HB24_MOUSE
ID HB24_MOUSE Reviewed; 264 AA.
AC P20040;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=H-2 class II histocompatibility antigen, E-Q beta chain;
DE AltName: Full=E-W17;
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=2460545;
RA Vu T.H., Tacchini-Cottier F.M., Day C.E., Begovich A.B., Jones P.P.;
RT "Molecular basis for the defective expression of the mouse Ew17 beta
RT gene.";
RL J. Immunol. 141:3654-3661(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2106558;
RA Begovich A.B., Vu T.H., Jones P.P.;
RT "Characterization of the molecular defects in the mouse E beta f and E beta
RT q genes. Implications for the origin of MHC polymorphism.";
RL J. Immunol. 144:1957-1964(1990).
RN [3]
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 -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR EMBL; M23693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M35682; AAA39595.1; -; Genomic_DNA.
DR EMBL; M35680; AAA39595.1; JOINED; Genomic_DNA.
DR EMBL; M35681; AAA39595.1; JOINED; Genomic_DNA.
DR PIR; A30529; A30529.
DR AlphaFoldDB; P20040; -.
DR SMR; P20040; -.
DR GlyGen; P20040; 1 site.
DR PhosphoSitePlus; P20040; -.
DR MaxQB; P20040; -.
DR PRIDE; P20040; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P20040; 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 1: Evidence at protein level;
KW Adaptive immunity; Disulfide bond; Glycoprotein; Immunity; Membrane;
KW MHC II; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT CHAIN 27..264
FT /note="H-2 class II histocompatibility antigen, E-Q beta
FT chain"
FT /id="PRO_0000019002"
FT TOPO_DOM 27..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 124..214
FT /note="Ig-like C1-type"
FT REGION 27..121
FT /note="Beta-1"
FT REGION 122..225
FT /note="Beta-2"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 264 AA; 30205 MW; FF81C532A9B72D7A CRC64;
MVWLPRVPCV AAVILLLTVL SPPVALVRDS RPWFLEYCKS ECHFYNGTQR VRFLKRYFYN
LEENLRFDSD VGEFRAVTEL GRPDAENWNS QPEILEQKRA AVDTYCRHNY EIFDNFLVRR
RVEPTVTVYP TKTQPLEHHN LLVCSVSDFY PGNIEVRWFR NGKEEKTGIV STGLVRNGDW
TFQTLVMLET VPQSGEVYTC QVEHPSLTDP VTVEWKAQST SAQNKMLSGV GGFVLGLLFL
GAGLFIYFRN QKGQSGLQPT GLLS
