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HA2F_MOUSE
ID   HA2F_MOUSE              Reviewed;         233 AA.
AC   P14435;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=H-2 class II histocompatibility antigen, A-F alpha chain;
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=6309407; DOI=10.1016/0092-8674(83)90147-2;
RA   Benoist C.O., Mathis D.J., Kanter M.R., Williams V.E., McDevitt H.O.;
RT   "Regions of allelic hypervariability in the murine A alpha immune response
RT   gene.";
RL   Cell 34:169-177(1983).
RN   [2]
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).
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; K01924; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P14435; -.
DR   SMR; P14435; -.
DR   MaxQB; P14435; -.
DR   PRIDE; P14435; -.
DR   ProteomicsDB; 269805; -.
DR   MGI; MGI:95895; H2-Aa.
DR   ChiTaRS; H2-Aa; mouse.
DR   Proteomes; UP000000589; Unplaced.
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   Adaptive immunity; Disulfide bond; Glycoprotein; Immunity; Membrane;
KW   MHC II; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..233
FT                   /note="H-2 class II histocompatibility antigen, A-F alpha
FT                   chain"
FT                   /id="PRO_0000080745"
FT   TOPO_DOM        1..195
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..233
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          91..183
FT                   /note="Ig-like C1-type"
FT   REGION          1..88
FT                   /note="Alpha-1"
FT   REGION          89..182
FT                   /note="Alpha-2"
FT   REGION          183..195
FT                   /note="Connecting peptide"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        111..167
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   233 AA;  25930 MW;  E8D64AD44FAC79D8 CRC64;
     EDDIEADHVG FYGISVYQSP GDIGQYTFEF DGDEWFYVDL DKKETVWRLP EFGQLTSFDP
     QGGLQEIATG KHNLGILTKR SNFTPATNEA PQATVFPKSP VLLGQPNTLI CFVDNIFPPV
     INITWLRNSK SVTDGVYETS FLVNRDHSFH KLSYLTFIPS DDDIYDCKVE HWGLEEPVLK
     HWEPEIPAPM SELTETVVCA LGLSVGLVGI VVGTIFIIQG LRSGGTSRHP GPL
 
 
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