HB22_MOUSE
ID HB22_MOUSE Reviewed; 264 AA.
AC P01915;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=H-2 class II histocompatibility antigen, E-D beta chain;
DE Flags: Precursor;
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=6310581; DOI=10.1073/pnas.80.18.5520;
RA Saito H., Maki R.A., Clayton L.K., Tonegawa S.;
RT "Complete primary structures of the E beta chain and gene of the mouse
RT major histocompatibility complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:5520-5524(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RX PubMed=6087163; DOI=10.1038/310594a0;
RA Gillies S.D., Folsom V., Tonegawa S.;
RT "Cell type-specific enhancer element associated with a mouse MHC gene, E
RT beta.";
RL Nature 310:594-597(1984).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: The structure of the E beta gene is more similar to
CC class I MHC genes than to class II, in that, unlike either the E alpha
CC or DR alpha genes, (1) the core portion of the E beta cytoplasmic
CC segment is encoded by its own exon and (2) the sixth exon of the E beta
CC chain is not split into two exons, but rather encodes both the carboxyl
CC end of the cytoplasmic segment and the entire 3'-UTR.
CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR EMBL; X00777; CAA25354.1; -; Genomic_DNA.
DR EMBL; K00123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A02225; HLMSEB.
DR AlphaFoldDB; P01915; -.
DR SMR; P01915; -.
DR GlyGen; P01915; 1 site.
DR MaxQB; P01915; -.
DR PeptideAtlas; P01915; -.
DR PRIDE; P01915; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01915; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0042613; C:MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IBA:GO_Central.
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 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 3: Inferred from homology;
KW Adaptive immunity; Disulfide bond; Glycoprotein; Immunity; Membrane;
KW MHC II; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT CHAIN 32..264
FT /note="H-2 class II histocompatibility antigen, E-D beta
FT chain"
FT /id="PRO_0000019001"
FT TOPO_DOM 32..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 124..214
FT /note="Ig-like C1-type"
FT REGION 32..121
FT /note="Beta-1"
FT REGION 122..215
FT /note="Beta-2"
FT REGION 216..225
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 144..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 264 AA; 30049 MW; 29117F30B8A56942 CRC64;
MVWLPRVPCV AAVILLLTVL SPPVALVRDT RPRFLEYVTS ECHFYNGTQH VRFLERFIYN
REENLRFDSD VGEYRAVTEL GRPDAENWNS QPEILEDARA SVDTYCRHNY EISDKFLVRR
RVEPTVTVYP TKTQPLEHHN LLVCSVSDFY PGNIEVRWFR NGKEEETGIV STGLVRNGDW
TFQTLVMLET VPQSGEVYTC QVEHPSLTDP VTVEWKAQST SAQNKMLSGV GGFVLGLLFL
GAGLFIYFRN QKGQSGLQPT GLLS
