HB2F_MOUSE
ID HB2F_MOUSE Reviewed; 252 AA.
AC P06346;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=H-2 class II histocompatibility antigen, A-F beta chain;
DE Flags: Precursor; Fragment;
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 [MRNA].
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 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 [3]
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}.
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DR EMBL; M13541; AAA39629.1; -; mRNA.
DR PIR; A02241; HLMSBF.
DR AlphaFoldDB; P06346; -.
DR SMR; P06346; -.
DR MINT; P06346; -.
DR jPOST; P06346; -.
DR MaxQB; P06346; -.
DR PRIDE; P06346; -.
DR ProteomicsDB; 269680; -.
DR MGI; MGI:103070; H2-Ab1.
DR ChiTaRS; H2-Ab1; mouse.
DR Proteomes; UP000000589; Unplaced.
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: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: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;
KW Ubl conjugation.
FT SIGNAL <1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..252
FT /note="H-2 class II histocompatibility antigen, A-F beta
FT chain"
FT /id="PRO_0000018995"
FT TOPO_DOM 17..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 112..200
FT /note="Ig-like C1-type"
FT REGION 17..109
FT /note="Beta-1"
FT REGION 110..203
FT /note="Beta-2"
FT REGION 204..213
FT /note="Connecting peptide"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 132..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
SQ SEQUENCE 252 AA; 28602 MW; E9D91C8A213E629B CRC64;
AAVVVLMVLS SPGTEGGNSE RHFVSQFKGE CYFTNGTQRI RSVDRYIYNR EEYLRFDSDV
GEYRAVTELG RSDAEYYNKQ YLERTRAELD TVCRHNYEGV ETPTSLRRLE QPNVVISLSR
TEALNHHNTL VCSVTDFYPA KIKVRWFRNG QEETVGVSST QLIRNGDWTF QVLVMLEMAP
RRGEVYTCHV EHPSLKSPIT VEWRAQSESA RSKMLSGIGG CVLGVIFLGL GLFIRYRSQK
GPRGPPPAGL LQ
