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HLA class II histocompatibility antigen, DM alpha chain (MHC class II antigen DMA) (Really interesting new gene 6 protein)

 DMA_HUMAN               Reviewed;         261 AA.
P28067; Q29639; Q29640;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
12-SEP-2018, entry version 172.
RecName: Full=HLA class II histocompatibility antigen, DM alpha chain;
AltName: Full=MHC class II antigen DMA;
AltName: Full=Really interesting new gene 6 protein;
Flags: Precursor;
Name=HLA-DMA; Synonyms=DMA, RING6;
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 DMA*01:01).
PubMed=1922365; DOI=10.1038/353571a0;
Kelly A.P., Monaco J.J., Cho S., Trowsdale J.;
"A new human HLA class II-related locus, DM.";
Nature 353:571-573(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-218 (ALLELE DMA*01:02).
PubMed=8225438; DOI=10.1007/BF00171797;
Sanderson F., Powis S.H., Kelly A.P., Trowsdale J.;
"Limited polymorphism in HLA-DM does not involve the peptide binding
groove.";
Immunogenetics 39:56-58(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-217 (ALLELES DMA*01:03 AND
DMA*01:04).
PubMed=8026867; DOI=10.1007/BF00188184;
Carrington M., Harding A.;
"Sequence analysis of two novel HLA-DMA alleles.";
Immunogenetics 40:165-165(1994).
[5]
FUNCTION.
PubMed=8849454; DOI=10.1126/science.274.5287.618;
Weber D.A., Evavold B.D., Jensen P.E.;
"Enhanced dissociation of HLA-DR-bound peptides in the presence of
HLA-DM.";
Science 274:618-620(1996).
[6]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-230 IN COMPLEX WITH DMB,
FUNCTION, SUBUNIT, AND DISULFIDE BONDS.
PubMed=9768757; DOI=10.1016/S1074-7613(00)80620-2;
Mosyak L., Zaller D.M., Wiley D.C.;
"The structure of HLA-DM, the peptide exchange catalyst that loads
antigen onto class II MHC molecules during antigen presentation.";
Immunity 9:377-383(1998).
[7]
X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 27-229 IN COMPLEX WITH DMB,
FUNCTION, SUBUNIT, AND DISULFIDE BONDS.
PubMed=16547258; DOI=10.4049/jimmunol.176.7.4208;
Nicholson M.J., Moradi B., Seth N.P., Xing X., Cuny G.D., Stein R.L.,
Wucherpfennig K.W.;
"Small molecules that enhance the catalytic efficiency of HLA-DM.";
J. Immunol. 176:4208-4220(2006).
-!- FUNCTION: Plays a critical role in catalyzing the release of class
II-associated invariant chain peptide (CLIP) from newly
synthesized MHC class II molecules and freeing the peptide binding
site for acquisition of antigenic peptides. In B-cells, the
interaction between HLA-DM and MHC class II molecules is regulated
by HLA-DO. {ECO:0000269|PubMed:16547258,
ECO:0000269|PubMed:8849454, ECO:0000269|PubMed:9768757}.
-!- SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain
(DMB). {ECO:0000269|PubMed:16547258, ECO:0000269|PubMed:9768757}.
-!- SUBCELLULAR LOCATION: Late endosome membrane; Single-pass type I
membrane protein. Lysosome membrane; Single-pass type I membrane
protein. Note=Localizes to late endocytic compartment. Associates
with lysosome membranes.
-!- POLYMORPHISM: The following alleles of DMA are known: DMA*01:01,
DMA*01:02, DMA*01:03 (DMA3.2) and DMA*01:04 (DMA3.4). The sequence
shown is that of DMA*01:01.
-!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X62744; CAA44606.1; -; mRNA.
EMBL; AL935042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z24753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U04878; AAA56994.1; -; Genomic_DNA.
EMBL; U04877; AAA56993.1; -; Genomic_DNA.
CCDS; CCDS4761.1; -.
PIR; I38490; I38490.
PIR; S17886; S17886.
UniGene; Hs.728759; -.
PDB; 1HDM; X-ray; 2.50 A; A=27-230.
PDB; 2BC4; X-ray; 2.27 A; A/C=27-229.
PDB; 4FQX; X-ray; 2.60 A; C=27-225.
PDB; 4GBX; X-ray; 3.00 A; C=27-225.
PDBsum; 1HDM; -.
PDBsum; 2BC4; -.
PDBsum; 4FQX; -.
PDBsum; 4GBX; -.
ProteinModelPortal; P28067; -.
SMR; P28067; -.
DIP; DIP-6184N; -.
IntAct; P28067; 7.
MINT; P28067; -.
STRING; 9606.ENSP00000363976; -.
iPTMnet; P28067; -.
PhosphoSitePlus; P28067; -.
DMDM; 133158; -.
EPD; P28067; -.
MaxQB; P28067; -.
PaxDb; P28067; -.
PeptideAtlas; P28067; -.
PRIDE; P28067; -.
ProteomicsDB; 54442; -.
Ensembl; ENST00000374843; ENSP00000363976; ENSG00000204257.
Ensembl; ENST00000383230; ENSP00000372717; ENSG00000243215.
Ensembl; ENST00000434337; ENSP00000407198; ENSG00000242361.
Ensembl; ENST00000441375; ENSP00000410591; ENSG00000239463.
Ensembl; ENST00000450601; ENSP00000392842; ENSG00000242685.
Ensembl; ENST00000452615; ENSP00000395349; ENSG00000243189.
Ensembl; ENST00000453490; ENSP00000404018; ENSG00000243719.
DisGeNET; 3108; -.
EuPathDB; HostDB:ENSG00000204257.14; -.
GeneCards; HLA-DMA; -.
H-InvDB; HIX0207683; -.
HGNC; HGNC:4934; HLA-DMA.
HPA; HPA012750; -.
HPA; HPA017295; -.
MIM; 142855; gene.
neXtProt; NX_P28067; -.
eggNOG; ENOG410IR26; Eukaryota.
eggNOG; ENOG410YJDD; LUCA.
HOGENOM; HOG000126882; -.
HOVERGEN; HBG001688; -.
InParanoid; P28067; -.
OrthoDB; EOG091G0LMN; -.
PhylomeDB; P28067; -.
TreeFam; TF333797; -.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
SIGNOR; P28067; -.
ChiTaRS; HLA-DMA; human.
EvolutionaryTrace; P28067; -.
PRO; PR:P28067; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204257; Expressed in 207 organ(s), highest expression level in small intestine Peyer's patch.
CleanEx; HS_HLA-DMA; -.
ExpressionAtlas; P28067; baseline and differential.
Genevisible; P28067; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB.
GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.320.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR014745; MHC_II_a/b_N.
InterPro; IPR001003; MHC_II_a_N.
Pfam; PF07654; C1-set; 1.
Pfam; PF00993; MHC_II_alpha; 1.
SMART; SM00407; IGc1; 1.
SMART; SM00920; MHC_II_alpha; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Endosome;
Glycoprotein; Immunity; Lysosome; Membrane; MHC II; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 261 HLA class II histocompatibility antigen,
DM alpha chain.
/FTId=PRO_0000018958.
TOPO_DOM 27 233 Lumenal. {ECO:0000255}.
TRANSMEM 234 254 Helical. {ECO:0000255}.
TOPO_DOM 255 261 Cytoplasmic. {ECO:0000255}.
DOMAIN 121 215 Ig-like C1-type.
REGION 27 124 Alpha-1.
REGION 125 217 Alpha-2.
REGION 218 233 Connecting peptide. {ECO:0000255}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 50 105
DISULFID 147 202
VARIANT 162 162 H -> Q (in allele DMA*01:03 and allele
DMA*01:04).
/FTId=VAR_016746.
VARIANT 163 163 D -> H (in allele DMA*01:03 and allele
DMA*01:04).
/FTId=VAR_016747.
VARIANT 166 166 V -> I (in allele DMA*01:02 and allele
DMA*01:04; dbSNP:rs1063478).
/FTId=VAR_016748.
VARIANT 181 181 G -> A (in allele DMA*01:03;
dbSNP:rs6926628).
/FTId=VAR_016749.
VARIANT 210 210 R -> C (in allele DMA*01:04;
dbSNP:rs17214044).
/FTId=VAR_016750.
VARIANT 210 210 R -> H (in allele DMA*01:03;
dbSNP:rs41555121).
/FTId=VAR_016751.
VARIANT 235 235 V -> M (in dbSNP:rs9469319).
/FTId=VAR_056544.
STRAND 41 63 {ECO:0000244|PDB:2BC4}.
STRAND 66 72 {ECO:0000244|PDB:2BC4}.
TURN 73 76 {ECO:0000244|PDB:2BC4}.
STRAND 77 82 {ECO:0000244|PDB:2BC4}.
HELIX 83 85 {ECO:0000244|PDB:2BC4}.
HELIX 87 89 {ECO:0000244|PDB:2BC4}.
HELIX 95 110 {ECO:0000244|PDB:2BC4}.
TURN 114 116 {ECO:0000244|PDB:2BC4}.
TURN 117 119 {ECO:0000244|PDB:1HDM}.
STRAND 122 124 {ECO:0000244|PDB:4FQX}.
STRAND 128 135 {ECO:0000244|PDB:2BC4}.
STRAND 143 155 {ECO:0000244|PDB:2BC4}.
STRAND 157 163 {ECO:0000244|PDB:2BC4}.
STRAND 166 168 {ECO:0000244|PDB:2BC4}.
STRAND 175 179 {ECO:0000244|PDB:2BC4}.
TURN 180 182 {ECO:0000244|PDB:2BC4}.
STRAND 183 192 {ECO:0000244|PDB:2BC4}.
STRAND 200 206 {ECO:0000244|PDB:2BC4}.
TURN 207 210 {ECO:0000244|PDB:2BC4}.
STRAND 211 217 {ECO:0000244|PDB:2BC4}.
SEQUENCE 261 AA; 29194 MW; 1986C3C1989F02E9 CRC64;
MGHEQNQGAA LLQMLPLLWL LPHSWAVPEA PTPMWPDDLQ NHTFLHTVYC QDGSPSVGLS
EAYDEDQLFF FDFSQNTRVP RLPEFADWAQ EQGDAPAILF DKEFCEWMIQ QIGPKLDGKI
PVSRGFPIAE VFTLKPLEFG KPNTLVCFVS NLFPPMLTVN WHDHSVPVEG FGPTFVSAVD
GLSFQAFSYL NFTPEPSDIF SCIVTHEIDR YTAIAYWVPR NALPSDLLEN VLCGVAFGLG
VLGIIVGIVL IIYFRKPCSG D


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