HA2D_MOUSE
ID HA2D_MOUSE Reviewed; 256 AA.
AC P04228;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=H-2 class II histocompatibility antigen, A-D alpha chain;
DE Flags: Precursor;
GN Name=H2-Aa;
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=6309407; DOI=10.1016/0092-8674(83)90147-2;
RA Benoist C.O., Mathis D.J., Kanter M.R., Williams V.E., McDevitt H.O.;
RT "Regions of allelic hypervariability in the murine A alpha immune response
RT gene.";
RL Cell 34:169-177(1983).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Pancreas, 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; K01923; AAA39615.1; -; mRNA.
DR PIR; A02219; HLMSA2.
DR PDB; 1ES0; X-ray; 2.60 A; A=24-205.
DR PDB; 1F3J; X-ray; 3.10 A; A/D=27-208.
DR PDB; 1IAO; X-ray; 2.60 A; A=24-209.
DR PDB; 2IAD; X-ray; 2.40 A; A=24-209.
DR PDB; 3CUP; X-ray; 3.09 A; A=24-205.
DR PDB; 3MBE; X-ray; 2.89 A; A/E=24-205.
DR PDB; 5DMK; X-ray; 2.45 A; A/C/E/G=26-198.
DR PDB; 6BLQ; X-ray; 1.80 A; A=24-208.
DR PDB; 6BLR; X-ray; 1.96 A; A=26-208.
DR PDB; 6BLX; X-ray; 2.32 A; A=26-208.
DR PDB; 6DFS; X-ray; 3.10 A; C=26-208.
DR PDB; 6DFW; X-ray; 3.20 A; A/C=26-208.
DR PDBsum; 1ES0; -.
DR PDBsum; 1F3J; -.
DR PDBsum; 1IAO; -.
DR PDBsum; 2IAD; -.
DR PDBsum; 3CUP; -.
DR PDBsum; 3MBE; -.
DR PDBsum; 5DMK; -.
DR PDBsum; 6BLQ; -.
DR PDBsum; 6BLR; -.
DR PDBsum; 6BLX; -.
DR PDBsum; 6DFS; -.
DR PDBsum; 6DFW; -.
DR AlphaFoldDB; P04228; -.
DR SMR; P04228; -.
DR IntAct; P04228; 2.
DR MINT; P04228; -.
DR MaxQB; P04228; -.
DR PRIDE; P04228; -.
DR ProteomicsDB; 270880; -.
DR ABCD; P04228; 2 sequenced antibodies.
DR MGI; MGI:95895; H2-Aa.
DR ChiTaRS; H2-Aa; mouse.
DR EvolutionaryTrace; P04228; -.
DR Proteomes; UP000000589; Unplaced.
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; 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: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 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..23
FT CHAIN 24..256
FT /note="H-2 class II histocompatibility antigen, A-D alpha
FT chain"
FT /id="PRO_0000018976"
FT TOPO_DOM 24..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 114..206
FT /note="Ig-like C1-type"
FT REGION 24..111
FT /note="Alpha-1"
FT REGION 112..205
FT /note="Alpha-2"
FT REGION 206..218
FT /note="Connecting peptide"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 134..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 30..42
FT /evidence="ECO:0007829|PDB:6BLQ"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6BLQ"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:6BLQ"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:6BLQ"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:6BLQ"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6BLQ"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:6BLQ"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6BLQ"
FT HELIX 84..103
FT /evidence="ECO:0007829|PDB:6BLQ"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3MBE"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:6BLQ"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:6BLQ"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:6BLQ"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6BLQ"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6BLQ"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6DFW"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:6BLQ"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:1IAO"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:6BLQ"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:6BLQ"
SQ SEQUENCE 256 AA; 28243 MW; 085B3FE643B58BBB CRC64;
MPCSRALILG VLALNTMLSL CGGEDDIEAD HVGFYGTTVY QSPGDIGQYT HEFDGDELFY
VDLDKKKTVW RLPEFGQLIL FEPQGGLQNI AAEKHNLGIL TKRSNFTPAT NEAPQATVFP
KSPVLLGQPN TLICFVDNIF PPVINITWLR NSKSVTDGVY ETSFLVNRDH SFHKLSYLTF
IPSDDDIYDC KVEHWGLEEP VLKHWEPEIP APMSELTETV VCALGLSVGL VGIVVGTIFI
IQGLRSGGTS RHPGPL
