HA2K_MOUSE
ID HA2K_MOUSE Reviewed; 256 AA.
AC P01910;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=H-2 class II histocompatibility antigen, A-K alpha chain;
DE Flags: Precursor;
GN Name=H2-Aa;
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=3137158; DOI=10.1007/bf00375858;
RA Bishop G.A., McMillan M.S., Haughton G., Frelinger J.A.;
RT "Signaling to a B-cell clone by Ek, but not Ak, does not reflect alteration
RT of Ak genes.";
RL Immunogenetics 28:184-192(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6300851; DOI=10.1073/pnas.80.2.534;
RA Benoist C.O., Mathis D.J., Kanter M.R., Williams V.E., McDevitt H.O.;
RT "The murine Ia alpha chains, E alpha and A alpha, show a surprising degree
RT of sequence homology.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:534-538(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-256.
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-256.
RX PubMed=2581258; DOI=10.1073/pnas.82.9.2930;
RA Landais D., Matthes H., Benoist C., Mathis D.;
RT "A molecular basis for the Ia.2 and Ia.19 antigenic determinants.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2930-2934(1985).
RN [5]
RP GLYCOSYLATION AT ASN-105 AND ASN-145.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, 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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 27-208.
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 -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR EMBL; M21931; AAA39636.1; -; mRNA.
DR EMBL; V00832; CAA24215.1; -; mRNA.
DR EMBL; M11357; AAA39613.1; -; mRNA.
DR PIR; A02217; HLMSAA.
DR PIR; I54447; I54447.
DR PDB; 1D9K; X-ray; 3.20 A; C/G=27-209.
DR PDB; 1IAK; X-ray; 1.90 A; A=24-222.
DR PDB; 1JL4; X-ray; 4.30 A; A=31-208.
DR PDBsum; 1D9K; -.
DR PDBsum; 1IAK; -.
DR PDBsum; 1JL4; -.
DR AlphaFoldDB; P01910; -.
DR SMR; P01910; -.
DR DIP; DIP-6133N; -.
DR IntAct; P01910; 1.
DR MINT; P01910; -.
DR GlyGen; P01910; 2 sites.
DR iPTMnet; P01910; -.
DR PhosphoSitePlus; P01910; -.
DR MaxQB; P01910; -.
DR PeptideAtlas; P01910; -.
DR PRIDE; P01910; -.
DR ProteomicsDB; 269806; -.
DR MGI; MGI:95895; H2-Aa.
DR InParanoid; P01910; -.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse.
DR Reactome; R-MMU-202433; Generation of second messenger molecules.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-389948; PD-1 signaling.
DR ChiTaRS; H2-Aa; mouse.
DR EvolutionaryTrace; P01910; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01910; protein.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0042613; C:MHC class II protein complex; 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:0042130; P:negative regulation of T cell proliferation; ISO: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 GO; GO:0045582; P:positive regulation of T cell differentiation; IDA:MGI.
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; IPR001003; MHC_II_a_N.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00993; MHC_II_alpha; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00920; MHC_II_alpha; 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..23
FT /evidence="ECO:0000250"
FT CHAIN 24..256
FT /note="H-2 class II histocompatibility antigen, A-K alpha
FT chain"
FT /id="PRO_0000018977"
FT TOPO_DOM 24..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 114..206
FT /note="Ig-like C1-type"
FT REGION 24..111
FT /note="Alpha-1"
FT REGION 112..205
FT /note="Alpha-2"
FT REGION 206..218
FT /note="Connecting peptide"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3980466"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3980466"
FT DISULFID 134..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 30..42
FT /evidence="ECO:0007829|PDB:1IAK"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1IAK"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1IAK"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:1IAK"
FT HELIX 83..104
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1D9K"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1D9K"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1IAK"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1IAK"
SQ SEQUENCE 256 AA; 28351 MW; 78E7D4A33CCE4582 CRC64;
MPRSRALILG VLALTTMLSL CGGEDDIEAD HVGSYGITVY QSPGDIGQYT FEFDGDELFY
VDLDKKETVW MLPEFAQLRR FEPQGGLQNI ATGKHNLEIL TKRSNSTPAT NEAPQATVFP
KSPVLLGQPN TLICFVDNIF PPVINITWLR NSKSVTDGVY ETSFFVNRDY SFHKLSYLTF
IPSDDDIYDC KVEHWGLEEP VLKHWEPEIP APMSELTETV VCALGLSVGL VGIVVGTIFI
IQGLRSGGTS RHPGPL
