HB2A_MOUSE
ID HB2A_MOUSE Reviewed; 265 AA.
AC P14483;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=H-2 class II histocompatibility antigen, A beta chain;
DE Flags: Precursor;
GN Name=H2-Ab1; Synonyms=H2-iabeta;
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].
RX PubMed=6411350; DOI=10.1016/0092-8674(83)90148-4;
RA Larhammar D., Hammerling U., Denaro M., Lund T., Flavell R.A., Rask L.,
RA Peterson P.A.;
RT "Structure of the murine immune response I-A beta locus: sequence of the I-
RT A beta gene and an adjacent beta-chain second domain exon.";
RL Cell 34:179-188(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rowen L., Qin S., Ahearn M.E., Loretz C., Faust J., Lasky S., Mahairas G.,
RA Hood L.E.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP UBIQUITINATION.
RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001;
RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A.,
RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.;
RT "Dendritic cells regulate exposure of MHC class II at their plasma membrane
RT by oligoubiquitination.";
RL Immunity 25:885-894(2006).
RN [4]
RP UBIQUITINATION.
RX PubMed=17051151; DOI=10.1038/nature05261;
RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., Mellman I.;
RT "Surface expression of MHC class II in dendritic cells is controlled by
RT regulated ubiquitination.";
RL Nature 444:115-118(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down-
CC regulation of MHC class II. {ECO:0000269|PubMed:17051151,
CC ECO:0000269|PubMed:17174123}.
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; V01527; CAA24768.1; -; Genomic_DNA.
DR EMBL; AF027865; AAB81531.1; -; Genomic_DNA.
DR CCDS; CCDS37583.1; -.
DR PIR; I48656; I48656.
DR RefSeq; NP_996988.2; NM_207105.3.
DR PDB; 1LNU; X-ray; 2.50 A; B/D/F/H=27-216.
DR PDB; 1MUJ; X-ray; 2.15 A; B=28-216.
DR PDB; 3C5Z; X-ray; 2.55 A; D/H=30-216.
DR PDB; 3C60; X-ray; 3.05 A; D/H=30-216.
DR PDB; 3C6L; X-ray; 3.40 A; D/H=30-216.
DR PDB; 3RDT; X-ray; 2.70 A; D=30-218.
DR PDB; 4P23; X-ray; 2.25 A; D=31-219.
DR PDB; 4P46; X-ray; 2.85 A; D=31-219.
DR PDB; 4P5T; X-ray; 3.26 A; D/H=27-218.
DR PDB; 6MKD; X-ray; 3.20 A; D=21-218.
DR PDB; 6MKR; X-ray; 3.35 A; D=21-218.
DR PDB; 6MNG; X-ray; 2.66 A; D=21-218.
DR PDB; 6MNM; X-ray; 3.10 A; D=21-218.
DR PDB; 6MNN; X-ray; 2.83 A; D=21-218.
DR PDB; 6MNO; X-ray; 2.90 A; D=31-218.
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; P14483; -.
DR SMR; P14483; -.
DR BioGRID; 200147; 1.
DR IntAct; P14483; 1.
DR MINT; P14483; -.
DR STRING; 10090.ENSMUSP00000041008; -.
DR PhosphoSitePlus; P14483; -.
DR EPD; P14483; -.
DR jPOST; P14483; -.
DR PaxDb; P14483; -.
DR PRIDE; P14483; -.
DR ProteomicsDB; 269678; -.
DR ABCD; P14483; 5 sequenced antibodies.
DR Antibodypedia; 53255; 85 antibodies from 19 providers.
DR DNASU; 14961; -.
DR Ensembl; ENSMUST00000040828; ENSMUSP00000041008; ENSMUSG00000073421.
DR GeneID; 14961; -.
DR KEGG; mmu:14961; -.
DR UCSC; uc008ccb.2; mouse.
DR CTD; 14961; -.
DR MGI; MGI:103070; H2-Ab1.
DR VEuPathDB; HostDB:ENSMUSG00000073421; -.
DR eggNOG; ENOG502RYBQ; Eukaryota.
DR GeneTree; ENSGT00940000154723; -.
DR HOGENOM; CLU_047501_13_1_1; -.
DR OMA; FTWQRRV; -.
DR OrthoDB; 1186163at2759; -.
DR PhylomeDB; P14483; -.
DR TreeFam; TF336626; -.
DR BioGRID-ORCS; 14961; 2 hits in 76 CRISPR screens.
DR ChiTaRS; H2-Ab1; mouse.
DR EvolutionaryTrace; P14483; -.
DR Proteomes; UP000000589; Chromosome 17.
DR Bgee; ENSMUSG00000073421; Expressed in peripheral lymph node and 177 other tissues.
DR ExpressionAtlas; P14483; baseline and differential.
DR Genevisible; P14483; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0042613; C:MHC class II protein complex; IDA:MGI.
DR GO; GO:0005771; C:multivesicular body; 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:1990405; F:protein antigen binding; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0015643; F:toxic substance binding; IPI:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
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:0002344; P:B cell affinity maturation; IDA:BHF-UCL.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:BHF-UCL.
DR GO; GO:0006955; P:immune response; IMP:MGI.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0046635; P:positive regulation of alpha-beta T cell activation; IDA:BHF-UCL.
DR GO; GO:0002579; P:positive regulation of antigen processing and presentation; IDA:BHF-UCL.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; 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; IPR000353; MHC_II_b_N.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00969; MHC_II_beta; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00921; MHC_II_beta; 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; Ubl conjugation.
FT SIGNAL 1..27
FT CHAIN 28..265
FT /note="H-2 class II histocompatibility antigen, A beta
FT chain"
FT /id="PRO_0000018993"
FT TOPO_DOM 28..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 125..213
FT /note="Ig-like C1-type"
FT REGION 28..122
FT /note="Beta-1"
FT REGION 123..216
FT /note="Beta-2"
FT REGION 217..226
FT /note="Connecting peptide"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 145..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:1MUJ"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:1MUJ"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:1MUJ"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1MUJ"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1MUJ"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1MUJ"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1MUJ"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:1MUJ"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1MUJ"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:1MUJ"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:1MUJ"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1MUJ"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1MUJ"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1LNU"
FT STRAND 142..153
FT /evidence="ECO:0007829|PDB:1MUJ"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:1MUJ"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1MUJ"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1MUJ"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1MUJ"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:1MUJ"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1MUJ"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1MUJ"
SQ SEQUENCE 265 AA; 30128 MW; DA5118187D254BD6 CRC64;
MALQIPSLLL SAAVVVLMVL SSPGTEGGDS ERHFVYQFMG ECYFTNGTQR IRYVTRYIYN
REEYVRYDSD VGEHRAVTEL GRPDAEYWNS QPEILERTRA ELDTVCRHNY EGPETHTSLR
RLEQPNVVIS LSRTEALNHH NTLVCSVTDF YPAKIKVRWF RNGQEETVGV SSTQLIRNGD
WTFQVLVMLE MTPRRGEVYT CHVEHPSLKS PITVEWRAQS ESAWSKMLSG IGGCVLGVIF
LGLGLFIRHR SQKGPRGPPP AGLLQ
