[1]	NUCLEOTIDE SEQUENCE [MRNA] (DMA*0101). DOI=10.1038/353571a0; PubMed=1922365 [NCBI, ExPASy, EBI, Israel, Japan] 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 [GENOMIC DNA] OF 31-218 (DMA*0102). DOI=10.1007/BF00171797; PubMed=8225438 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-217 (DMA0103 AND DMA0104). DOI=10.1007/BF00188184; PubMed=8026867 [NCBI, ExPASy, EBI, Israel, Japan] Carrington M., Harding A.; "Sequence analysis of two novel HLA-DMA alleles."; Immunogenetics 40:165-165(1994).
[4]	FUNCTION. DOI=10.1126/science.274.5287.618; PubMed=8849454 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[5]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-230. DOI=10.1016/S1074-7613(00)80620-2; PubMed=9768757 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: Plays a critical role in catalyzing the release of class II HLA-associated invariant chain-derived peptides (CLIP) from newly synthesized class II HLA molecules and freeing the peptide binding site for acquisition of antigenic peptides.
SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain (DMB).
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*0101, DMA*0102, DMA*0103 (DMA3.2) and DMA*0104 (DMA3.4). The sequence shown is that of DMA*0101.
SIMILARITY: Belongs to the MHC class II family.
SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X62744; CAA44606.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z24753; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
U04878; AAA56994.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U04877; AAA56993.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00291924; -.

PIR

I38490; I38490.
S17886; S17886.

UniGene

Hs.351279

3D structure databases

PDB

1HDM; X-ray; 2.50 A; A=27-230.

[ExPASy / RCSB / EBI]

PDBsum

1HDM; -.

ModBase

P28067.

Protein-protein interaction databases

DIP

DIP:6184N; -.

Enzyme and pathway databases

Reactome

REACT_6900; Signaling in Immune system.

Organism-specific databases

GC06M033024; -.

HGNC:4934; HLA-DMA.

CAB016176; -.
HPA012750; -.

MIM

142855; gene. [NCBI / EBI]

PharmGKB

PA35058; -.

Gene expression databases

P28067; -.

P28067; -.

HS_HLA-DMA; -.

ENSG00000204257; Homo sapiens.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031902;	Cellular component: late endosome membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005765;	Cellular component: lysosomal membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0042613;	Cellular component: MHC class II protein complex (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR003006; Ig/MHC_CS.
IPR003597; Ig_C1-set.
IPR014745; MHC_II_a/b_N.
IPR001003; MHC_II_a_N.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.10; Ig-like_fold; 1.
G3DSA:3.10.320.10; MHC_II_alpha_N; 1.

Pfam

PF07654; C1-set; 1.
PF00993; MHC_II_alpha; 1.
Pfam graphical view of domain structure.

SMART

SM00407; IGc1; 1.
SMART graphical view of domain structure.

PROSITE

PS50835; IG_LIKE; 1.
PS00290; IG_MHC; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSG00000204257; Homo sapiens. [Contig view]
ENSG00000206229; Homo sapiens. [Contig view]
ENSG00000206293; Homo sapiens. [Contig view]

Phylogenomic databases

HOGENOM

P28067; -.

HOVERGEN

P28067; -.

Other

NextBio

12333; -.

SOURCE

HLA-DMA; Homo sapiens.

ProtoNet

P28067.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Disulfide bond; Endosome; Glycoprotein; Immune response; Lysosome; Membrane; MHC II; Polymorphism; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 26`	`26`	`Potential.`
`CHAIN`	`27 261`	`235`	`HLA class II histocompatibility antigen, DM alpha chain.`	`PRO_0000018958`
`TOPO_DOM`	`27 233`	`207`	`Lumenal (Potential).`
`TRANSMEM`	`234 254`	`21`	`Potential.`
`TOPO_DOM`	`255 261`	`7`	`Cytoplasmic (Potential).`
`DOMAIN`	`121 215`	`95`	`Ig-like C1-type.`
`REGION`	`27 124`	`98`	`Alpha-1.`
`REGION`	`125 217`	`93`	`Alpha-2.`
`REGION`	`218 233`	`16`	`Connecting peptide (Potential).`
`CARBOHYD`	`41 41`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`147 202`		`By similarity.`
`VARIANT`	`162 162`	`1`	`H -> Q (in allele DMA0103 and allele DMA0104).`	`VAR_016746 [3D]`
`VARIANT`	`163 163`	`1`	`D -> H (in allele DMA0103 and allele DMA0104).`	`VAR_016747 [3D]`
`VARIANT`	`166 166`	`1`	`V -> I (in allele DMA0102 and allele DMA0104; dbSNP:rs1063478 [NCBI]).`	`VAR_016748 [3D]`
`VARIANT`	`181 181`	`1`	`G -> A (in allele DMA*0103; dbSNP:rs6926628 [NCBI]).`	`VAR_016749 [3D]`
`VARIANT`	`210 210`	`1`	`R -> C (in allele DMA*0104; dbSNP:rs17214044 [NCBI]).`	`VAR_016750 [3D]`
`VARIANT`	`210 210`	`1`	`R -> H (in allele DMA*0103).`	`VAR_016751 [3D]`
`VARIANT`	`235 235`	`1`	`V -> M (in dbSNP:rs9469319 [NCBI]).`	`VAR_056544`
`STRAND`	`41 63`	`23`
`STRAND`	`66 72`	`7`
`TURN`	`73 76`	`4`
`STRAND`	`77 82`	`6`
`HELIX`	`83 88`	`6`
`HELIX`	`98 111`	`14`
`TURN`	`117 119`	`3`
`STRAND`	`128 135`	`8`
`STRAND`	`143 155`	`13`
`STRAND`	`157 163`	`7`
`STRAND`	`174 179`	`6`
`TURN`	`180 182`	`3`
`STRAND`	`183 192`	`10`
`STRAND`	`200 206`	`7`
`TURN`	`207 210`	`4`
`STRAND`	`211 217`	`7`

Sequence information

Length: 261 AA [This is the length of the unprocessed precursor]

Molecular weight: 29194 Da [This is the MW of the unprocessed precursor]

CRC64: 1986C3C1989F02E9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGHEQNQGAA LLQMLPLLWL LPHSWAVPEA PTPMWPDDLQ NHTFLHTVYC QDGSPSVGLS 

        70         80         90        100        110        120 
EAYDEDQLFF FDFSQNTRVP RLPEFADWAQ EQGDAPAILF DKEFCEWMIQ QIGPKLDGKI 

       130        140        150        160        170        180 
PVSRGFPIAE VFTLKPLEFG KPNTLVCFVS NLFPPMLTVN WHDHSVPVEG FGPTFVSAVD 

       190        200        210        220        230        240 
GLSFQAFSYL NFTPEPSDIF SCIVTHEIDR YTAIAYWVPR NALPSDLLEN VLCGVAFGLG 

       250        260 
VLGIIVGIVL IIYFRKPCSG D

P28067 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools