HA23_MOUSE
ID HA23_MOUSE Reviewed; 255 AA.
AC P14439; Q31092;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=H-2 class II histocompatibility antigen, E-U alpha chain;
DE Flags: Precursor;
GN Name=H2-Ea; Synonyms=H2-Ea-ps;
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].
RC STRAIN=TW2; TISSUE=Spleen;
RX PubMed=7495754; DOI=10.1093/intimm/7.9.1459;
RA Tacchini-Cottier F., Mayer W.E., Begovich A.B., Jones P.P.;
RT "Inactivation of E alpha and E beta expression in inbred and wild mice by
RT multiple distinct mutations, some of which predate speciation within Mus
RT species.";
RL Int. Immunol. 7:1459-1471(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-255.
RC STRAIN=B10.PL; TISSUE=Spleen;
RX PubMed=3755150;
RA Ayane M., Mengle-Gaw L., McDevitt H.O., Benoist C., Mathis D.;
RT "E alpha u and E beta u chain association: where lies the anomaly?";
RL J. Immunol. 137:948-951(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-109.
RC STRAIN=NZW/LacJ;
RX PubMed=2769184; DOI=10.1084/jem.170.3.971;
RA Schiffenbauer J., McCarthy D.M., Nygard N.R., Woulfe S.L., Didier D.K.,
RA Schwartz B.D.;
RT "A unique sequence of the NZW I-E beta chain and its possible contribution
RT to autoimmunity in the (NZB x NZW)F1 mouse.";
RL J. Exp. Med. 170:971-984(1989).
RN [4]
RP ANALYSIS OF THE HAPLOTYPE-SPECIFIC VARIABLE EXPRESSION.
RX PubMed=6937437; DOI=10.1007/bf01561674;
RA Jones P.P., Murphy D.B., McDevitt H.O.;
RT "Variable synthesis and expression of E alpha and Ae (E beta) Ia
RT polypeptide chains in mice of different H-2 haplotypes.";
RL Immunogenetics 12:321-337(1981).
RN [5]
RP TRANSCRIPT ANALYSIS, AND POLYMORPHISM.
RX PubMed=6296871; DOI=10.1073/pnas.80.1.273;
RA Mathis D.J., Benoist C., Williams V.E. II, Kanter M., McDevitt H.O.;
RT "Several mechanisms can account for defective E alpha gene expression in
RT different mouse haplotypes.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:273-277(1983).
RN [6]
RP POLYMORPHISM.
RX PubMed=2701937;
RA Vu T.H., Begovich A.B., Tacchini-Cottier F.M., Jones P.P.;
RT "Molecular defects in the non-expressed H-2 E alpha genes of the f and q
RT haplotypes.";
RL J. Immunol. 142:2936-2942(1989).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- POLYMORPHISM: In H2b and H2s haplotype strains (e.g. C57BL/6, C57BL/10,
CC C57L/J, LP/J, 129 and SJL/J mice), there is a deletion of 627 bp in the
CC promoter and the first exon, leading to a failure to express the gene.
CC In the haplotype H2q gene, an insertion in the second exon results in a
CC frameshift and a premature stop codon, and in the haplotype H2f gene, a
CC base substitution creates a stop codon in the first exon, leading to
CC defective protein translation in the strains of these haplotypes.
CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
CC -!- CAUTION: Defined as a polymorphic pseudogene by MGI. {ECO:0000305}.
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DR EMBL; U13648; AAC52482.1; -; mRNA.
DR EMBL; M12818; AAA39638.1; -; mRNA.
DR PIR; I55971; I55971.
DR PIR; PL0127; PL0127.
DR RefSeq; NP_034511.2; NM_010381.2.
DR AlphaFoldDB; P14439; -.
DR SMR; P14439; -.
DR PRIDE; P14439; -.
DR GeneID; 100504404; -.
DR KEGG; mmu:100504404; -.
DR CTD; 100504404; -.
DR MGI; MGI:95900; H2-Ea.
DR OrthoDB; 1132781at2759; -.
DR BioGRID-ORCS; 100504404; 2 hits in 17 CRISPR screens.
DR ChiTaRS; H2-Ea-ps; 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; ISO:MGI.
DR GO; GO:0042613; C:MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IDA:MGI.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0050778; P:positive regulation of immune response; IDA:MGI.
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 2: Evidence at transcript level;
KW Adaptive immunity; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; MHC II; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..255
FT /note="H-2 class II histocompatibility antigen, E-U alpha
FT chain"
FT /id="PRO_0000080750"
FT TOPO_DOM 26..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..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 CONFLICT 47
FT /note="Y -> F (in Ref. 1; AAC52482)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="K -> E (in Ref. 1; AAC52482)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="V -> I (in Ref. 1; AAC52482)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="L -> F (in Ref. 1; AAC52482)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="Q -> R (in Ref. 1; AAC52482)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="K -> T (in Ref. 1; AAC52482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 29108 MW; 7CD23D89374D4B37 CRC64;
MATIGALLLR FFFIAVLMSS QKSWAIKEEH TIIQAEFYLL PDKRGEYMFD FDGDEIFHVD
IEKSETIWRL EEFAKFASFE AQGALANIAV DKANLDVMKK RSNNTPDANV APEVTVLSRS
PVNLGEPNIL VCFIDKFSPP VVNVTWLRNG QPVTEGVSET VFLPRDDHLF RKFHYLTFLP
STDDFYDCEV DHWGLEEPLR KHWEFEEKTL LPETKENVVC ALGLFVGLVG IVVGIILIMK
GIKKRNVVER RQGAL
