HA1Q_MOUSE
ID HA1Q_MOUSE Reviewed; 328 AA.
AC P14428;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=H-2 class I histocompatibility antigen, K-Q alpha chain;
DE Short=H-2K(Q);
DE Flags: Fragment;
GN Name=H2-K1; Synonyms=H2-K;
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=3838967; DOI=10.1007/bf00430802;
RA Morita T., Delarbre C., Kress M., Kourilsky P., Gachelin G.;
RT "An H-2K gene of the tw32 mutant at the T/t complex is a close parent of an
RT H-2Kq gene.";
RL Immunogenetics 21:367-383(1985).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, 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 -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR EMBL; M14827; AAA39656.1; -; mRNA.
DR PIR; I54414; I54414.
DR AlphaFoldDB; P14428; -.
DR SMR; P14428; -.
DR iPTMnet; P14428; -.
DR jPOST; P14428; -.
DR MaxQB; P14428; -.
DR PeptideAtlas; P14428; -.
DR PRIDE; P14428; -.
DR ProteomicsDB; 269801; -.
DR MGI; MGI:95904; H2-K1.
DR ChiTaRS; H2-K1; 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; ISO: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; IDA: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:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IDA:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IDA:MGI.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
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 Disulfide bond; Glycoprotein; Immunity; Membrane; MHC I; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN <1..328
FT /note="H-2 class I histocompatibility antigen, K-Q alpha
FT chain"
FT /id="PRO_0000080741"
FT TOPO_DOM <1..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 166..252
FT /note="Ig-like C1-type"
FT REGION <1..71
FT /note="Alpha-1"
FT REGION 72..163
FT /note="Alpha-2"
FT REGION 164..255
FT /note="Alpha-3"
FT REGION 256..265
FT /note="Connecting peptide"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01900"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 184..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
SQ SEQUENCE 328 AA; 36856 MW; ADFF1BD811BC37B4 CRC64;
PRFISVGYVD DTELVRFDSD AENPRYEPRA RWMEQVEPEY WERNTQIAKD NEQSSRVDLR
TLLRYYNQSA GGSHTIQRMY GCDVGSDGRL LRGYEQVAYD GCDYIALNED LKTWTAADMA
ALITKHKWEQ AGAAERRRAY LEGACVEWLS RHLKNGNATL LRTDSPKAHV THHSRPEDKV
TLRCWALGFY PADITLTWQL NGEELTQDME LVETRPAGDG TFQKWASVVV PLGKEQYYTC
HVYHQGLPKP LTLRWEPPPS AVSNTVIIAV LVVLGAAIVT GAVVAFVMMR RRNTGGKGGD
YALAPGSQTS DLSLPDCKVM VHDPHSLA
