HA2B_MOUSE
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 03-AUG-2022, entry version 175.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 iPTMnet; P14434; -.
DR EPD; P14434; -.
DR MaxQB; P14434; -.
DR PaxDb; P14434; -.
DR PeptideAtlas; P14434; -.
DR PRIDE; P14434; -.
DR ProteomicsDB; 271385; -.
DR DNASU; 14960; -.
DR Ensembl; ENSMUST00000040655; ENSMUSP00000046105; ENSMUSG00000036594.
DR GeneID; 14960; -.
DR KEGG; mmu:14960; -.
DR UCSC; uc008ccd.1; mouse.
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; VADLQIC; -.
DR OrthoDB; 1132781at2759; -.
DR PhylomeDB; P14434; -.
DR TreeFam; TF333797; -.
DR BioGRID-ORCS; 14960; 2 hits in 74 CRISPR screens.
DR ChiTaRS; H2-Aa; mouse.
DR EvolutionaryTrace; P14434; -.
DR Proteomes; UP000000589; Chromosome 17.
DR Bgee; ENSMUSG00000036594; Expressed in spleen and 173 other tissues.
DR ExpressionAtlas; P14434; baseline and differential.
DR Genevisible; P14434; MM.
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 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; 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 /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
