ID HA2J_MOUSE Reviewed; 254 AA.
AC P23150;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 13-SEP-2023, entry version 129.
DE RecName: Full=H-2 class II histocompatibility antigen, I-E alpha chain;
DE Flags: Precursor; Fragment;
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 GLYCOSYLATION AT ASN-103 AND ASN-143.
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, and 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 -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR EMBL; X52643; CAA36865.1; -; mRNA.
DR PIR; I48421; S11649.
DR AlphaFoldDB; P23150; -.
DR SMR; P23150; -.
DR IntAct; P23150; 1.
DR iPTMnet; P23150; -.
DR MaxQB; P23150; -.
DR AGR; MGI:95895; -.
DR MGI; MGI:95895; H2-Aa.
DR Proteomes; UP000000589; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0042613; C:MHC class II protein complex; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR GO; GO:0042605; F:peptide antigen binding; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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:0048002; P:antigen processing and presentation of peptide antigen; IDA:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0050778; P:positive regulation of immune response; IBA:GO_Central.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IDA:MGI.
DR CDD; cd21006; IgC1_MHC_II_alpha_I-A; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR001003; MHC_II_a_N.
DR PANTHER; PTHR19944:SF59; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DQ ALPHA 1 CHAIN; 1.
DR PANTHER; PTHR19944; MHC CLASS II-RELATED; 1.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00993; MHC_II_alpha; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00920; MHC_II_alpha; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF54452; MHC antigen-recognition domain; 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.
FT SIGNAL <1..24
FT CHAIN 25..254
FT /note="H-2 class II histocompatibility antigen, I-E alpha
FT chain"
FT /id="PRO_0000018980"
FT TOPO_DOM 25..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 112..204
FT /note="Ig-like C1-type"
FT REGION 25..109
FT /note="Alpha-1"
FT REGION 110..203
FT /note="Alpha-2"
FT REGION 204..216
FT /note="Connecting peptide"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3980466"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3980466"
FT DISULFID 132..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
SQ SEQUENCE 254 AA; 28013 MW; B8A0D62B87E4CFC8 CRC64;
RSRALILGVL ALTTMLSLCG GEDDIEADHV AFYGISVYQS PGDIGQYTFE FDGDELFYVD
LDKKETVWML PEFGQLTSFD PQGGLQEIAT GKYNLEILIK DSNFTPAANE APQATVFPKS
PVLLGQPNTL ICFVDNIFPP VINITWLRNS KSVTDGVYET SFLVNRDHSF HKLSYLTFIP
SDDDIYDCKV EHWGLEEPVL KHWEPEIPAP MSELTETVVC ALGLSVGLVG IVVGTIFIIQ
GLRSGGTSRH PGPL
//
