HB21_MOUSE
ID HB21_MOUSE Reviewed; 264 AA.
AC P04230; O78226;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=H-2 class II histocompatibility antigen, E-B 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 [GENOMIC DNA].
RC STRAIN=C57BL/10;
RX PubMed=6086309; DOI=10.1002/j.1460-2075.1984.tb01956.x;
RA Widera G., Flavell R.A.;
RT "The nucleotide sequence of the murine I-E beta b immune response gene:
RT evidence for gene conversion events in class II genes of the major
RT histocompatibility complex.";
RL EMBO J. 3:1221-1225(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3150763; DOI=10.1111/j.1744-313x.1988.tb00423.x;
RA King L.B., Sharma S., Corley R.B.;
RT "Complete coding region sequence of E beta k cDNA clones: lack of
RT polymorphism in the NH2-terminus between E beta k and E beta b molecules.";
RL J. Immunogenet. 15:209-214(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 113-121.
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 [4]
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 [5]
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; X00623; CAA25257.1; -; Genomic_DNA.
DR EMBL; X00701; CAB51615.2; ALT_SEQ; Genomic_DNA.
DR EMBL; X00702; CAB51615.2; JOINED; Genomic_DNA.
DR EMBL; M36940; AAA39590.1; -; mRNA.
DR EMBL; L38590; AAA57294.1; -; Genomic_DNA.
DR CCDS; CCDS37584.1; -.
DR PIR; A02226; HLMSE1.
DR PDB; 1I3R; X-ray; 2.40 A; B/D/F/H=30-225.
DR PDB; 1KT2; X-ray; 2.80 A; B/D=30-215.
DR PDB; 1KTD; X-ray; 2.40 A; B/D=30-215.
DR PDB; 3QIB; X-ray; 2.70 A; B=30-225.
DR PDB; 3QIU; X-ray; 2.70 A; B=30-225.
DR PDB; 3QIW; X-ray; 3.30 A; B=30-225.
DR PDBsum; 1I3R; -.
DR PDBsum; 1KT2; -.
DR PDBsum; 1KTD; -.
DR PDBsum; 3QIB; -.
DR PDBsum; 3QIU; -.
DR PDBsum; 3QIW; -.
DR AlphaFoldDB; P04230; -.
DR SMR; P04230; -.
DR STRING; 10090.ENSMUSP00000074143; -.
DR GlyGen; P04230; 1 site.
DR PhosphoSitePlus; P04230; -.
DR MaxQB; P04230; -.
DR PaxDb; P04230; -.
DR PRIDE; P04230; -.
DR ProteomicsDB; 269676; -.
DR MGI; MGI:95901; H2-Eb1.
DR eggNOG; ENOG502RYBQ; Eukaryota.
DR InParanoid; P04230; -.
DR PhylomeDB; P04230; -.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse.
DR Reactome; R-MMU-202433; Generation of second messenger molecules.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-389948; PD-1 signaling.
DR ChiTaRS; H2-Eb1; mouse.
DR EvolutionaryTrace; P04230; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P04230; protein.
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 3D-structure; Adaptive immunity; Disulfide bond; Glycoprotein; Immunity;
KW Membrane; MHC II; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..26
FT CHAIN 27..264
FT /note="H-2 class II histocompatibility antigen, E-B beta
FT chain"
FT /id="PRO_0000019000"
FT TOPO_DOM 27..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 124..214
FT /note="Ig-like C1-type"
FT REGION 27..121
FT /note="Beta-1"
FT REGION 122..225
FT /note="Beta-2"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:1I3R"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1I3R"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1I3R"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1I3R"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:1I3R"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1I3R"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:1I3R"
FT TURN 114..119
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 141..152
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:1I3R"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1I3R"
SQ SEQUENCE 264 AA; 30166 MW; BF1264C41AF8D1C0 CRC64;
MVWLPRVPCV AAVILLLTVL SPPMALVRDS RPWFLEYCKS ECHFYNGTQR VRLLERYFYN
LEENLRFDSD VGEFHAVTEL GRPDAENWNS QPEFLEQKRA EVDTVCRHNY EISDKFLVRR
RVEPTVTVYP TKTQPLEHHN LLVCSVSDFY PGNIEVRWFR NGKEEKTGIV STGLVRNGDW
TFQTLVMLET VPQSGEVYTC QVEHPSLTDP VTVEWKAQST SAQNKMLSGV GGFVLGLLFL
GAGLFIYFRN QKGQSGLQPT GLLS
