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P28067

- DMA_HUMAN

UniProt

P28067 - DMA_HUMAN

Protein

HLA class II histocompatibility antigen, DM alpha chain

Gene

HLA-DMA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    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.3 Publications

    GO - Molecular functioni

    1. MHC class II protein complex binding Source: UniProt

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. chaperone mediated protein folding requiring cofactor Source: Ensembl
    3. immunoglobulin mediated immune response Source: Ensembl
    4. inner ear development Source: Ensembl
    5. peptide antigen assembly with MHC class II protein complex Source: UniProt
    6. positive regulation of immune response Source: Ensembl
    7. positive regulation of T cell differentiation Source: Ensembl
    8. positive thymic T cell selection Source: Ensembl
    9. protein transport Source: Ensembl

    Keywords - Biological processi

    Immunity

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    HLA class II histocompatibility antigen, DM alpha chain
    Alternative name(s):
    MHC class II antigen DMA
    Really interesting new gene 6 protein
    Gene namesi
    Name:HLA-DMA
    Synonyms:DMA, RING6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4934. HLA-DMA.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cell surface Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: UniProtKB-KW
    4. late endosome membrane Source: UniProtKB-SubCell
    5. lysosomal membrane Source: Reactome
    6. membrane Source: UniProtKB
    7. MHC class II protein complex Source: UniProt
    8. multivesicular body Source: Ensembl

    Keywords - Cellular componenti

    Endosome, Lysosome, Membrane, MHC II

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 261235HLA class II histocompatibility antigen, DM alpha chainPRO_0000018958Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi50 ↔ 105
    Disulfide bondi147 ↔ 202

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP28067.
    PRIDEiP28067.

    PTM databases

    PhosphoSiteiP28067.

    Expressioni

    Gene expression databases

    ArrayExpressiP28067.
    BgeeiP28067.
    CleanExiHS_HLA-DMA.
    GenevestigatoriP28067.

    Organism-specific databases

    HPAiHPA012750.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha chain (DMA) and a beta chain (DMB).2 Publications

    Protein-protein interaction databases

    DIPiDIP-6184N.
    IntActiP28067. 7 interactions.
    MINTiMINT-1539780.
    STRINGi9606.ENSP00000408311.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi41 – 6323
    Beta strandi66 – 727
    Turni73 – 764
    Beta strandi77 – 826
    Helixi83 – 853
    Helixi87 – 893
    Helixi95 – 11016
    Turni114 – 1163
    Turni117 – 1193
    Beta strandi122 – 1243
    Beta strandi128 – 1358
    Beta strandi143 – 15513
    Beta strandi157 – 1637
    Beta strandi166 – 1683
    Beta strandi175 – 1795
    Turni180 – 1823
    Beta strandi183 – 19210
    Beta strandi200 – 2067
    Turni207 – 2104
    Beta strandi211 – 2177

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HDMX-ray2.50A27-230[»]
    2BC4X-ray2.27A/C27-229[»]
    4FQXX-ray2.60C27-225[»]
    4GBXX-ray3.00C27-225[»]
    ProteinModelPortaliP28067.
    SMRiP28067. Positions 38-230.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28067.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 233207LumenalSequence AnalysisAdd
    BLAST
    Topological domaini255 – 2617CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei234 – 25421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini121 – 21595Ig-like C1-typeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 12498Alpha-1Add
    BLAST
    Regioni125 – 21793Alpha-2Add
    BLAST
    Regioni218 – 23316Connecting peptideSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MHC class II family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG43075.
    HOGENOMiHOG000126882.
    HOVERGENiHBG001688.
    InParanoidiP28067.
    PhylomeDBiP28067.
    TreeFamiTF333797.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.10.320.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    IPR011162. MHC_I/II-like_Ag-recog.
    IPR014745. MHC_II_a/b_N.
    IPR001003. MHC_II_a_N.
    [Graphical view]
    PfamiPF07654. C1-set. 1 hit.
    PF00993. MHC_II_alpha. 1 hit.
    [Graphical view]
    SMARTiSM00407. IGc1. 1 hit.
    SM00920. MHC_II_alpha. 1 hit.
    [Graphical view]
    SUPFAMiSSF54452. SSF54452. 1 hit.
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P28067-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGHEQNQGAA LLQMLPLLWL LPHSWAVPEA PTPMWPDDLQ NHTFLHTVYC    50
    QDGSPSVGLS EAYDEDQLFF FDFSQNTRVP RLPEFADWAQ EQGDAPAILF 100
    DKEFCEWMIQ QIGPKLDGKI PVSRGFPIAE VFTLKPLEFG KPNTLVCFVS 150
    NLFPPMLTVN WHDHSVPVEG FGPTFVSAVD GLSFQAFSYL NFTPEPSDIF 200
    SCIVTHEIDR YTAIAYWVPR NALPSDLLEN VLCGVAFGLG VLGIIVGIVL 250
    IIYFRKPCSG D 261
    Length:261
    Mass (Da):29,194
    Last modified:August 1, 1992 - v1
    Checksum:i1986C3C1989F02E9
    GO

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti162 – 1621H → Q in allele DMA*01:03 and allele DMA*01:04.
    VAR_016746
    Natural varianti163 – 1631D → H in allele DMA*01:03 and allele DMA*01:04.
    VAR_016747
    Natural varianti166 – 1661V → I in allele DMA*01:02 and allele DMA*01:04.
    Corresponds to variant rs1063478 [ dbSNP | Ensembl ].
    VAR_016748
    Natural varianti181 – 1811G → A in allele DMA*01:03.
    Corresponds to variant rs6926628 [ dbSNP | Ensembl ].
    VAR_016749
    Natural varianti210 – 2101R → C in allele DMA*01:04.
    Corresponds to variant rs17214044 [ dbSNP | Ensembl ].
    VAR_016750
    Natural varianti210 – 2101R → H in allele DMA*01:03.
    Corresponds to variant rs41555121 [ dbSNP | Ensembl ].
    VAR_016751
    Natural varianti235 – 2351V → M.
    Corresponds to variant rs9469319 [ dbSNP | Ensembl ].
    VAR_056544

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62744 mRNA. Translation: CAA44606.1.
    AL935042 Genomic DNA. No translation available.
    Z24753 Genomic DNA. No translation available.
    U04878 Genomic DNA. Translation: AAA56994.1.
    U04877 Genomic DNA. Translation: AAA56993.1.
    CCDSiCCDS4761.1.
    PIRiI38490.
    S17886.
    UniGeneiHs.728759.

    Genome annotation databases

    EnsembliENST00000374843; ENSP00000363976; ENSG00000204257.
    ENST00000383230; ENSP00000372717; ENSG00000243215.
    ENST00000434337; ENSP00000407198; ENSG00000242361.
    ENST00000441375; ENSP00000410591; ENSG00000239463.
    ENST00000450601; ENSP00000392842; ENSG00000242685.
    ENST00000452615; ENSP00000395349; ENSG00000243189.
    ENST00000453490; ENSP00000404018; ENSG00000243719.

    Polymorphism databases

    DMDMi133158.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62744 mRNA. Translation: CAA44606.1 .
    AL935042 Genomic DNA. No translation available.
    Z24753 Genomic DNA. No translation available.
    U04878 Genomic DNA. Translation: AAA56994.1 .
    U04877 Genomic DNA. Translation: AAA56993.1 .
    CCDSi CCDS4761.1.
    PIRi I38490.
    S17886.
    UniGenei Hs.728759.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HDM X-ray 2.50 A 27-230 [» ]
    2BC4 X-ray 2.27 A/C 27-229 [» ]
    4FQX X-ray 2.60 C 27-225 [» ]
    4GBX X-ray 3.00 C 27-225 [» ]
    ProteinModelPortali P28067.
    SMRi P28067. Positions 38-230.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6184N.
    IntActi P28067. 7 interactions.
    MINTi MINT-1539780.
    STRINGi 9606.ENSP00000408311.

    PTM databases

    PhosphoSitei P28067.

    Polymorphism databases

    DMDMi 133158.

    Proteomic databases

    PaxDbi P28067.
    PRIDEi P28067.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374843 ; ENSP00000363976 ; ENSG00000204257 .
    ENST00000383230 ; ENSP00000372717 ; ENSG00000243215 .
    ENST00000434337 ; ENSP00000407198 ; ENSG00000242361 .
    ENST00000441375 ; ENSP00000410591 ; ENSG00000239463 .
    ENST00000450601 ; ENSP00000392842 ; ENSG00000242685 .
    ENST00000452615 ; ENSP00000395349 ; ENSG00000243189 .
    ENST00000453490 ; ENSP00000404018 ; ENSG00000243719 .

    Organism-specific databases

    GeneCardsi GC06M032924.
    GC06Mi32899.
    GC06Mj32838.
    GC06Ml33070.
    GC06Mm32949.
    GC06Mn32845.
    GC06Mo33006.
    H-InvDB HIX0207683.
    HGNCi HGNC:4934. HLA-DMA.
    HPAi HPA012750.
    MIMi 142855. gene.
    neXtProti NX_P28067.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43075.
    HOGENOMi HOG000126882.
    HOVERGENi HBG001688.
    InParanoidi P28067.
    PhylomeDBi P28067.
    TreeFami TF333797.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.

    Miscellaneous databases

    EvolutionaryTracei P28067.
    PROi P28067.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28067.
    Bgeei P28067.
    CleanExi HS_HLA-DMA.
    Genevestigatori P28067.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.10.320.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    IPR011162. MHC_I/II-like_Ag-recog.
    IPR014745. MHC_II_a/b_N.
    IPR001003. MHC_II_a_N.
    [Graphical view ]
    Pfami PF07654. C1-set. 1 hit.
    PF00993. MHC_II_alpha. 1 hit.
    [Graphical view ]
    SMARTi SM00407. IGc1. 1 hit.
    SM00920. MHC_II_alpha. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54452. SSF54452. 1 hit.
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new human HLA class II-related locus, DM."
      Kelly A.P., Monaco J.J., Cho S., Trowsdale J.
      Nature 353:571-573(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DMA*01:01).
    2. "The DNA sequence and analysis of human chromosome 6."
      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.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Limited polymorphism in HLA-DM does not involve the peptide binding groove."
      Sanderson F., Powis S.H., Kelly A.P., Trowsdale J.
      Immunogenetics 39:56-58(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-218 (ALLELE DMA*01:02).
    4. "Sequence analysis of two novel HLA-DMA alleles."
      Carrington M., Harding A.
      Immunogenetics 40:165-165(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-217 (ALLELES DMA*01:03 AND DMA*01:04).
    5. "Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM."
      Weber D.A., Evavold B.D., Jensen P.E.
      Science 274:618-620(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The structure of HLA-DM, the peptide exchange catalyst that loads antigen onto class II MHC molecules during antigen presentation."
      Mosyak L., Zaller D.M., Wiley D.C.
      Immunity 9:377-383(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-230 IN COMPLEX WITH DMB, FUNCTION, SUBUNIT, DISULFIDE BONDS.
    7. Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 27-229 IN COMPLEX WITH DMB, FUNCTION, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiDMA_HUMAN
    AccessioniPrimary (citable) accession number: P28067
    Secondary accession number(s): Q29639, Q29640
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3