DRB3*02:18, allele DRB3*02:20, allele DRB3*02:21,
FT allele DRB3*02:23, allele DRB3*02:24, allele DRB3*02:25,
FT allele DRB3*03:01 and allele DRB3*03:02; dbSNP:rs1059598)"
FT /id="VAR_060768"
FT VARIANT 106
FT /note="N -> T (in allele DRB3*02:15; dbSNP:rs115817940)"
FT /id="VAR_060769"
FT VARIANT 113
FT /note="G -> R (in allele DRB3*01:12)"
FT /id="VAR_060770"
FT VARIANT 114
FT /note="V -> A (in dbSNP:rs1136778)"
FT /id="VAR_033397"
FT VARIANT 115
FT /note="G -> A (in allele DRB3*02:14)"
FT /id="VAR_060771"
FT VARIANT 115
FT /note="G -> V (in allele DRB3*02:01, allele DRB3*02:04,
FT allele DRB3*02:24, allele DRB3*03:01 and allele DRB3*03:02;
FT dbSNP:rs41556512)"
FT /id="VAR_060772"
FT VARIANT 169
FT /note="A -> T (in allele DRB3*03:01; dbSNP:rs75709987)"
FT /id="VAR_060773"
FT VARIANT 178
FT /note="Q -> H (in allele DRB3*03:01; dbSNP:rs139485758)"
FT /id="VAR_060774"
FT VARIANT 193
FT /note="V -> F (in allele DRB3*02:01)"
FT /id="VAR_060775"
FT VARIANT 212
FT /note="A -> P (in allele DRB3*02:01, allele DRB3*02:02,
FT allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:24 and
FT allele DRB3*03:01; dbSNP:rs142204283)"
FT /id="VAR_060776"
FT VARIANT 218
FT /note="R -> S (in allele DRB3*02:01, allele DRB3*02:02,
FT allele DRB3*02:10 and allele DRB3*02:11;
FT dbSNP:rs147669022)"
FT /id="VAR_060777"
FT STRAND 36..47
FT /evidence="ECO:0007829|PDB:2Q6W"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:4H1L"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:2Q6W"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:2Q6W"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2Q6W"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2Q6W"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2Q6W"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:2Q6W"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2Q6W"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2Q6W"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:2Q6W"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:2Q6W"
FT TURN 116..121
FT /evidence="ECO:0007829|PDB:2Q6W"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:2Q6W"
FT STRAND 142..154
FT /evidence="ECO:0007829|PDB:2Q6W"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:2Q6W"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2Q6W"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2Q6W"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2Q6W"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:2Q6W"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:2Q6W"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:2Q6W"
SQ SEQUENCE 266 AA; 29962 MW; 2FC3AE68D3B10EAD CRC64;
MVCLKLPGGS SLAALTVTLM VLSSRLAFAG DTRPRFLELR KSECHFFNGT ERVRYLDRYF
HNQEEFLRFD SDVGEYRAVT ELGRPVAESW NSQKDLLEQK RGRVDNYCRH NYGVGESFTV
QRRVHPQVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG
DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SALTVEWRAR SESAQSKMLS GVGGFVLGLL
FLGAGLFIYF RNQKGHSGLQ PTGFLS
