HA21_MOUSE
ID HA21_MOUSE Reviewed; 255 AA.
AC P01904; Q31157;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=H-2 class II histocompatibility antigen, E-D alpha chain;
DE Short=H2-IE-alpha;
DE Flags: Precursor;
GN Name=H2-Ea;
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=BALB/cJ;
RX PubMed=6308570; DOI=10.1093/nar/11.15.5055;
RA Hyldig-Nielsen J.J., Schenning L., Hammerling U., Widmark E., Heldin E.,
RA Lind P., Servenius B., Lund T., Flavell R., Lee J.S., Trowsdale J.,
RA Schreier P.H., Zablitzky F., Larhammar D., Peterson P.A., Rask L.;
RT "The complete nucleotide sequence of the I-E alpha d immune response
RT gene.";
RL Nucleic Acids Res. 11:5055-5071(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6415003; DOI=10.1016/0198-8859(83)90087-3;
RA Larhammar D., Andersson G., Andersson M., Bill P., Boehme J., Claesson L.,
RA Denaro M., Emmoth E., Gustafsson K., Hammarling U., Heldin E.,
RA Hyldig-Nielsen J.-J., Lind P., Schenning L., Servenius B., Widmark E.,
RA Rask L., Peterson P.A.;
RT "Molecular analysis of human class II transplantation antigens and their
RT genes.";
RL Hum. Immunol. 8:95-103(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-255.
RC STRAIN=BALB/cJ;
RX PubMed=6815800; DOI=10.1126/science.6815800;
RA McNicholas J., Steinmetz M., Hunkapiller T., Jones P., Hood L.E.;
RT "DNA sequence of the gene encoding the E alpha Ia polypeptide of the BALB/c
RT mouse.";
RL Science 218:1229-1232(1982).
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; K00971; AAA98624.1; -; Genomic_DNA.
DR EMBL; J00396; AAA39582.1; -; Genomic_DNA.
DR PIR; B91743; HLMSED.
DR PDB; 1IEA; X-ray; 2.30 A; A/C=26-217.
DR PDB; 1IEB; X-ray; 2.70 A; A/C=26-217.
DR PDB; 1KT2; X-ray; 2.80 A; A/C=26-207.
DR PDB; 1KTD; X-ray; 2.40 A; A/C=26-207.
DR PDBsum; 1IEA; -.
DR PDBsum; 1IEB; -.
DR PDBsum; 1KT2; -.
DR PDBsum; 1KTD; -.
DR AlphaFoldDB; P01904; -.
DR SMR; P01904; -.
DR GlyGen; P01904; 2 sites.
DR PRIDE; P01904; -.
DR MGI; MGI:95900; H2-Ea.
DR InParanoid; P01904; -.
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-Ea-ps; mouse.
DR EvolutionaryTrace; P01904; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01904; protein.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0042613; C:MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IDA: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; IDA:MGI.
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; IPR001003; MHC_II_a_N.
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; 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.
FT SIGNAL 1..25
FT CHAIN 26..255
FT /note="H-2 class II histocompatibility antigen, E-D alpha
FT chain"
FT /id="PRO_0000018978"
FT TOPO_DOM 26..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 112..204
FT /note="Ig-like C1-type"
FT REGION 26..109
FT /note="Alpha-1"
FT REGION 110..203
FT /note="Alpha-2"
FT REGION 204..216
FT /note="Connecting peptide"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 132..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 155
FT /note="E -> T (in Ref. 3; AAA39582)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="T -> A (in Ref. 3; AAA39582)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="M -> A (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 30..40
FT /evidence="ECO:0007829|PDB:1IEA"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1IEA"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:1IEA"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1IEA"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:1IEA"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1IEA"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:1IEA"
FT HELIX 81..101
FT /evidence="ECO:0007829|PDB:1IEA"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1IEA"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1IEA"
FT STRAND 128..140
FT /evidence="ECO:0007829|PDB:1IEA"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1IEA"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1KT2"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1IEA"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1IEA"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:1IEA"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:1IEA"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1IEA"
SQ SEQUENCE 255 AA; 29117 MW; 0852EA3AA4EE2674 CRC64;
MATIGALVLR FFFIAVLMSS QKSWAIKEEH TIIQAEFYLL PDKRGEFMFD FDGDEIFHVD
IEKSETIWRL EEFAKFASFE AQGALANIAV DKANLDVMKE RSNNTPDANV APEVTVLSRS
PVNLGEPNIL ICFIDKFSPP VVNVTWLRNG RPVTEGVSET VFLPRDDHLF RKFHYLTFLP
STDDFYDCEV DHWGLEEPLR KTWEFEEKTL LPETKENVMC ALGLFVGLVG IVVGIILIMK
GIKKRNVVER RQGAL
