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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
 
 
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