HB23_MOUSE
ID HB23_MOUSE Reviewed; 232 AA.
AC P04231; O78225;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=H-2 class II histocompatibility antigen, E-S beta chain;
DE Flags: Fragment;
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=2986145; DOI=10.1073/pnas.82.9.2910;
RA Mengle-Gaw L., McDevitt H.O.;
RT "Predicted protein sequence of the murine I-E-beta S-polypeptide chain from
RT cDNA and genomic clones.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2910-2914(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-89.
RX PubMed=3692165; DOI=10.1017/s0016672300023545;
RA Golubic M., Budimir O., Schoepfer R., Kasahara M., Mayer W.E., Figueroa F.,
RA Klein J.;
RT "Nucleotide sequence analysis of class II genes borne by mouse t
RT chromosomes.";
RL Genet. Res. 50:137-146(1987).
RN [3]
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 [4]
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).
RN [5]
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).
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; M11355; AAA39644.1; -; mRNA.
DR EMBL; L38589; AAA57293.1; -; Genomic_DNA.
DR PIR; A02227; HLMSE2.
DR AlphaFoldDB; P04231; -.
DR SMR; P04231; -.
DR MaxQB; P04231; -.
DR PRIDE; P04231; -.
DR ProteomicsDB; 270944; -.
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; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN <1..232
FT /note="H-2 class II histocompatibility antigen, E-S beta
FT chain"
FT /id="PRO_0000080754"
FT TOPO_DOM <1..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 92..182
FT /note="Ig-like C1-type"
FT REGION <1..90
FT /note="Beta-1"
FT REGION 91..193
FT /note="Beta-2"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 10..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 112..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
SQ SEQUENCE 232 AA; 26647 MW; 8960CFC0BD6A8CB4 CRC64;
WFLEYSTSEC HFYNGTQRVR LLERYFYNLE ENLRFDSDVG EFRAVTELGR PDAENWNSQP
EFLEQRRAAV DTYCRHNYEI LDKFLVPRRV EPTVTVYPTK TQPLEHHNLL VCSVSDFYPG
NIEVRWFRNG KEEKTGIVST GLVRNGDWTF QTLVMLETVP QSGEVYTCQV EHPSLTDPVT
VEWKAQSTSA QNKMLSGVGG FVLGLLFLGA GLFIYFRNQK GQSGLQPTGL LS
