HB2K_MOUSE
ID HB2K_MOUSE Reviewed; 263 AA.
AC P06343; Q31137;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=H-2 class II histocompatibility antigen, A-K 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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-214.
RC STRAIN=CRO435;
RX PubMed=3692165; DOI=10.1017/s0016672300023545;
RA Golubic M., Budimir O., Schoepfer R., Kasahara M., Mayer W.E., Figueroa F.,
RA Klein J.;
RT "Nucleotide sequence analysis of class II genes borne by mouse t
RT chromosomes.";
RL Genet. Res. 50:137-146(1987).
RN [3]
RP GLYCOSYLATION AT ASN-46.
RX PubMed=3980466; DOI=10.1016/s0021-9258(18)89229-8;
RA Swiedler S.J., Freed J.H., Tarentino A.L., Plummer T.H. Jr., Hart G.W.;
RT "Oligosaccharide microheterogeneity of the murine major histocompatibility
RT antigens. Reproducible site-specific patterns of sialylation and branching
RT in asparagine-linked oligosaccharides.";
RL J. Biol. Chem. 260:4046-4054(1985).
RN [4]
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 [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 32-216.
RX PubMed=9529148; DOI=10.1016/s1074-7613(00)80536-1;
RA Fremont D.H., Monnaie D., Nelson C.A., Hendrickson W.A., Unanue E.R.;
RT "Crystal structure of I-Ak in complex with a dominant epitope of
RT lysozyme.";
RL Immunity 8:305-317(1998).
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; M13538; AAA39632.1; -; mRNA.
DR EMBL; M27456; AAA57291.1; -; Genomic_DNA.
DR PIR; A02238; HLMSBK.
DR PIR; I68208; I68208.
DR PIR; PL0285; PL0285.
DR PIR; PL0286; PL0286.
DR PDB; 1D9K; X-ray; 3.20 A; D/H=30-216.
DR PDB; 1IAK; X-ray; 1.90 A; B=34-216.
DR PDB; 1JL4; X-ray; 4.30 A; B=34-216.
DR PDBsum; 1D9K; -.
DR PDBsum; 1IAK; -.
DR PDBsum; 1JL4; -.
DR AlphaFoldDB; P06343; -.
DR SMR; P06343; -.
DR DIP; DIP-6134N; -.
DR IntAct; P06343; 1.
DR MINT; P06343; -.
DR iPTMnet; P06343; -.
DR jPOST; P06343; -.
DR MaxQB; P06343; -.
DR PRIDE; P06343; -.
DR ProteomicsDB; 270893; -.
DR MGI; MGI:103070; H2-Ab1.
DR ChiTaRS; H2-Ab1; mouse.
DR EvolutionaryTrace; P06343; -.
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 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..263
FT /note="H-2 class II histocompatibility antigen, A-K beta
FT chain"
FT /id="PRO_0000018996"
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:0000269|PubMed:3980466"
FT DISULFID 42..104
FT DISULFID 143..199
FT CONFLICT 36
FT /note="H -> Y (in Ref. 2; AAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="I -> T (in Ref. 2; AAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 64..65
FT /note="YV -> FM (in Ref. 2; AAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="A -> V (in Ref. 2; AAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="K -> S (in Ref. 2; AAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="P -> H (in Ref. 2; AAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="L -> F (in Ref. 2; AAA57291)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="S -> N (in Ref. 2; AAA57291)"
FT /evidence="ECO:0000305"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:1IAK"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1IAK"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1IAK"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1IAK"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1IAK"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:1IAK"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1IAK"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:1IAK"
FT TURN 111..115
FT /evidence="ECO:0007829|PDB:1IAK"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1D9K"
FT STRAND 139..151
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1IAK"
SQ SEQUENCE 263 AA; 29967 MW; 48F8FB38370EADF8 CRC64;
MALQIPSLLL LAAVVVLTVL SSPGTEGGNS ERHFVHQFQP FCYFTNGTQR IRLVIRYIYN
REEYVRFDSD VGEYRAVTEL GRPDAEYWNK QYLERTRAEL DTVCRHNYEK TETPTSLRRL
EQPSVVISLS RTEALNHHNT LVCSVTDFYP AKIKVRWFRN GQEETVGVSS TQLIRNGDWT
FQVLVMLEMT PRRGEVYTCH VEHPSLKSPI TVEWRAQSES ARSKMLSGIG GCVLGVIFLG
LGLFIRHRSQ KGPRGPPPAG LLQ
