ID   DMB_MOUSE               Reviewed;         261 AA.
AC   P35737;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 142.
DE   RecName: Full=Class II histocompatibility antigen, M beta 1 chain;
DE   AltName: Full=H2-M beta 1 chain;
DE   Flags: Precursor;
GN   Name=H2-DMb1; Synonyms=H-2Mb1, Mb;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=8575819; DOI=10.1007/bf00587301;
RA   Peleraux A., Karlsson L., Chambers J., Peterson P.A.;
RT   "Genomic organization of a mouse MHC class II region including the H2-M and
RT   Lmp2 loci.";
RL   Immunogenetics 43:204-214(1996).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=7584146; DOI=10.1016/1074-7613(95)90127-2;
RA   Lindstedt R., Liljedahl M., Peleraux A., Peterson P.A., Karlsson L.;
RT   "The MHC class II molecule H2-M is targeted to an endosomal compartment by
RT   a tyrosine-based targeting motif.";
RL   Immunity 3:561-572(1995).
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:P28068}.
CC   -!- SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain (DMB).
CC       Interacts with MHCII; this interaction mediates rapid selection of
CC       high-affinity peptides. {ECO:0000250|UniProtKB:P28068}.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000269|PubMed:7584146}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:7584146}. Lysosome membrane
CC       {ECO:0000269|PubMed:7584146}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:7584146}. Note=Localizes to late endocytic
CC       compartment. Associates with lysosome membranes.
CC   -!- DOMAIN: The YXXZ (Tyr-Xaa-Xaa-Zaa, where Zaa is a hydrophobic residue)
CC       motif mediates the targeting to the lysosomal compartments.
CC   -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR   EMBL; X62743; CAA44605.1; -; mRNA.
DR   EMBL; U35323; AAA98931.1; -; Genomic_DNA.
DR   CCDS; CCDS37581.1; -.
DR   PIR; S17889; S17889.
DR   AlphaFoldDB; P35737; -.
DR   SMR; P35737; -.
DR   STRING; 10090.ENSMUSP00000109870; -.
DR   GlyGen; P35737; 1 site.
DR   iPTMnet; P35737; -.
DR   PhosphoSitePlus; P35737; -.
DR   PaxDb; P35737; -.
DR   PRIDE; P35737; -.
DR   ProteomicsDB; 279786; -.
DR   MGI; MGI:95922; H2-DMb1.
DR   eggNOG; ENOG502SAA4; Eukaryota.
DR   InParanoid; P35737; -.
DR   PhylomeDB; P35737; -.
DR   ChiTaRS; H2-DMb1; mouse.
DR   PRO; PR:P35737; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P35737; protein.
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:0031902; C:late endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0042613; C:MHC class II protein complex; ISO:MGI.
DR   GO; GO:0023026; F:MHC class II protein complex binding; ISS:UniProtKB.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
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:0002399; P:MHC class II protein complex assembly; ISO:MGI.
DR   GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; ISS:UniProtKB.
DR   GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR   GO; GO:2001190; P:positive regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; ISO:MGI.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISO: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; IPR000353; MHC_II_b_N.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00969; MHC_II_beta; 1.
DR   SMART; SM00407; IGc1; 1.
DR   SMART; SM00921; MHC_II_beta; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF54452; SSF54452; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   2: Evidence at transcript level;
KW   Adaptive immunity; Disulfide bond; Endosome; Glycoprotein; Immunity;
KW   Lysosome; Membrane; MHC II; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..261
FT                   /note="Class II histocompatibility antigen, M beta 1 chain"
FT                   /id="PRO_0000018961"
FT   TOPO_DOM        19..218
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        240..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          114..204
FT                   /note="Ig-like C1-type"
FT   REGION          19..112
FT                   /note="Beta-1"
FT   REGION          113..207
FT                   /note="Beta-2"
FT   REGION          208..218
FT                   /note="Connecting peptide"
FT                   /evidence="ECO:0000255"
FT   MOTIF           248..251
FT                   /note="YXXZ motif"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..97
FT                   /evidence="ECO:0000250|UniProtKB:P28068,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        43..53
FT                   /evidence="ECO:0000250|UniProtKB:P28068"
FT   DISULFID        135..192
FT                   /evidence="ECO:0000250|UniProtKB:P28068,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   261 AA;  28899 MW;  4986A222912286D9 CRC64;
     MAALWLLLLV LSLHCMGAGG FVAHVESTCV LDDAGTPQDF TYCVSFNKDL LACWDPIVGK
     IVPCEFGVLY PLAENFSRIL NKEESLLQRL QNGLPDCASH TQPFWNALTH RTRPPSVRVA
     QTTPFNTREP VMLACYVWGF YPADVTITWM KNGQLVPSHS NKEKTAQPNG DWTYQTVSYL
     ALTPSYGDVY TCVVQHSGTS EPIRGDWTPG LSPIQTVKVS VSAATLGLGF IIFCVGFFRW
     RKSHSSSYTP LSGSTYPEGR H