HA1D_MOUSE
ID HA1D_MOUSE Reviewed; 368 AA.
AC P01902;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=H-2 class I histocompatibility antigen, K-D alpha chain;
DE Short=H-2K(D);
DE Flags: Precursor;
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=11894934; DOI=10.1002/j.1460-2075.1983.tb01413.x;
RA Kvist S., Roberts L., Dobberstein B.;
RT "Mouse histocompatibility genes: structure and organisation of a Kd gene.";
RL EMBO J. 2:245-254(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=6298749; DOI=10.1093/nar/11.5.1567;
RA Lalanne J.-L., Delarbre C., Gachelin G., Kourilsky P.;
RT "A cDNA clone containing the entire coding sequence of a mouse H-2Kd
RT histocompatibility antigen.";
RL Nucleic Acids Res. 11:1567-1577(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NOD/LT;
RA Girgis K.R., Capra D.J., Stroynowski I.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=9869916;
RA Wang M., Stepkowski S.M., Hebert J.S., Tian L., Yu J., Kahan B.D.;
RT "Nucleotide sequences of three H-2K and three H-2D complementary DNA clones
RT coding mouse class I MHC heavy chain proteins.";
RL Ann. Transplant. 1:26-31(1996).
RN [5]
RP PROTEIN SEQUENCE OF 22-119.
RX PubMed=7018573; DOI=10.1021/bi00514a049;
RA Kimball E.S., Nathenson S.G., Coligan J.E.;
RT "Amino acid sequence of residues 1-98 of the K-2Kb murine major
RT histocompatibility alloantigen: comparison with H-2Kb and H-2db reveals
RT extensive localized differences.";
RL Biochemistry 20:3301-3308(1981).
RN [6]
RP GLYCOSYLATION AT ASN-107 AND ASN-277.
RX PubMed=3980466; DOI=10.1016/s0021-9258(18)89229-8;
RA Swiedler S.J., Freed J.H., Tarentino A.L., Plummer T.H. Jr., Hart G.W.;
RT "Oligosaccharide microheterogeneity of the murine major histocompatibility
RT antigens. Reproducible site-specific patterns of sialylation and branching
RT in asparagine-linked oligosaccharides.";
RL J. Biol. Chem. 260:4046-4054(1985).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-353, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J00402; AAA39652.1; -; mRNA.
DR EMBL; L36065; AAA89205.1; -; mRNA.
DR EMBL; U47329; AAB17607.1; -; mRNA.
DR PIR; A90977; HLMSKD.
DR PDB; 1VGK; X-ray; 2.06 A; A=22-295.
DR PDB; 2FWO; X-ray; 2.60 A; A=22-304.
DR PDB; 3NWM; X-ray; 2.70 A; A=22-295.
DR PDB; 4WDI; X-ray; 2.31 A; A/D=22-296.
DR PDB; 4Z76; X-ray; 1.88 A; A/D=22-296.
DR PDB; 4Z77; X-ray; 1.85 A; A/D=22-296.
DR PDB; 4Z78; X-ray; 2.30 A; A/D/G=22-296.
DR PDB; 5GR7; X-ray; 2.40 A; A=22-295.
DR PDB; 5GSB; X-ray; 1.80 A; A=22-295.
DR PDB; 5GSR; X-ray; 2.20 A; A/C=22-295.
DR PDB; 5GSV; X-ray; 2.00 A; A=22-295.
DR PDB; 5GSX; X-ray; 2.50 A; A/D=22-295.
DR PDB; 5TRZ; X-ray; 2.25 A; A/C=23-297.
DR PDB; 5TS1; X-ray; 2.30 A; A/C/E/G=23-297.
DR PDBsum; 1VGK; -.
DR PDBsum; 2FWO; -.
DR PDBsum; 3NWM; -.
DR PDBsum; 4WDI; -.
DR PDBsum; 4Z76; -.
DR PDBsum; 4Z77; -.
DR PDBsum; 4Z78; -.
DR PDBsum; 5GR7; -.
DR PDBsum; 5GSB; -.
DR PDBsum; 5GSR; -.
DR PDBsum; 5GSV; -.
DR PDBsum; 5GSX; -.
DR PDBsum; 5TRZ; -.
DR PDBsum; 5TS1; -.
DR AlphaFoldDB; P01902; -.
DR SMR; P01902; -.
DR IntAct; P01902; 1.
DR iPTMnet; P01902; -.
DR PhosphoSitePlus; P01902; -.
DR EPD; P01902; -.
DR jPOST; P01902; -.
DR MaxQB; P01902; -.
DR PRIDE; P01902; -.
DR ProteomicsDB; 271381; -.
DR MGI; MGI:95904; H2-K1.
DR ChiTaRS; H2-K1; mouse.
DR EvolutionaryTrace; P01902; -.
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 Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunity; Membrane; MHC I; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:7018573"
FT CHAIN 22..368
FT /note="H-2 class I histocompatibility antigen, K-D alpha
FT chain"
FT /id="PRO_0000018929"
FT TOPO_DOM 22..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 206..294
FT /note="Ig-like C1-type"
FT REGION 22..111
FT /note="Alpha-1"
FT REGION 112..203
FT /note="Alpha-2"
FT REGION 204..295
FT /note="Alpha-3"
FT REGION 296..305
FT /note="Connecting peptide"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3980466,
FT ECO:0000269|PubMed:6298749"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:6298749"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3980466"
FT DISULFID 122..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 224..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 135
FT /note="Q -> H (in Ref. 2; AAA39652)"
FT /evidence="ECO:0000305"
FT STRAND 24..35
FT /evidence="ECO:0007829|PDB:5GSB"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 39..49
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:5GSB"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:5GSB"
FT HELIX 78..105
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3NWM"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:5GSB"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:5GSB"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:5GSB"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:5GSB"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:4Z77"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 216..232
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5GSV"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4Z77"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5GSV"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:5GSB"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:5GSB"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:4Z76"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:5GSB"
SQ SEQUENCE 368 AA; 41490 MW; 4C83897CBCF7C6E5 CRC64;
MAPCTLLLLL AAALAPTQTR AGPHSLRYFV TAVSRPGLGE PRFIAVGYVD DTQFVRFDSD
ADNPRFEPRA PWMEQEGPEY WEEQTQRAKS DEQWFRVSLR TAQRYYNQSK GGSHTFQRMF
GCDVGSDWRL LRGYQQFAYD GRDYIALNED LKTWTAADTA ALITRRKWEQ AGDAEYYRAY
LEGECVEWLR RYLELGNETL LRTDSPKAHV TYHPRSQVDV TLRCWALGFY PADITLTWQL
NGEDLTQDME LVETRPAGDG TFQKWAAVVV PLGKEQNYTC HVHHKGLPEP LTLRWKLPPS
TVSNTVIIAV LVVLGAAIVT GAVVAFVMKM RRNTGGKGVN YALAPGSQTS DLSLPDGKVM
VHDPHSLA
