ID HB2D_MOUSE Reviewed; 265 AA.
AC P01921; O19456; O19457; O19458; Q31133; Q31138; Q31139;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 13-SEP-2023, entry version 153.
DE RecName: Full=H-2 class II histocompatibility antigen, A-D beta chain;
DE Flags: Precursor;
GN Name=H2-Ab1;
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=6410508; DOI=10.1126/science.6410508;
RA Malissen M., Hunkapiller T., Hood L.E.;
RT "Nucleotide sequence of a light chain gene of the mouse I-A subregion: A
RT beta d.";
RL Science 221:750-754(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-265.
RX PubMed=6407114; DOI=10.1126/science.6407114;
RA Choi E.C., McIntyre K., Germain R.N., Seidman J.G.;
RT "Murine i-a-beta chain polymorphism: nucleotide sequences of three allelic
RT i-a-beta genes.";
RL Science 221:283-286(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 124-261.
RX PubMed=2555693; DOI=10.1128/mcb.9.10.4402-4408.1989;
RA Ghogawala Z., Choi E., Daly K.R., Blanco L.R., Griffith I.J.,
RA Glimcher L.H.;
RT "An intronic 10-base-pair deletion in a class II A beta gene affects RNA
RT processing.";
RL Mol. Cell. Biol. 9:4402-4408(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 215-265.
RX PubMed=6311906;
RA Robinson R.R., Germain R.N., McKean D.J., Mescher M., Seidman J.G.;
RT "Extensive polymorphism surrounding the murine Ia A-beta chain gene.";
RL J. Immunol. 131:2025-2031(1983).
RN [5]
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 [6]
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
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; K00008; AAA39548.1; -; Genomic_DNA.
DR EMBL; K00007; AAA39548.1; JOINED; Genomic_DNA.
DR EMBL; M29248; AAA39543.1; -; Genomic_DNA.
DR EMBL; K00113; AAA39544.1; -; Genomic_DNA.
DR EMBL; K00109; AAA39544.1; JOINED; Genomic_DNA.
DR EMBL; K00110; AAA39544.1; JOINED; Genomic_DNA.
DR EMBL; K00112; AAA39544.1; JOINED; Genomic_DNA.
DR EMBL; K00111; AAA39544.1; JOINED; Genomic_DNA.
DR EMBL; K01143; AAA39545.1; -; mRNA.
DR PIR; A02236; HLMSAB.
DR PDB; 1IAO; X-ray; 2.60 A; B=28-216.
DR PDB; 2IAD; X-ray; 2.40 A; B=28-216.
DR PDB; 7RDV; X-ray; 2.90 A; B=31-216.
DR PDBsum; 1IAO; -.
DR PDBsum; 2IAD; -.
DR PDBsum; 7RDV; -.
DR AlphaFoldDB; P01921; -.
DR SMR; P01921; -.
DR MINT; P01921; -.
DR GlyCosmos; P01921; 1 site, No reported glycans.
DR GlyGen; P01921; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P01921; -.
DR jPOST; P01921; -.
DR MaxQB; P01921; -.
DR PeptideAtlas; P01921; -.
DR ProteomicsDB; 269679; -.
DR ABCD; P01921; 3 sequenced antibodies.
DR AGR; MGI:103070; -.
DR MGI; MGI:103070; H2-Ab1.
DR InParanoid; P01921; -.
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-Ab1; mouse.
DR EvolutionaryTrace; P01921; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01921; Protein.
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:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0016020; C: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: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: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: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 CDD; cd21001; IgC1_MHC_II_beta_HLA-DQ_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; IPR000353; MHC_II_b_N.
DR PANTHER; PTHR19944:SF101; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DQ BETA 1 CHAIN; 1.
DR PANTHER; PTHR19944; MHC CLASS II-RELATED; 1.
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; Immunoglobulin; 1.
DR SUPFAM; SSF54452; MHC antigen-recognition domain; 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-D beta
FT chain"
FT /id="PRO_0000018994"
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 35..45
FT /evidence="ECO:0007829|PDB:2IAD"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:2IAD"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2IAD"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2IAD"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:2IAD"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:2IAD"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:2IAD"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:2IAD"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 143..153
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:7RDV"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:2IAD"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1IAO"
SQ SEQUENCE 265 AA; 29954 MW; 3A6274DD8920F564 CRC64;
MALQIPSLLL SAAVVVLMVL SSPRTEGGNS ERHFVVQFKG ECYYTNGTQR IRLVTRYIYN
REEYVRYDSD VGEYRAVTEL GRPDAEYWNS QPEILERTRA EVDTACRHNY EGPETSTSLR
RLEQPNVAIS LSRTEALNHH NTLVCSVTDF YPAKIKVRWF RNGQEETVGV SSTQLIRNGD
WTFQVLVMLE MTPHQGEVYT CHVEHPSLKS PITVEWRAQS ESARSKMLSG IGGCVLGVIF
LGLGLFIRHR SQKGPRGPPP AGLLQ
//
