HA1Y_MOUSE
ID HA1Y_MOUSE Reviewed; 298 AA.
AC P01895;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=H-2 class I histocompatibility antigen, alpha chain;
DE AltName: Full=Clone PAG64;
DE Flags: Fragment;
GN Name=H2-D1;
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] OF 1-285 (CLONE PAG64).
RX PubMed=6318117; DOI=10.1038/306756a0;
RA Brickell P.M., Latchman D.S., Murphy D., Willison K., Rigby P.W.J.;
RT "Activation of a Qa/Tla class I major histocompatibility antigen gene is a
RT general feature of oncogenesis in the mouse.";
RL Nature 306:756-760(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 90-298 (CLONE PH-2D-1).
RX PubMed=6895103; DOI=10.1038/292078a0;
RA Bregegere F., Abastado J.P., Kvist S., Rask L., Lalanne J.-L., Garoff H.,
RA Cami B., Wiman K.G., Larhammar D., Peterson P.A., Gachelin G.,
RA Kourilsky P., Dobberstein B.;
RT "Structure of C-terminal half of two H-2 antigens from cloned mRNA.";
RL Nature 292:78-81(1981).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-292, VARIANT
RP [LARGE SCALE ANALYSIS] GLY-285, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-285, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 -!- FUNCTION: Involved in the presentation of foreign antigens to the
CC immune system.
CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-
CC microglobulin).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P01895-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P01895-2; Sequence=VSP_003228;
CC -!- MISCELLANEOUS: The antigen encoded by the PAG64 clone, normally
CC expressed only on lymphocyte subsets and thymocytes, is found in
CC increased concentrations in all transformed cells tested, in an
CC embryonic carcinoma cell line, and in pluripotent embryonic cells.
CC Activation of the gene appears to be a general feature of
CC carcinogenesis in the mouse. The PAG64 clone, and related cDNA clones,
CC have in common a repetitive sequence in their 3' transcription units
CC that has characteristics of a transposable element.
CC -!- MISCELLANEOUS: [Isoform 2]: Exon 7 is missing. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR EMBL; X00246; CAA25061.1; -; mRNA.
DR PIR; A93322; HLMS1.
DR AlphaFoldDB; P01895; -.
DR SMR; P01895; -.
DR iPTMnet; P01895; -.
DR PhosphoSitePlus; P01895; -.
DR jPOST; P01895; -.
DR MaxQB; P01895; -.
DR PeptideAtlas; P01895; -.
DR PRIDE; P01895; -.
DR ProteomicsDB; 270925; -. [P01895-1]
DR ProteomicsDB; 270926; -. [P01895-2]
DR MGI; MGI:95896; H2-D1.
DR ChiTaRS; H2-D1; mouse.
DR Proteomes; UP000000589; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0033106; C:cis-Golgi network membrane; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005797; C:Golgi medial cisterna; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0042824; C:MHC class I peptide loading complex; ISO:MGI.
DR GO; GO:0042612; C:MHC class I protein complex; ISO:MGI.
DR GO; GO:0032398; C:MHC class Ib protein complex; ISO:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0071889; F:14-3-3 protein binding; ISO:MGI.
DR GO; GO:0030881; F:beta-2-microglobulin binding; ISO:MGI.
DR GO; GO:0042610; F:CD8 receptor binding; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042288; F:MHC class I protein binding; ISO:MGI.
DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; ISO:MGI.
DR GO; GO:0042605; F:peptide antigen binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0042608; F:T cell receptor binding; ISO:MGI.
DR GO; GO:0046977; F:TAP binding; ISO:MGI.
DR GO; GO:0062061; F:TAP complex binding; ISO:MGI.
DR GO; GO:0046978; F:TAP1 binding; ISO:MGI.
DR GO; GO:0046979; F:TAP2 binding; ISO:MGI.
DR GO; GO:0002485; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent; IDA:MGI.
DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:MGI.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:MGI.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 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; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR001039; MHC_I_a_a1/a2.
DR InterPro; IPR010579; MHC_I_a_C.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR Pfam; PF06623; MHC_I_C; 1.
DR PRINTS; PR01638; MHCCLASSI.
DR SMART; SM00407; IGc1; 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 Alternative splicing; Disulfide bond; Glycoprotein; Immunity; Membrane;
KW MHC I; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..298
FT /note="H-2 class I histocompatibility antigen, alpha chain"
FT /id="PRO_0000080742"
FT TOPO_DOM <1..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 142..230
FT /note="Ig-like C1-type"
FT REGION 277..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 160..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 286..298
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003228"
FT VARIANT 212
FT /note="Q -> L (in clone PH-2D-1)"
FT VARIANT 223
FT /note="Missing (in clone PH-2D-1)"
FT VARIANT 285
FT /note="V -> G (in clone PH-2D-1)"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT NON_TER 1
SQ SEQUENCE 298 AA; 33850 MW; 7F9CE29A053B06FB CRC64;
RYEPRARWIE QEGPEYWERE TRRAKGNEQS FRVDLRTALR YYNQSAGGSH TLQWMAGCDV
ESDGRLLRGY WQFAYDGCDY IALNEDLKTW TAADMAAQIT RRKWEQAGAA ERDRAYLEGE
CVEWLRRYLK NGNATLLRTD PPKAHVTHHR RPEGDVTLRC WALGFYPADI TLTWQLNGEE
LTQEMELVET RPAGDGTFQK WASVVVPLGK EQKYTCHVEH EGLPEPLTLR WGKEEPPSST
KTNTVIIAVP VVLGAVVILG AVMAFVMKRR RNTGGKGGDY ALAPVSQSSD MSLPDCKV
