HB2U_MOUSE
ID HB2U_MOUSE Reviewed; 263 AA.
AC P06344;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=H-2 class II histocompatibility antigen, A-U 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.
RX PubMed=3086866; DOI=10.1073/pnas.83.11.3594;
RA Estess P., Begovich A.B., Koo M., Jones P.P., McDevitt H.O.;
RT "Sequence analysis and structure-function correlations of murine q, k, u,
RT s, and f haplotype I-A beta cDNA clones.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3594-3598(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 174-263.
RX PubMed=3500915; DOI=10.3109/08820138709087096;
RA Sharma S., King L.B., Corley R.B., Maki R.;
RT "Comparative sequence analysis of cDNA clones encoding I-A molecules of the
RT CH12 B cell lymphoma: nucleotide differences do not account for their
RT 'defective' function in B cell stimulation.";
RL Immunol. Invest. 16:425-436(1987).
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 PIR; A02239; HLMSBU.
DR PDB; 1K2D; X-ray; 2.20 A; B=28-216.
DR PDB; 1U3H; X-ray; 2.42 A; D/H=28-215.
DR PDB; 2P24; X-ray; 2.15 A; B=28-224.
DR PDB; 2PXY; X-ray; 2.23 A; D=29-217.
DR PDB; 2Z31; X-ray; 2.70 A; D=28-216.
DR PDBsum; 1K2D; -.
DR PDBsum; 1U3H; -.
DR PDBsum; 2P24; -.
DR PDBsum; 2PXY; -.
DR PDBsum; 2Z31; -.
DR AlphaFoldDB; P06344; -.
DR SMR; P06344; -.
DR MINT; P06344; -.
DR GlyGen; P06344; 1 site.
DR jPOST; P06344; -.
DR MaxQB; P06344; -.
DR PRIDE; P06344; -.
DR EvolutionaryTrace; P06344; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P06344; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 3D-structure; Adaptive immunity; Disulfide bond; Glycoprotein; Immunity;
KW Membrane; MHC II; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT CHAIN 28..263
FT /note="H-2 class II histocompatibility antigen, A-U beta
FT chain"
FT /id="PRO_0000018999"
FT TOPO_DOM 28..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 123..211
FT /note="Ig-like C1-type"
FT REGION 28..120
FT /note="Beta-1"
FT REGION 121..214
FT /note="Beta-2"
FT REGION 215..224
FT /note="Connecting peptide"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 143..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:2P24"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:2P24"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2P24"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2P24"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2P24"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:2P24"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:2P24"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:2P24"
FT TURN 112..118
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1K2D"
FT STRAND 140..151
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:2P24"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2P24"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2P24"
SQ SEQUENCE 263 AA; 30041 MW; 1ECEF8669CF91389 CRC64;
MALQIPSLLL LAAVVVLMVL SSPGTEGGDS ERHFVVQFQP FCYFTNGTQR IRYVTRYIYN
REEYLRFDSD VGEYRAVTEL GRPDAEYYNK QYLERTRAEL DTVCRYNYEE TEVPTSLRRL
EQPNVVISLS RTEALNHHNT LVCSVTDFYP AKIKVRWFRN GQEETVGVSS TQLIRNGDWT
FQVLVMLEMT PRRGEVYTCH VEHPSLKSPI TVEWRAQSES ARSKMLSGIG GCVLGVIFLG
LGLFIRHRSQ KGPRGPPPAG LLQ
