ID   HA2B_MOUSE              Reviewed;         256 AA.
AC   P14434; O78195;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   24-JAN-2024, entry version 182.
DE   RecName: Full=H-2 class II histocompatibility antigen, A-B alpha chain;
DE            Short=IAalpha;
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.
RA   Rowen L., Qin S., Ahearn M.E., Loretz C., Faust J., Lasky S., Mahairas G.,
RA   Hood L.E.;
RT   "Sequence of the mouse major histocompatibility locus class II region.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Rowen L., Qin S., Loretz C., Mix L., Lasky S., Madan A., Hood L.E.;
RT   "Sequence of the mouse major histocompatibility class II region.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-256.
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   [5]
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).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 24-205 IN COMPLEX WITH HUMAN CLIP
RP   PEPTIDE, GLYCOSYLATION AT ASN-145, AND DISULFIDE BONDS.
RX   PubMed=12589760; DOI=10.1016/s0022-2836(02)01437-7;
RA   Zhu Y., Rudensky A.Y., Corper A.L., Teyton L., Wilson I.A.;
RT   "Crystal structure of MHC class II I-Ab in complex with a human CLIP
RT   peptide: prediction of an I-Ab peptide-binding motif.";
RL   J. Mol. Biol. 326:1157-1174(2003).
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; AF027865; AAB81529.1; -; Genomic_DNA.
DR   EMBL; AF050157; AAC05285.1; -; Genomic_DNA.
DR   EMBL; BC019721; AAH19721.1; -; mRNA.
DR   EMBL; BC031711; AAH31711.1; -; mRNA.
DR   EMBL; K01922; AAA39614.1; -; mRNA.
DR   CCDS; CCDS28645.1; -.
DR   RefSeq; NP_034508.2; NM_010378.2.
DR   PDB; 1LNU; X-ray; 2.50 A; A/C/E/G=27-208.
DR   PDB; 1MUJ; X-ray; 2.15 A; A=24-205.
DR   PDB; 3C5Z; X-ray; 2.55 A; C/G=27-208.
DR   PDB; 3C60; X-ray; 3.05 A; C/G=27-208.
DR   PDB; 3C6L; X-ray; 3.40 A; C/G=27-208.
DR   PDB; 3RDT; X-ray; 2.70 A; C=27-208.
DR   PDB; 4P23; X-ray; 2.25 A; C=27-205.
DR   PDB; 4P46; X-ray; 2.85 A; C=27-205.
DR   PDB; 4P5T; X-ray; 3.26 A; C/G=27-208.
DR   PDB; 6MKD; X-ray; 3.20 A; C=27-205.
DR   PDB; 6MKR; X-ray; 3.35 A; C=27-205.
DR   PDB; 6MNG; X-ray; 2.66 A; C=27-205.
DR   PDB; 6MNM; X-ray; 3.10 A; C=27-205.
DR   PDB; 6MNN; X-ray; 2.83 A; C=27-205.
DR   PDB; 6MNO; X-ray; 2.90 A; C=27-205.
DR   PDBsum; 1LNU; -.
DR   PDBsum; 1MUJ; -.
DR   PDBsum; 3C5Z; -.
DR   PDBsum; 3C60; -.
DR   PDBsum; 3C6L; -.
DR   PDBsum; 3RDT; -.
DR   PDBsum; 4P23; -.
DR   PDBsum; 4P46; -.
DR   PDBsum; 4P5T; -.
DR   PDBsum; 6MKD; -.
DR   PDBsum; 6MKR; -.
DR   PDBsum; 6MNG; -.
DR   PDBsum; 6MNM; -.
DR   PDBsum; 6MNN; -.
DR   PDBsum; 6MNO; -.
DR   AlphaFoldDB; P14434; -.
DR   SMR; P14434; -.
DR   BioGRID; 200146; 2.
DR   IntAct; P14434; 1.
DR   MINT; P14434; -.
DR   STRING; 10090.ENSMUSP00000046105; -.
DR   GlyCosmos; P14434; 1 site, No reported glycans.
DR   iPTMnet; P14434; -.
DR   EPD; P14434; -.
DR   MaxQB; P14434; -.
DR   PaxDb; 10090-ENSMUSP00000046105; -.
DR   PeptideAtlas; P14434; -.
DR   ProteomicsDB; 271385; -.
DR   DNASU; 14960; -.
DR   Ensembl; ENSMUST00000040655.14; ENSMUSP00000046105.7; ENSMUSG00000036594.16.
DR   GeneID; 14960; -.
DR   KEGG; mmu:14960; -.
DR   UCSC; uc008ccd.1; mouse.
DR   AGR; MGI:95895; -.
DR   CTD; 14960; -.
DR   MGI; MGI:95895; H2-Aa.
DR   VEuPathDB; HostDB:ENSMUSG00000036594; -.
DR   eggNOG; ENOG502RXYJ; Eukaryota.
DR   GeneTree; ENSGT00940000161821; -.
DR   HOGENOM; CLU_069380_0_0_1; -.
DR   OMA; KERACEY; -.
DR   OrthoDB; 4118190at2759; -.
DR   PhylomeDB; P14434; -.
DR   TreeFam; TF333797; -.
DR   BioGRID-ORCS; 14960; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; H2-Aa; mouse.
DR   EvolutionaryTrace; P14434; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000036594; Expressed in spleen and 176 other cell types or tissues.
DR   ExpressionAtlas; P14434; baseline and differential.
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   GO; GO:0034341; P:response to type II interferon; IDA:BHF-UCL.
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.
DR   Genevisible; P14434; MM.
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                   /evidence="ECO:0000255"
FT   CHAIN           24..256
FT                   /note="H-2 class II histocompatibility antigen, A-B alpha
FT                   chain"
FT                   /id="PRO_0000018975"
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:0000269|PubMed:12589760"
FT   DISULFID        134..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:12589760"
FT   STRAND          30..42
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   STRAND          46..53
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   STRAND          56..62
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   TURN            63..66
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   HELIX           73..76
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   HELIX           83..103
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:1LNU"
FT   STRAND          115..122
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   STRAND          126..128
FT                   /evidence="ECO:0007829|PDB:3C5Z"
FT   STRAND          130..139
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   STRAND          145..154
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:3C6L"
FT   TURN            168..170
FT                   /evidence="ECO:0007829|PDB:3C6L"
FT   STRAND          172..180
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   STRAND          188..193
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   STRAND          197..199
FT                   /evidence="ECO:0007829|PDB:1MUJ"
FT   STRAND          201..205
FT                   /evidence="ECO:0007829|PDB:1MUJ"
SQ   SEQUENCE   256 AA;  28093 MW;  C9DD084F6179B41F CRC64;
     MPRSRALILG VLALTTMLSL CGGEDDIEAD HVGTYGISVY QSPGDIGQYT FEFDGDELFY
     VDLDKKETVW MLPEFGQLAS FDPQGGLQNI AVVKHNLGVL TKRSNSTPAT NEAPQATVFP
     KSPVLLGQPN TLICFVDNIF PPVINITWLR NSKSVADGVY ETSFFVNRDY SFHKLSYLTF
     IPSDDDIYDC KVEHWGLEEP VLKHWEPEIP APMSELTETV VCALGLSVGL VGIVVGTIFI
     IQGLRSGGTS RHPGPL
//