HA12_MOUSE
ID HA12_MOUSE Reviewed; 365 AA.
AC P01900;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=H-2 class I histocompatibility antigen, D-D alpha chain;
DE Short=H-2D(D);
DE Flags: Precursor;
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 [GENOMIC DNA].
RX PubMed=6571712;
RA Margulies D.H., Evans G.A., Ozato K., Camerini-Otero R.D., Tanaka K.,
RA Appella E., Seidman J.G.;
RT "Expression of H-2Dd and H-2Ld mouse major histocompatibility antigen genes
RT in L cells after DNA-mediated gene transfer.";
RL J. Immunol. 130:463-470(1983).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=3925012;
RA Margulies D.H., Evans G.A., Ozato K., Camerini-Otero R.D., Tanaka K.,
RA Appella E., Seidman J.G.;
RT "Partial nucleotide sequence of H-2Dd major histocompatibility antigen
RT gene.";
RL J. Immunol. 135:1537-1537(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3856254; DOI=10.1073/pnas.82.4.1175;
RA Sher B.T., Nairn R., Coligan J.E., Hood L.E.;
RT "DNA sequence of the mouse H-2Dd transplantation antigen gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1175-1179(1985).
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 25-125.
RX PubMed=7295646; DOI=10.1021/bi00519a033;
RA Nairn R., Nathenson S.G., Coligan J.E.;
RT "Amino acid sequence of cyanogen bromide fragment CN-C (residues 24-98) of
RT the mouse histocompatibility antigen H-2Dd. A comparison of the amino-
RT terminal 100 residues of H-2Dd, Dd, Kd, and Kb reveals discrete areas of
RT diversity.";
RL Biochemistry 20:4739-4745(1981).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-359, AND
RP IDENTIFICATION BY 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, 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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9729040; DOI=10.1016/s1074-7613(00)80602-0;
RA Achour A., Persson K., Harris R.A., Sundbaeck J., Sentman C.L.,
RA Lindqvist Y., Schneider G., Kaerre K.;
RT "The crystal structure of H-2Dd MHC class I complexed with the HIV-1-
RT derived peptide P18-I10 at 2.4-A resolution: implications for T cell and NK
RT cell recognition.";
RL Immunity 9:199-208(1998).
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; L29190; AAA39581.1; -; Genomic_DNA.
DR EMBL; U47326; AAB17604.1; -; mRNA.
DR PDB; 1BII; X-ray; 2.40 A; A=1-365.
DR PDB; 1DDH; X-ray; 3.10 A; A=26-298.
DR PDB; 1QO3; X-ray; 2.30 A; A=26-301.
DR PDB; 3DMM; X-ray; 2.60 A; A=26-299.
DR PDB; 3E6F; X-ray; 2.41 A; A=26-298.
DR PDB; 3E6H; X-ray; 2.10 A; A=26-299.
DR PDB; 3ECB; X-ray; 1.70 A; A=26-301.
DR PDB; 5IVX; X-ray; 2.10 A; A=26-301.
DR PDB; 5KD4; X-ray; 3.05 A; A/C=26-301.
DR PDB; 5KD7; X-ray; 2.35 A; A/C/F/I=26-300.
DR PDB; 5T7G; X-ray; 1.96 A; A/C=26-300.
DR PDB; 5WER; X-ray; 3.41 A; A/D/G/J=26-301.
DR PDB; 5WES; X-ray; 2.71 A; A=26-301.
DR PDB; 5WET; X-ray; 2.64 A; A=26-301.
DR PDB; 5WEU; X-ray; 1.58 A; A=26-301.
DR PDB; 6NPR; X-ray; 2.37 A; A/C=26-301.
DR PDBsum; 1BII; -.
DR PDBsum; 1DDH; -.
DR PDBsum; 1QO3; -.
DR PDBsum; 3DMM; -.
DR PDBsum; 3E6F; -.
DR PDBsum; 3E6H; -.
DR PDBsum; 3ECB; -.
DR PDBsum; 5IVX; -.
DR PDBsum; 5KD4; -.
DR PDBsum; 5KD7; -.
DR PDBsum; 5T7G; -.
DR PDBsum; 5WER; -.
DR PDBsum; 5WES; -.
DR PDBsum; 5WET; -.
DR PDBsum; 5WEU; -.
DR PDBsum; 6NPR; -.
DR AlphaFoldDB; P01900; -.
DR SMR; P01900; -.
DR DIP; DIP-6110N; -.
DR MINT; P01900; -.
DR iPTMnet; P01900; -.
DR PhosphoSitePlus; P01900; -.
DR SwissPalm; P01900; -.
DR EPD; P01900; -.
DR jPOST; P01900; -.
DR MaxQB; P01900; -.
DR PeptideAtlas; P01900; -.
DR PRIDE; P01900; -.
DR ProteomicsDB; 269797; -.
DR MGI; MGI:95896; H2-D1.
DR ChiTaRS; H2-D1; mouse.
DR EvolutionaryTrace; P01900; -.
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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunity; Membrane; MHC I; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:7295646"
FT CHAIN 25..365
FT /note="H-2 class I histocompatibility antigen, D-D alpha
FT chain"
FT /id="PRO_0000018924"
FT TOPO_DOM 25..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 209..297
FT /note="Ig-like C1-type"
FT REGION 25..114
FT /note="Alpha-1"
FT REGION 115..206
FT /note="Alpha-2"
FT REGION 207..298
FT /note="Alpha-3"
FT REGION 299..311
FT /note="Connecting peptide"
FT REGION 343..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 227..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3E6H"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5WEU"
FT HELIX 81..109
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5IVX"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3E6H"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5WEU"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:5WEU"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:5WEU"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:5WEU"
FT TURN 199..204
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 221..235
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:5WEU"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:3ECB"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:5WEU"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:5WEU"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3E6H"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:5WEU"
SQ SEQUENCE 365 AA; 41110 MW; D127F5A4F0E79513 CRC64;
MGAMAPRTLL LLLAAALGPT QTRAGSHSLR YFVTAVSRPG FGEPRYMEVG YVDNTEFVRF
DSDAENPRYE PRARWIEQEG PEYWERETRR AKGNEQSFRV DLRTALRYYN QSAGGSHTLQ
WMAGCDVESD GRLLRGYWQF AYDGCDYIAL NEDLKTWTAA DMAAQITRRK WEQAGAAERD
RAYLEGECVE WLRRYLKNGN ATLLRTDPPK AHVTHHRRPE GDVTLRCWAL GFYPADITLT
WQLNGEELTQ EMELVETRPA GDGTFQKWAS VVVPLGKEQK YTCHVEHEGL PEPLTLRWGK
EEPPSSTKTN TVIIAVPVVL GAVVILGAVM AFVMKRRRNT GGKGGDYALA PGSQSSDMSL
PDCKV
