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HLA class II histocompatibility antigen, DR alpha chain (MHC class II antigen DRA)

 DRA_HUMAN               Reviewed;         254 AA.
P01903; A2BET4; Q30160; Q6IAZ1; Q861I2; Q9TP70;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
18-JUL-2018, entry version 194.
RecName: Full=HLA class II histocompatibility antigen, DR alpha chain;
AltName: Full=MHC class II antigen DRA;
Flags: Precursor;
Name=HLA-DRA; Synonyms=HLA-DRA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRA*01:01).
PubMed=6811954; DOI=10.1038/299750a0;
Lee J.S., Trowsdale J., Travers P.J., Carey J., Grosveld F.,
Jenkins J., Bodmer W.F.;
"Sequence of an HLA-DR alpha-chain cDNA clone and intron-exon
organization of the corresponding gene.";
Nature 299:750-752(1982).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRA*01:01).
PubMed=6416803; DOI=10.1089/dna.1983.2.175;
Kajimura Y., Toyoda H., Sato M., Miyakoshi S., Kaplan S.A., Ike Y.,
Goyert S.M., Silver J., Hawke D., Shively J.E., Suggs S.V.,
Wallace R.B., Itakura K.;
"Cloning the heavy chain of human HLA-DR antigen using synthetic
oligodeoxyribonucleotides as hybridization probes.";
DNA 2:175-182(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRA*01:02).
PubMed=6324094; DOI=10.1093/nar/11.24.8663;
Schamboeck A., Korman A.J., Kamb A., Strominger J.L.;
"Organization of the transcriptional unit of a human class II
histocompatibility antigen: HLA-DR heavy chain.";
Nucleic Acids Res. 11:8663-8675(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRA*01:01).
PubMed=6304715; DOI=10.1073/pnas.80.12.3543;
Das H.K., Lawrance S.K., Weissman S.M.;
"Structure and nucleotide sequence of the heavy chain gene of HLA-
DR.";
Proc. Natl. Acad. Sci. U.S.A. 80:3543-3547(1983).
[5]
ERRATUM, AND SEQUENCE REVISION.
Das H.K., Lawrance S.K., Weissman S.M.;
Proc. Natl. Acad. Sci. U.S.A. 80:7024-7024(1983).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRA*01:02).
PubMed=2212658;
Koppelman B., Cresswell P.;
"Rapid nonlysosomal degradation of assembled HLA class II
glycoproteins incorporating a mutant DR alpha-chain.";
J. Immunol. 145:2730-2736(1990).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRA*01:01).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES DRA*01:01 AND
DRA*01:02).
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRA*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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DRA*01:01 AND
DRA*01:02).
TISSUE=Blood, and Colon;
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).
[11]
PROTEIN SEQUENCE OF 26-204.
PubMed=6955253;
Yang C.-Y., Kratzin H., Gotz H., Thinnes F.P., Kruse T., Egert G.,
Pauly E., Kolbel S., Wernet P., Hilschmann N.;
"Primary structure of class II human histocompatibility antigens. 2nd
Communication. Amino acid sequence of the N-terminal 179 residues of
the alpha-chain of an HLA-Dw2/DR2 alloantigen.";
Hoppe-Seyler's Z. Physiol. Chem. 363:671-676(1982).
[12]
PROTEIN SEQUENCE OF 26-94.
TISSUE=B-cell;
PubMed=6600932; DOI=10.1021/bi00270a027;
Walker L.E., Hewick R., Hunkapiller M.W., Hood L.E., Dreyer W.J.,
Reisfeld R.A.;
"N-terminal amino acid sequences of the alpha and beta chains of HLA-
DR1 and HLA-DR2 antigens.";
Biochemistry 22:185-188(1983).
[13]
PROTEIN SEQUENCE OF 26-60, AND NUCLEOTIDE SEQUENCE [MRNA] OF 32-202
AND 204-254.
PubMed=6812963; DOI=10.1016/0092-8674(82)90021-6;
Larhammar D., Gustafsson K., Claesson L., Bill P., Wiman K.,
Schenning L., Sundelin J., Widmark E., Peterson P.A., Rask L.;
"Alpha chain of HLA-DR transplantation antigens is a member of the
same protein superfamily as the immunoglobulins.";
Cell 30:153-161(1982).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-254 (ALLELE DRA*01:02).
PubMed=6821129; DOI=10.1073/pnas.79.19.6013;
Korman A.J., Auffray C., Schamboeck A., Strominger J.L.;
"The amino acid sequence and gene organization of the heavy chain of
the HLA-DR antigen: homology to immunoglobulins.";
Proc. Natl. Acad. Sci. U.S.A. 79:6013-6017(1982).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-254 (ALLELE DRA*01:02).
TISSUE=Blood;
PubMed=12445311; DOI=10.1034/j.1399-0039.2002.600310.x;
Kralovicova J., Marsh S.G., Waller M.J., Hammarstrom L.,
Vorechovsky I.;
"The HLA-DRA*0102 allele: correct nucleotide sequence and associated
HLA haplotypes.";
Tissue Antigens 60:266-267(2002).
[16]
INVOLVEMENT IN SUSCEPTIBILITY TO HBV INFECTION.
PubMed=9288086; DOI=10.1038/ng0997-11;
Thursz M.R., Thomas H.C., Greenwood B.M., Hill A.V.S.;
"Heterozygote advantage for HLA class-II type in hepatitis B virus
infection.";
Nat. Genet. 17:11-12(1997).
[17]
ERRATUM.
Thursz M.R., Thomas H.C., Greenwood B.M., Hill A.V.S.;
Nat. Genet. 18:88-88(1998).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
SUBCELLULAR LOCATION.
PubMed=18305173; DOI=10.1073/pnas.0708874105;
De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N.,
Pierre P., Gatti E.;
"MHC class II stabilization at the surface of human dendritic cells is
the result of maturation-dependent MARCH I down-regulation.";
Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008).
[23]
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).
[24]
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).
[25]
UBIQUITINATION AT LYS-244 BY MARCH1 AND MARCH8, MUTAGENESIS OF
LYS-244, AND SUBCELLULAR LOCATION.
PubMed=19117940; DOI=10.1074/jbc.M805736200;
Lapaque N., Jahnke M., Trowsdale J., Kelly A.P.;
"The HLA-DRalpha chain is modified by polyubiquitination.";
J. Biol. Chem. 284:7007-7016(2009).
[26]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103 AND ASN-143.
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).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
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).
[29]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-207.
PubMed=8316295; DOI=10.1038/364033a0;
Brown J.H., Jardetzky T.S., Gorga J.C., Stern L.J., Urban R.G.,
Strominger J.L., Wiley D.C.;
"Three-dimensional structure of the human class II histocompatibility
antigen HLA-DR1.";
Nature 364:33-39(1993).
[30]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-207.
PubMed=8145819; DOI=10.1038/368215a0;
Stern L.J., Brown J.H., Jardetzky T.J., Gorga J.C., Urban R.G.,
Strominger J.L., Wiley D.C.;
"Crystal structure of the human class II MHC protein HLA-DR1 complexed
with an influenza virus peptide.";
Nature 368:215-221(1994).
[31]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH SEB.
PubMed=8152483; DOI=10.1038/368711a0;
Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G.,
Chi Y.I., Stauffacher C., Strominger J.L., Wiley D.C.;
"Three-dimensional structure of a human class II histocompatibility
molecule complexed with superantigen.";
Nature 368:711-718(1994).
[32]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 30-205 OF HLA-DRA/HLA-DRB1
HETERODIMER IN COMPLEX WITH CD74 PEPTIDE (CLIP), SUBUNIT,
GLYCOSYLATION AT ASN-103 AND ASN-143, AND DISULFIDE BOND.
PubMed=7477400; DOI=10.1038/378457a0;
Ghosh P., Amaya M., Mellins E., Wiley D.C.;
"The structure of an intermediate in class II MHC maturation: CLIP
bound to HLA-DR3.";
Nature 378:457-462(1995).
[33]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH PEPTIDE FROM
COLLAGEN.
PubMed=9354468; DOI=10.1016/S1074-7613(00)80369-6;
Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C.;
"X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed
with a peptide from human collagen II.";
Immunity 7:473-481(1997).
[34]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH PEPTIDE FROM
MYELIN BASIC PROTEIN.
PubMed=9782128; DOI=10.1084/jem.188.8.1511;
Smith K.J., Pyrdol J., Gauthier L., Wiley D.C., Wucherpfennig K.W.;
"Crystal structure of HLA-DR2 (DRA*0101, DRB1*1501) complexed with a
peptide from human myelin basic protein.";
J. Exp. Med. 188:1511-1520(1998).
[35]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 26-206 OF HLA-DRA/HLA-DRB5
HETERODIMER IN COMPLEX WITH MBP PEPTIDE, AND SUBUNIT.
PubMed=11080454; DOI=10.1006/jmbi.2000.4198;
Li Y., Li H., Martin R., Mariuzza R.A.;
"Structural basis for the binding of an immunodominant peptide from
myelin basic protein in different registers by two HLA-DR2 proteins.";
J. Mol. Biol. 304:177-188(2000).
[36]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-206 OF HLA-DRA/HLA-DRB5
HETERODIMER IN COMPLEX WITH MBP PEPTIDE AND STREPTOCOCCUS PYOGENES
SPEC PEPTIDE, SUBUNIT, AND DISULFIDE BOND.
PubMed=11163233; DOI=10.1016/S1074-7613(01)00092-9;
Li Y., Li H., Dimasi N., McCormick J.K., Martin R., Schuck P.,
Schlievert P.M., Mariuzza R.A.;
"Crystal structure of a superantigen bound to the high-affinity, zinc-
dependent site on MHC class II.";
Immunity 14:93-104(2001).
[37]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 28-207 IN COMPLEX WITH
EPSTEIN-BARR VIRUS BZLF2/GP42 (MICROBIAL INFECTION).
PubMed=11864610; DOI=10.1016/S1097-2765(02)00465-3;
Mullen M.M., Haan K.M., Longnecker R., Jardetzky T.S.;
"Structure of the Epstein-Barr virus gp42 protein bound to the MHC
class II receptor HLA-DR1.";
Mol. Cell 9:375-385(2002).
[38]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 26-207 OF HLA-DRA/HLA-DRB5
HETERODIMER IN COMPLEX EPSTEIN-BARR VIRUS BALF5 PEPTIDE, SUBUNIT, AND
DISULFIDE BOND.
PubMed=12244309; DOI=10.1038/ni835;
Lang H.L.E., Jacobsen H., Ikemizu S., Andersson C., Harlos K.,
Madsen L., Hjorth P., Sondergaard L., Svejgaard A., Wucherpfennig K.,
Stuart D.I., Bell J.I., Jones E.Y., Fugger L.;
"A functional and structural basis for TCR cross-reactivity in
multiple sclerosis.";
Nat. Immunol. 3:940-943(2002).
[39]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-206 OF HLA-DRA/HLA-DRB5
HETERODIMER IN COMPLEX WITH MBP PEPTIDE AND TRAC, SUBUNIT, AND
DISULFIDE BOND.
PubMed=16079912; DOI=10.1038/sj.emboj.7600771;
Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A.;
"Structure of a human autoimmune TCR bound to a myelin basic protein
self-peptide and a multiple sclerosis-associated MHC class II
molecule.";
EMBO J. 24:2968-2979(2005).
[40]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 26-207 OF HLA-DRA/HLA-DRB3
HETERODIMER IN COMPLEX WITH ITGB3 PEPTIDE (ALLOANTIGEN HPA-1A),
SUBUNIT, AND DISULFIDE BOND.
PubMed=17583734; DOI=10.1016/j.jmb.2007.05.025;
Parry C.S., Gorski J., Stern L.J.;
"Crystallographic structure of the human leukocyte antigen DRA,
DRB3*0101: models of a directional alloimmune response and
autoimmunity.";
J. Mol. Biol. 371:435-446(2007).
[41]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 26-206 OF HLA-DRA/HLA-DRB3
HETERODIMER IN COMPLEX WITH EEF1A2 PEPTIDE.
PubMed=18697946; DOI=10.1073/pnas.0805810105;
Dai S., Crawford F., Marrack P., Kappler J.W.;
"The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles.";
Proc. Natl. Acad. Sci. U.S.A. 105:11893-11897(2008).
-!- 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.
{ECO:0000269|PubMed:11080454, ECO:0000269|PubMed:11163233,
ECO:0000269|PubMed:12244309, ECO:0000269|PubMed:16079912,
ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:18697946,
ECO:0000269|PubMed:7477400}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
BZLF2/gp42. {ECO:0000269|PubMed:11864610}.
-!- INTERACTION:
P04229:HLA-DRB1; NbExp=4; IntAct=EBI-1030473, EBI-3865697;
-!- 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. Late endosome 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.
-!- PTM: Ubiquitinated by MARCH1 or MARCH8 at Lys-244 leading to down-
regulation of MHC class II. When associated with ubiquitination of
the beta subunit of HLA-DR: HLA-DRB4 'Lys-254', the down-
regulation of MHC class II may be highly effective.
{ECO:0000269|PubMed:19117940}.
-!- POLYMORPHISM: The following alleles of DRA are known: DRA*01:01
and DRA*01:02. The sequence shown is that of DRA*01:01.
-!- POLYMORPHISM: Genetic variations in HLA-DRA influence
susceptibility to hepatitis B virus (HBV) infection [MIM:610424].
-!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA25076.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; J00194; AAA36275.1; -; mRNA.
EMBL; K01171; AAA59785.1; -; mRNA.
EMBL; X00274; CAA25076.1; ALT_INIT; Genomic_DNA.
EMBL; J00204; AAA36302.1; -; Genomic_DNA.
EMBL; J00203; AAA36302.1; JOINED; Genomic_DNA.
EMBL; M60334; AAA59783.1; -; mRNA.
EMBL; CR457013; CAG33294.1; -; mRNA.
EMBL; AL662796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL670296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL935032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX120007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z84814; CAB06609.1; -; Genomic_DNA.
EMBL; CH471081; EAX03630.1; -; Genomic_DNA.
EMBL; BC032350; AAH32350.1; -; mRNA.
EMBL; BC071659; AAH71659.1; -; mRNA.
EMBL; V00523; CAA23782.1; -; mRNA.
EMBL; J00201; AAA36301.1; -; Genomic_DNA.
EMBL; AF481359; AAO23887.1; -; Genomic_DNA.
CCDS; CCDS4750.1; -.
PIR; A93952; HLHUDA.
RefSeq; NP_061984.2; NM_019111.4.
UniGene; Hs.520048; -.
PDB; 1A6A; X-ray; 2.75 A; A=30-205.
PDB; 1AQD; X-ray; 2.45 A; A/D/G/J=26-217.
PDB; 1BX2; X-ray; 2.60 A; A/D=27-206.
PDB; 1D5M; X-ray; 2.00 A; A=26-206.
PDB; 1D5X; X-ray; 2.45 A; A=26-206.
PDB; 1D5Z; X-ray; 2.00 A; A=26-206.
PDB; 1D6E; X-ray; 2.45 A; A=26-206.
PDB; 1DLH; X-ray; 2.80 A; A/D=28-207.
PDB; 1FV1; X-ray; 1.90 A; A/D=26-206.
PDB; 1FYT; X-ray; 2.60 A; A=26-206.
PDB; 1H15; X-ray; 3.10 A; A/D=26-207.
PDB; 1HQR; X-ray; 3.20 A; A=26-206.
PDB; 1HXY; X-ray; 2.60 A; A=26-207.
PDB; 1J8H; X-ray; 2.40 A; A=26-206.
PDB; 1JWM; X-ray; 2.70 A; A=26-207.
PDB; 1JWS; X-ray; 2.60 A; A=26-207.
PDB; 1JWU; X-ray; 2.30 A; A=26-207.
PDB; 1KG0; X-ray; 2.65 A; A=28-207.
PDB; 1KLG; X-ray; 2.40 A; A=29-205.
PDB; 1KLU; X-ray; 1.93 A; A=29-207.
PDB; 1LO5; X-ray; 3.20 A; A=26-207.
PDB; 1PYW; X-ray; 2.10 A; A=26-207.
PDB; 1R5I; X-ray; 2.60 A; A/E=26-206.
PDB; 1SEB; X-ray; 2.70 A; A/E=26-206.
PDB; 1SJE; X-ray; 2.45 A; A=28-207.
PDB; 1SJH; X-ray; 2.25 A; A=28-207.
PDB; 1T5W; X-ray; 2.40 A; A/D=27-206.
PDB; 1T5X; X-ray; 2.50 A; A=27-207.
PDB; 1YMM; X-ray; 3.50 A; A=26-216.
PDB; 1ZGL; X-ray; 2.80 A; A/D/G/J=26-206.
PDB; 2FSE; X-ray; 3.10 A; A/C=29-205.
PDB; 2G9H; X-ray; 2.00 A; A=26-207.
PDB; 2IAM; X-ray; 2.80 A; A=26-207.
PDB; 2IAN; X-ray; 2.80 A; A/F/K/P=26-207.
PDB; 2ICW; X-ray; 2.41 A; A/D=28-206.
PDB; 2IPK; X-ray; 2.30 A; A=26-207.
PDB; 2OJE; X-ray; 3.00 A; A/E=27-206.
PDB; 2Q6W; X-ray; 2.25 A; A/D=26-207.
PDB; 2SEB; X-ray; 2.50 A; A=26-206.
PDB; 2WBJ; X-ray; 3.00 A; A/E=26-218.
PDB; 2XN9; X-ray; 2.30 A; D=26-207.
PDB; 3C5J; X-ray; 1.80 A; A=26-206.
PDB; 3L6F; X-ray; 2.10 A; A=26-207.
PDB; 3O6F; X-ray; 2.80 A; A/E=26-207.
PDB; 3PDO; X-ray; 1.95 A; A=26-217.
PDB; 3PGC; X-ray; 2.66 A; A/D=26-217.
PDB; 3PGD; X-ray; 2.72 A; A/D=26-217.
PDB; 3QXA; X-ray; 2.71 A; A/D=26-207.
PDB; 3QXD; X-ray; 2.30 A; A/D=26-207.
PDB; 3S4S; X-ray; 2.40 A; A/D=26-207.
PDB; 3S5L; X-ray; 2.10 A; A/D=26-207.
PDB; 3T0E; X-ray; 4.00 A; A=26-207.
PDB; 4AEN; X-ray; 2.20 A; A=26-217.
PDB; 4AH2; X-ray; 2.36 A; A=26-217.
PDB; 4C56; X-ray; 2.90 A; D/J=26-207.
PDB; 4E41; X-ray; 2.60 A; A/F=26-207.
PDB; 4FQX; X-ray; 2.60 A; A=26-216.
PDB; 4GBX; X-ray; 3.00 A; A=26-216.
PDB; 4H1L; X-ray; 3.30 A; A/D=28-205.
PDB; 4H25; X-ray; 2.20 A; A/D=28-207.
PDB; 4H26; X-ray; 2.50 A; A/D=28-206.
PDB; 4I5B; X-ray; 2.12 A; A/D=27-213.
PDB; 4IS6; X-ray; 2.50 A; A=26-207.
PDB; 4MCY; X-ray; 2.30 A; A=26-206.
PDB; 4MCZ; X-ray; 2.41 A; A=26-206.
PDB; 4MD0; X-ray; 2.19 A; A=26-206.
PDB; 4MD4; X-ray; 1.95 A; A=26-206.
PDB; 4MD5; X-ray; 1.65 A; A=26-206.
PDB; 4MDI; X-ray; 2.00 A; A=26-206.
PDB; 4MDJ; X-ray; 1.70 A; A=26-206.
PDB; 4OV5; X-ray; 2.20 A; A/D/G/J/M/P=26-207.
PDB; 4X5W; X-ray; 1.34 A; A=26-217.
PDB; 4X5X; X-ray; 3.20 A; A/C=26-217.
PDB; 4Y19; X-ray; 2.50 A; A=26-206.
PDB; 4Y1A; X-ray; 4.00 A; A=26-206.
PDB; 5JLZ; X-ray; 1.99 A; A/C=26-206.
PDB; 5LAX; X-ray; 2.60 A; A/C=26-206.
PDB; 5V4M; X-ray; 2.10 A; A/D/G/J=26-206.
PDB; 5V4N; X-ray; 3.40 A; A/D=26-206.
PDB; 6ATF; X-ray; 1.90 A; A/D=26-206.
PDB; 6ATI; X-ray; 1.98 A; A/D=26-206.
PDB; 6ATZ; X-ray; 2.70 A; A/C=29-205.
PDB; 6BIJ; X-ray; 2.10 A; A=29-205.
PDB; 6BIL; X-ray; 2.40 A; A=26-206.
PDB; 6BIN; X-ray; 2.50 A; A=30-206.
PDB; 6BIR; X-ray; 2.30 A; A=26-206.
PDB; 6BIV; X-ray; 2.90 A; B=26-206.
PDB; 6BIX; X-ray; 2.20 A; A=26-206.
PDB; 6BIY; X-ray; 2.05 A; A=26-206.
PDB; 6BIZ; X-ray; 2.10 A; A=26-206.
PDB; 6CPL; X-ray; 2.45 A; A=26-254.
PDB; 6CPN; X-ray; 2.00 A; A=26-206.
PDB; 6CPO; X-ray; 2.40 A; A/D=26-207.
PDB; 6CQJ; X-ray; 2.75 A; A/D/G=26-207.
PDB; 6CQL; X-ray; 2.40 A; A=26-206.
PDB; 6CQN; X-ray; 2.50 A; A=26-206.
PDB; 6CQQ; X-ray; 2.80 A; A/F=26-207.
PDB; 6CQR; X-ray; 3.04 A; A/F=26-207.
PDBsum; 1A6A; -.
PDBsum; 1AQD; -.
PDBsum; 1BX2; -.
PDBsum; 1D5M; -.
PDBsum; 1D5X; -.
PDBsum; 1D5Z; -.
PDBsum; 1D6E; -.
PDBsum; 1DLH; -.
PDBsum; 1FV1; -.
PDBsum; 1FYT; -.
PDBsum; 1H15; -.
PDBsum; 1HQR; -.
PDBsum; 1HXY; -.
PDBsum; 1J8H; -.
PDBsum; 1JWM; -.
PDBsum; 1JWS; -.
PDBsum; 1JWU; -.
PDBsum; 1KG0; -.
PDBsum; 1KLG; -.
PDBsum; 1KLU; -.
PDBsum; 1LO5; -.
PDBsum; 1PYW; -.
PDBsum; 1R5I; -.
PDBsum; 1SEB; -.
PDBsum; 1SJE; -.
PDBsum; 1SJH; -.
PDBsum; 1T5W; -.
PDBsum; 1T5X; -.
PDBsum; 1YMM; -.
PDBsum; 1ZGL; -.
PDBsum; 2FSE; -.
PDBsum; 2G9H; -.
PDBsum; 2IAM; -.
PDBsum; 2IAN; -.
PDBsum; 2ICW; -.
PDBsum; 2IPK; -.
PDBsum; 2OJE; -.
PDBsum; 2Q6W; -.
PDBsum; 2SEB; -.
PDBsum; 2WBJ; -.
PDBsum; 2XN9; -.
PDBsum; 3C5J; -.
PDBsum; 3L6F; -.
PDBsum; 3O6F; -.
PDBsum; 3PDO; -.
PDBsum; 3PGC; -.
PDBsum; 3PGD; -.
PDBsum; 3QXA; -.
PDBsum; 3QXD; -.
PDBsum; 3S4S; -.
PDBsum; 3S5L; -.
PDBsum; 3T0E; -.
PDBsum; 4AEN; -.
PDBsum; 4AH2; -.
PDBsum; 4C56; -.
PDBsum; 4E41; -.
PDBsum; 4FQX; -.
PDBsum; 4GBX; -.
PDBsum; 4H1L; -.
PDBsum; 4H25; -.
PDBsum; 4H26; -.
PDBsum; 4I5B; -.
PDBsum; 4IS6; -.
PDBsum; 4MCY; -.
PDBsum; 4MCZ; -.
PDBsum; 4MD0; -.
PDBsum; 4MD4; -.
PDBsum; 4MD5; -.
PDBsum; 4MDI; -.
PDBsum; 4MDJ; -.
PDBsum; 4OV5; -.
PDBsum; 4X5W; -.
PDBsum; 4X5X; -.
PDBsum; 4Y19; -.
PDBsum; 4Y1A; -.
PDBsum; 5JLZ; -.
PDBsum; 5LAX; -.
PDBsum; 5V4M; -.
PDBsum; 5V4N; -.
PDBsum; 6ATF; -.
PDBsum; 6ATI; -.
PDBsum; 6ATZ; -.
PDBsum; 6BIJ; -.
PDBsum; 6BIL; -.
PDBsum; 6BIN; -.
PDBsum; 6BIR; -.
PDBsum; 6BIV; -.
PDBsum; 6BIX; -.
PDBsum; 6BIY; -.
PDBsum; 6BIZ; -.
PDBsum; 6CPL; -.
PDBsum; 6CPN; -.
PDBsum; 6CPO; -.
PDBsum; 6CQJ; -.
PDBsum; 6CQL; -.
PDBsum; 6CQN; -.
PDBsum; 6CQQ; -.
PDBsum; 6CQR; -.
ProteinModelPortal; P01903; -.
SMR; P01903; -.
BioGrid; 109367; 44.
DIP; DIP-6063N; -.
IntAct; P01903; 12.
MINT; P01903; -.
STRING; 9606.ENSP00000378786; -.
Allergome; 8362; Hom s HLA-DR-alpha.
iPTMnet; P01903; -.
PhosphoSitePlus; P01903; -.
SwissPalm; P01903; -.
BioMuta; HLA-DRA; -.
DMDM; 122206; -.
EPD; P01903; -.
MaxQB; P01903; -.
PaxDb; P01903; -.
PeptideAtlas; P01903; -.
PRIDE; P01903; -.
ProteomicsDB; 51508; -.
DNASU; 3122; -.
Ensembl; ENST00000383127; ENSP00000372608; ENSG00000227993.
Ensembl; ENST00000383259; ENSP00000372746; ENSG00000206308.
Ensembl; ENST00000395388; ENSP00000378786; ENSG00000204287.
Ensembl; ENST00000411524; ENSP00000405295; ENSG00000234794.
Ensembl; ENST00000414698; ENSP00000402951; ENSG00000230726.
Ensembl; ENST00000416883; ENSP00000410443; ENSG00000228987.
Ensembl; ENST00000442960; ENSP00000404533; ENSG00000226260.
GeneID; 3122; -.
KEGG; hsa:3122; -.
UCSC; uc003obh.5; human.
CTD; 3122; -.
DisGeNET; 3122; -.
EuPathDB; HostDB:ENSG00000204287.13; -.
GeneCards; HLA-DRA; -.
H-InvDB; HIX0005752; -.
H-InvDB; HIX0031098; -.
H-InvDB; HIX0166957; -.
H-InvDB; HIX0167205; -.
H-InvDB; HIX0167443; -.
HGNC; HGNC:4947; HLA-DRA.
HPA; CAB002798; -.
HPA; CAB015402; -.
HPA; HPA050162; -.
HPA; HPA053176; -.
MalaCards; HLA-DRA; -.
MIM; 142860; gene.
MIM; 610424; phenotype.
neXtProt; NX_P01903; -.
Orphanet; 505; Graham Little-Piccardi-Lassueur syndrome.
PharmGKB; PA35071; -.
eggNOG; ENOG410IZMF; Eukaryota.
eggNOG; ENOG410YHX9; LUCA.
HOVERGEN; HBG006862; -.
InParanoid; P01903; -.
KO; K06752; -.
OrthoDB; EOG091G0IC9; -.
PhylomeDB; P01903; -.
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; P01903; -.
ChiTaRS; HLA-DRA; human.
EvolutionaryTrace; P01903; -.
GeneWiki; HLA-DRA; -.
GenomeRNAi; 3122; -.
PRO; PR:P01903; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204287; -.
CleanEx; HS_HLA-DRA; -.
ExpressionAtlas; P01903; baseline and differential.
Genevisible; P01903; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:MGI.
GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB.
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; TAS:Reactome.
GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IDA:UniProtKB.
GO; GO:0050890; P:cognition; IMP:UniProtKB.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IDA:UniProtKB.
GO; GO:0002506; P:polysaccharide assembly with MHC class II protein complex; IDA:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Endosome; Glycoprotein; Golgi apparatus; Host-virus interaction;
Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Ubl conjugation.
SIGNAL 1 25 {ECO:0000269|PubMed:6600932,
ECO:0000269|PubMed:6812963,
ECO:0000269|PubMed:6955253}.
CHAIN 26 254 HLA class II histocompatibility antigen,
DR alpha chain.
/FTId=PRO_0000018947.
TOPO_DOM 26 216 Extracellular. {ECO:0000255}.
TRANSMEM 217 239 Helical. {ECO:0000255}.
TOPO_DOM 240 254 Cytoplasmic. {ECO:0000255}.
DOMAIN 112 204 Ig-like C1-type.
REGION 26 109 Alpha-1.
REGION 110 203 Alpha-2.
REGION 204 216 Connecting peptide.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:7477400}.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:7477400}.
DISULFID 132 188 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:11163233,
ECO:0000269|PubMed:12244309,
ECO:0000269|PubMed:16079912,
ECO:0000269|PubMed:17583734,
ECO:0000269|PubMed:7477400}.
CROSSLNK 244 244 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19117940}.
VARIANT 16 16 V -> L (in dbSNP:rs16822586).
/FTId=VAR_035241.
VARIANT 242 242 V -> L (in allele DRA*01:02;
dbSNP:rs7192).
/FTId=VAR_004399.
MUTAGEN 244 244 K->R: Almost no change in down-regulation
of MHC class II. No ubiquitination and
complete loss of down-regulation of MHC
class II; when associated with 'R-254' of
HLA-DRB. {ECO:0000269|PubMed:19117940}.
CONFLICT 28 29 EE -> AD (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 33 33 I -> T (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 34 35 QA -> YP (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 48 48 M -> Q (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 54 54 D -> T (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 59 59 V -> Y (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 64 64 K -> L (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 67 67 V -> A (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 69 69 R -> L (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 75 75 R -> P (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 78 78 S -> D (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 149 149 N -> E (in Ref. 11; AA sequence).
{ECO:0000305}.
STRAND 28 40 {ECO:0000244|PDB:4X5W}.
TURN 41 43 {ECO:0000244|PDB:4X5W}.
STRAND 44 51 {ECO:0000244|PDB:4X5W}.
STRAND 54 60 {ECO:0000244|PDB:4X5W}.
TURN 61 64 {ECO:0000244|PDB:4X5W}.
STRAND 65 70 {ECO:0000244|PDB:4X5W}.
HELIX 71 75 {ECO:0000244|PDB:4X5W}.
HELIX 82 101 {ECO:0000244|PDB:4X5W}.
TURN 102 104 {ECO:0000244|PDB:3C5J}.
STRAND 113 120 {ECO:0000244|PDB:4X5W}.
STRAND 124 126 {ECO:0000244|PDB:3S4S}.
STRAND 128 140 {ECO:0000244|PDB:4X5W}.
STRAND 143 148 {ECO:0000244|PDB:4X5W}.
STRAND 151 153 {ECO:0000244|PDB:4X5W}.
STRAND 155 159 {ECO:0000244|PDB:2FSE}.
STRAND 166 168 {ECO:0000244|PDB:6BIV}.
STRAND 170 178 {ECO:0000244|PDB:4X5W}.
STRAND 186 191 {ECO:0000244|PDB:4X5W}.
STRAND 195 197 {ECO:0000244|PDB:3C5J}.
STRAND 199 203 {ECO:0000244|PDB:4X5W}.
SEQUENCE 254 AA; 28607 MW; 3CD1CDBA952B2350 CRC64;
MAISGVPVLG FFIIAVLMSA QESWAIKEEH VIIQAEFYLN PDQSGEFMFD FDGDEIFHVD
MAKKETVWRL EEFGRFASFE AQGALANIAV DKANLEIMTK RSNYTPITNV PPEVTVLTNS
PVELREPNVL ICFIDKFTPP VVNVTWLRNG KPVTTGVSET VFLPREDHLF RKFHYLPFLP
STEDVYDCRV EHWGLDEPLL KHWEFDAPSP LPETTENVVC ALGLTVGLVG IIIGTIFIIK
GVRKSNAAER RGPL


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U1752h CLIA HLA class I histocompatibility antigen, alpha chain E,HLA-6.2,HLAE,HLA-E,Homo sapiens,Human,MHC class I antigen E 96T
E1752h ELISA kit HLA class I histocompatibility antigen, alpha chain E,HLA-6.2,HLAE,HLA-E,Homo sapiens,Human,MHC class I antigen E 96T
E1752h ELISA HLA class I histocompatibility antigen, alpha chain E,HLA-6.2,HLAE,HLA-E,Homo sapiens,Human,MHC class I antigen E 96T
EIAAB11895 HLA class II histocompatibility antigen, DR alpha chain,HLA-DRA,HLA-DRA1,Homo sapiens,Human,MHC class II antigen DRA
EIAAB11449 DMA,HLA class II histocompatibility antigen, DM alpha chain,HLA-DMA,Homo sapiens,Human,MHC class II antigen DMA,Really interesting new gene 6 protein,RING6
EIAAB11639 HLA class II histocompatibility antigen, DO alpha chain,HLA-DNA,HLA-DOA,HLA-DZA,Homo sapiens,Human,MHC class II antigen DOA,MHC DN-alpha,MHC DZ alpha
EIAAB11729 HLA class II histocompatibility antigen, DP beta 1 chain,HLA class II histocompatibility antigen, DP(W4) beta chain,HLA-DP1B,HLA-DPB1,Homo sapiens,Human,MHC class II antigen DPB1
EIAAB11726 DP(W3),DP(W4),HLA class II histocompatibility antigen, DP alpha 1 chain,HLA-DP1A,HLA-DPA1,HLASB,HLA-SB alpha chain,Homo sapiens,Human,MHC class II DP3-alpha,MHC class II DPA1
EIAAB11886 HLA class II histocompatibility antigen, DQ beta 2 chain,HLA class II histocompatibility antigen, DX beta chain,HLA-DQB2,HLA-DXB,Homo sapiens,Human,MHC class II antigen DQB2
EIAAB11453 DMB,HLA class II histocompatibility antigen, DM beta chain,HLA-DMB,Homo sapiens,Human,MHC class II antigen DMB,Really interesting new gene 7 protein,RING7
EIAAB11640 HLA class II histocompatibility antigen, DO beta chain,HLA-DOB,Homo sapiens,Human,MHC class II antigen DOB
EIAAB11883 DC-1 alpha chain,DC-alpha,HLA class II histocompatibility antigen, DQ alpha 1 chain,HLA-DCA,HLA-DQA1,Homo sapiens,Human,MHC class II DQA1
U1702m CLIA H-2 class I histocompatibility antigen, Q7 alpha chain,H2-Q7,Mouse,Mus musculus,QA-2 antigen 96T
E1702m ELISA H-2 class I histocompatibility antigen, Q7 alpha chain,H2-Q7,Mouse,Mus musculus,QA-2 antigen 96T
E1702m ELISA kit H-2 class I histocompatibility antigen, Q7 alpha chain,H2-Q7,Mouse,Mus musculus,QA-2 antigen 96T
U1555m CLIA H-2 class I histocompatibility antigen, TLA(B) alpha chain,H2-T3,MHC thymus leukemia antigen,Mouse,Mus musculus 96T
E1555m ELISA H-2 class I histocompatibility antigen, TLA(B) alpha chain,H2-T3,MHC thymus leukemia antigen,Mouse,Mus musculus 96T
E1555m ELISA kit H-2 class I histocompatibility antigen, TLA(B) alpha chain,H2-T3,MHC thymus leukemia antigen,Mouse,Mus musculus 96T
EIAAB11903 HLA class II histocompatibility antigen, DR beta 3 chain,HLA-DRB3,Homo sapiens,Human,MHC class II antigen DRB3
EIAAB11885 HLA class II histocompatibility antigen, DQ beta 1 chain,HLA-DQB,HLA-DQB1,Homo sapiens,Human,MHC class II antigen DQB1
EIAAB11904 HLA class II histocompatibility antigen, DR beta 4 chain,HLA-DRB4,Homo sapiens,Human,MHC class II antigen DRB4


 

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