DMA_MOUSE
ID DMA_MOUSE Reviewed; 261 AA.
AC P28078;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Class II histocompatibility antigen, M alpha chain;
DE Flags: Precursor;
GN Name=H2-DMa; Synonyms=H2-Ma, Ma;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=1922366; DOI=10.1038/353573a0;
RA Cho S., Attaya M., Monaco J.J.;
RT "New class II-like genes in the murine MHC.";
RL Nature 353:573-576(1991).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 30-220, SUBUNIT, GLYCOSYLATION AT
RP ASN-41, AND DISULFIDE BONDS.
RX PubMed=9768758; DOI=10.1016/s1074-7613(00)80621-4;
RA Fremont D.H., Crawford F., Marrack P., Hendrickson W.A., Kappler J.;
RT "Crystal structure of mouse H2-M.";
RL Immunity 9:385-393(1998).
CC -!- FUNCTION: Plays a critical role in catalyzing the release of class II-
CC associated invariant chain peptide (CLIP) from newly synthesized MHC
CC class II molecules and freeing the peptide binding site for acquisition
CC of antigenic peptides. {ECO:0000250|UniProtKB:P28067}.
CC -!- SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain (DMB)
CC (PubMed:9768758). Interacts with MHCII; this interaction mediates rapid
CC selection of high-affinity peptides (By similarity).
CC {ECO:0000250|UniProtKB:P28067, ECO:0000269|PubMed:9768758}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Single-pass type I
CC membrane protein. Lysosome membrane; Single-pass type I membrane
CC protein. Note=Localizes to late endocytic compartment. Associates with
CC lysosome membranes.
CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR EMBL; X62742; CAA44604.1; -; mRNA.
DR CCDS; CCDS37579.1; -.
DR PIR; S17888; S17888.
DR PDB; 1K8I; X-ray; 3.10 A; A=30-220.
DR PDBsum; 1K8I; -.
DR AlphaFoldDB; P28078; -.
DR SMR; P28078; -.
DR IntAct; P28078; 1.
DR STRING; 10090.ENSMUSP00000037088; -.
DR GlyGen; P28078; 2 sites.
DR iPTMnet; P28078; -.
DR PhosphoSitePlus; P28078; -.
DR MaxQB; P28078; -.
DR PaxDb; P28078; -.
DR PRIDE; P28078; -.
DR ProteomicsDB; 277339; -.
DR MGI; MGI:95921; H2-DMa.
DR eggNOG; ENOG502S6RX; Eukaryota.
DR InParanoid; P28078; -.
DR PhylomeDB; P28078; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR ChiTaRS; H2-DMa; mouse.
DR EvolutionaryTrace; P28078; -.
DR PRO; PR:P28078; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P28078; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0042613; C:MHC class II protein complex; ISO:MGI.
DR GO; GO:0005771; C:multivesicular body; IDA:MGI.
DR GO; GO:0023026; F:MHC class II protein complex binding; ISS:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; ISS:UniProtKB.
DR GO; GO:0002636; P:positive regulation of germinal center formation; IMP:BHF-UCL.
DR GO; GO:0002922; P:positive regulation of humoral immune response; IMP:BHF-UCL.
DR GO; GO:0050778; P:positive regulation of immune response; IMP:MGI.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:MGI.
DR GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IDA:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:MGI.
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; IPR001003; MHC_II_a_N.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00993; MHC_II_alpha; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00920; MHC_II_alpha; 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; Disulfide bond; Endosome; Glycoprotein;
KW Immunity; Lysosome; Membrane; MHC II; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..261
FT /note="Class II histocompatibility antigen, M alpha chain"
FT /id="PRO_0000018959"
FT TOPO_DOM 27..231
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 114..215
FT /note="Ig-like C1-type"
FT REGION 27..124
FT /note="Alpha-1"
FT REGION 125..217
FT /note="Alpha-2"
FT REGION 218..231
FT /note="Connecting peptide"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9768758"
FT DISULFID 50..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:9768758"
FT DISULFID 147..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:9768758"
FT STRAND 41..63
FT /evidence="ECO:0007829|PDB:1K8I"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:1K8I"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:1K8I"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1K8I"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:1K8I"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1K8I"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:1K8I"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:1K8I"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:1K8I"
FT STRAND 143..155
FT /evidence="ECO:0007829|PDB:1K8I"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1K8I"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1K8I"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:1K8I"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:1K8I"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:1K8I"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:1K8I"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1K8I"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1K8I"
SQ SEQUENCE 261 AA; 28950 MW; C8403C76CB54A55C CRC64;
MEHEQKSGAV LLRLLRLLWL LPHSWAVLEA STPVLWDDPQ NHTFRHTLFC QDGIPNIGLS
ETYDEDELFS FDFSQNTRVP RLPDFAEWAQ GQGDASAIAF GKSFCEMLMR EVSPKLEGQI
PVSRGLSVAE VFTLKPLEFG KPNTLVCFIS NLFPPTLTVN WQLHSAPVEG ASPTSISAVD
GLTFQAFSYL NFTPEPFDLY SCTVTHEIDR YTAIAYWVPQ NALPSDLLEN ALCGVAFALG
VLGTIIGIVF FLCSQRPCSG D
