HB2J_MOUSE
ID HB2J_MOUSE Reviewed; 264 AA.
AC P18469;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=H-2 class II histocompatibility antigen, I-E beta chain;
DE Flags: Precursor;
GN Name=H2-Eb1;
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].
RX PubMed=3018929; DOI=10.1126/science.3018929;
RA Kobori J.A., Strauss E., Minard K., Hood L.;
RT "Molecular analysis of the hotspot of recombination in the murine major
RT histocompatibility complex.";
RL Science 234:173-179(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=1855817; DOI=10.1007/bf00212313;
RA Acha-Orbea H., Scarpellino L.;
RT "Nonobese diabetic and nonobese nondiabetic mice have unique MHC class II
RT haplotypes.";
RL Immunogenetics 34:57-59(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1918991;
RA Padgett K.A., Shreffler D.C., Saha B.K.;
RT "Molecular mapping of murine I region recombinants. III. Crossing over at
RT two discrete sites within the beta 1-beta 2 intron of the E beta gene.";
RL J. Immunol. 147:2764-2770(1991).
RN [4]
RP GLYCOSYLATION AT ASN-46.
RX PubMed=3980466; DOI=10.1016/s0021-9258(18)89229-8;
RA Swiedler S.J., Freed J.H., Tarentino A.L., Plummer T.H. Jr., Hart G.W.;
RT "Oligosaccharide microheterogeneity of the murine major histocompatibility
RT antigens. Reproducible site-specific patterns of sialylation and branching
RT in asparagine-linked oligosaccharides.";
RL J. Biol. Chem. 260:4046-4054(1985).
RN [5]
RP UBIQUITINATION.
RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001;
RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A.,
RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.;
RT "Dendritic cells regulate exposure of MHC class II at their plasma membrane
RT by oligoubiquitination.";
RL Immunity 25:885-894(2006).
RN [6]
RP UBIQUITINATION.
RX PubMed=17051151; DOI=10.1038/nature05261;
RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., Mellman I.;
RT "Surface expression of MHC class II in dendritic cells is controlled by
RT regulated ubiquitination.";
RL Nature 444:115-118(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down-
CC regulation of MHC class II. {ECO:0000269|PubMed:17051151,
CC ECO:0000269|PubMed:17174123}.
CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR EMBL; X52642; CAA36864.1; -; mRNA.
DR PIR; I48422; I48422.
DR AlphaFoldDB; P18469; -.
DR SMR; P18469; -.
DR MINT; P18469; -.
DR iPTMnet; P18469; -.
DR PhosphoSitePlus; P18469; -.
DR MaxQB; P18469; -.
DR PRIDE; P18469; -.
DR ProteomicsDB; 270892; -.
DR MGI; MGI:95901; H2-Eb1.
DR ChiTaRS; H2-Eb1; mouse.
DR Proteomes; UP000000589; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0001772; C:immunological synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0042613; C:MHC class II protein complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042609; F:CD4 receptor binding; ISO:MGI.
DR GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR GO; GO:0032395; F:MHC class II receptor activity; ISO:MGI.
DR GO; GO:0042605; F:peptide antigen binding; ISO:MGI.
DR GO; GO:0030247; F:polysaccharide binding; ISO:MGI.
DR GO; GO:0042608; F:T cell receptor binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Adaptive immunity; Disulfide bond; Glycoprotein; Immunity; Membrane;
KW MHC II; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..31
FT CHAIN 32..264
FT /note="H-2 class II histocompatibility antigen, I-E beta
FT chain"
FT /id="PRO_0000019004"
FT TOPO_DOM 32..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 124..214
FT /note="Ig-like C1-type"
FT REGION 32..121
FT /note="Beta-1"
FT REGION 122..215
FT /note="Beta-2"
FT REGION 216..225
FT /note="Connecting peptide"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3980466"
FT DISULFID 42..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 264 AA; 30141 MW; 93178C1AE63987FF CRC64;
MVWLPRVPCV AAVILLLTVL SPPVALVRNS RPRFLEYSTS ECHFYNGTQR VRFLERYIYN
REEYVRFDSD VGEYRAVTEL GRPDAEYWNS QPEILEDARA TVDTYCRHNY EIFDNFLVPR
RVEPTVTVYP TKTQPLEHHN LLVCSVSDFY PGNIEVRWFR NGKEEKTGIV STGLVRNGDW
TFQTLVMLET VPQSGEVYTC QVEHPSLTDP VTVEWKAQST SAQNKMLSGV GGFVLGLLFL
GAGLFIYFRN QKGQSGLQPT GLLS
