HB2I_MOUSE
ID HB2I_MOUSE Reviewed; 264 AA.
AC P18468;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=H-2 class II histocompatibility antigen, I-A 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].
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 [2]
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 [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 32-215, AND DISULFIDE BONDS.
RX PubMed=14690592; DOI=10.1016/s1097-2765(03)00474-x;
RA Krogsgaard M., Prado N., Adams E.J., He X.L., Chow D.C., Wilson D.B.,
RA Garcia K.C., Davis M.M.;
RT "Evidence that structural rearrangements and/or flexibility during TCR
RT binding can contribute to T cell activation.";
RL Mol. Cell 12:1367-1378(2003).
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; X52641; CAA36863.1; -; mRNA.
DR PIR; I48224; S11650.
DR PDB; 1R5V; X-ray; 2.50 A; B/D=32-215.
DR PDBsum; 1R5V; -.
DR AlphaFoldDB; P18468; -.
DR SMR; P18468; -.
DR iPTMnet; P18468; -.
DR PhosphoSitePlus; P18468; -.
DR MaxQB; P18468; -.
DR PRIDE; P18468; -.
DR ProteomicsDB; 270945; -.
DR MGI; MGI:95901; H2-Eb1.
DR ChiTaRS; H2-Eb1; mouse.
DR EvolutionaryTrace; P18468; -.
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; ISS:BHF-UCL.
DR GO; GO:0005765; C:lysosomal membrane; ISS:BHF-UCL.
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:BHF-UCL.
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 GO; GO:0034341; P:response to interferon-gamma; IDA:BHF-UCL.
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..31
FT CHAIN 32..264
FT /note="H-2 class II histocompatibility antigen, I-A beta
FT chain"
FT /id="PRO_0000019003"
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:0000255"
FT DISULFID 42..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:14690592"
FT DISULFID 144..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:14690592"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:1R5V"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1R5V"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1R5V"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1R5V"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:1R5V"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1R5V"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:1R5V"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 141..152
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1R5V"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:1R5V"
SQ SEQUENCE 264 AA; 30232 MW; 04529F5E2E527D7A CRC64;
MVWLPRVPCV AAVILLLTVL SPPVALVRDS RPWFLEYCKS ECHFYNGTQR VRFLKRYFYN
LEENLRFDSD VGEFRAVTEL GRPDAENWNS QPEILDEKRA AVDTYCRHNY EIFDNFLVPR
RVEPTVTVYP TKTQPLEHHN LLVCSVSDFY PGNIEVRWFR NGKEEKTGIV STGLVRNGDW
TFQTLVMLET VPQSGEVYTC QVEHPSLTDP VTVEWKAQST SAQNKMLSGV GGFVLGLLFL
RAGLFIYFRN QKGQSGLQPT GLLS
