HA22_MOUSE
ID HA22_MOUSE Reviewed; 255 AA.
AC P04224;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=H-2 class II histocompatibility antigen, E-K alpha 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 [GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A/J;
RX PubMed=6403249; DOI=10.1016/0092-8674(83)90060-0;
RA Mathis D.J., Benoist C.O., Williams V.E. II, Kanter M.R., McDevitt H.O.;
RT "The murine E alpha immune response gene.";
RL Cell 32:745-754(1983).
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; V00833; CAA24216.2; -; Genomic_DNA.
DR EMBL; V00834; CAA24216.2; JOINED; Genomic_DNA.
DR PIR; A21938; HLMSEA.
DR PIR; B91743; HLMSED.
DR RefSeq; NP_034511.2; NM_010381.2.
DR PDB; 1FNE; X-ray; 1.90 A; A/C=26-217.
DR PDB; 1FNG; X-ray; 1.90 A; A/C=26-217.
DR PDB; 1I3R; X-ray; 2.40 A; A/C/E/G=26-217.
DR PDB; 1R5V; X-ray; 2.50 A; A/C=28-207.
DR PDB; 1R5W; X-ray; 2.90 A; A/C=28-207.
DR PDB; 3QIB; X-ray; 2.70 A; A=26-216.
DR PDB; 3QIU; X-ray; 2.70 A; A=28-206.
DR PDB; 3QIW; X-ray; 3.30 A; A=26-217.
DR PDB; 4P2O; X-ray; 2.60 A; A=26-216.
DR PDB; 4P2Q; X-ray; 3.30 A; A/F/K/P=26-216.
DR PDB; 4P2R; X-ray; 3.30 A; A/F/K/P=26-216.
DR PDB; 6BGA; X-ray; 2.31 A; A=26-216.
DR PDBsum; 1FNE; -.
DR PDBsum; 1FNG; -.
DR PDBsum; 1I3R; -.
DR PDBsum; 1R5V; -.
DR PDBsum; 1R5W; -.
DR PDBsum; 3QIB; -.
DR PDBsum; 3QIU; -.
DR PDBsum; 3QIW; -.
DR PDBsum; 4P2O; -.
DR PDBsum; 4P2Q; -.
DR PDBsum; 4P2R; -.
DR PDBsum; 6BGA; -.
DR AlphaFoldDB; P04224; -.
DR SMR; P04224; -.
DR IntAct; P04224; 1.
DR GlyGen; P04224; 2 sites.
DR PRIDE; P04224; -.
DR GeneID; 100504404; -.
DR KEGG; mmu:100504404; -.
DR UCSC; uc008cck.1; mouse.
DR CTD; 100504404; -.
DR EvolutionaryTrace; P04224; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P04224; 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; 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..25
FT CHAIN 26..255
FT /note="H-2 class II histocompatibility antigen, E-K alpha
FT chain"
FT /id="PRO_0000018979"
FT TOPO_DOM 26..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 112..204
FT /note="Ig-like C1-type"
FT REGION 26..109
FT /note="Alpha-1"
FT REGION 110..203
FT /note="Alpha-2"
FT REGION 204..216
FT /note="Connecting peptide"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 132..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 30..40
FT /evidence="ECO:0007829|PDB:1FNE"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1FNE"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1FNE"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:1FNE"
FT HELIX 81..101
FT /evidence="ECO:0007829|PDB:1FNE"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 128..140
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:1FNE"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:3QIB"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1FNE"
SQ SEQUENCE 255 AA; 29121 MW; 144EEA3AB1EF3724 CRC64;
MATIGALVLR FFFIAVLMSS QKSWAIKEEH TIIQAEFYLL PDKRGEFMFD FDGDEIFHVD
IEKSETIWRL EEFAKFASFE AQGALANIAV DKANLDVMKE RSNNTPDANV APEVTVLSRS
PVNLGEPNIL ICFIDKFSPP VVNVTWLRNG RPVTEGVSET VFLPRDDHLF RKFHYLTFLP
STDDFYDCEV DHWGLEEPLR KHWEFEEKTL LPETKENVVC ALGLFVGLVG IVVGIILIMK
GIKKRNVVER RQGAL
