HA11_MOUSE
ID HA11_MOUSE Reviewed; 362 AA.
AC P01899;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=H-2 class I histocompatibility antigen, D-B alpha chain;
DE Short=H-2D(B);
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].
RC STRAIN=C3H/HeJ;
RX PubMed=3680952;
RA Watts S., Vogel J.M., Harriman W.D., Itoh T., Stauss H.J., Goodenow R.S.;
RT "DNA sequence analysis of the C3H H-2Kk and H-2Dk loci. Evolutionary
RT relationships to H-2 genes from four other mouse strains.";
RL J. Immunol. 139:3878-3885(1987).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/10;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-362.
RX PubMed=7118211; DOI=10.1007/bf00364437;
RA Reyes A.A., Schold M., Wallace R.B.;
RT "The complete amino acid sequence of the murine transplantation antigen H-
RT 2Db as deduced by molecular cloning.";
RL Immunogenetics 16:1-9(1982).
RN [5]
RP PROTEIN SEQUENCE OF 25-122.
RX PubMed=7225204; DOI=10.1016/s0021-9258(19)69694-8;
RA Maloy W.L., Nathenson S.G., Coligan J.E.;
RT "Primary structure of murine major histocompatibility complex alloantigens.
RT Amino acid sequence of the NH2-terminal ninety-eight residues of the H-2Db
RT glycoprotein.";
RL J. Biol. Chem. 256:2863-2872(1981).
RN [6]
RP PROTEIN SEQUENCE OF 253-308 AND 332-358.
RX PubMed=7118212; DOI=10.1007/bf00364438;
RA Maloy W.L., Coligan J.E.;
RT "Primary structure of the H-2Db alloantigen. II. Additional amino acid
RT sequence information, localization of a third site of glycosylation and
RT evidence for K and D region specific sequences.";
RL Immunogenetics 16:11-22(1982).
RN [7]
RP GLYCOSYLATION AT ASN-110 AND ASN-280.
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 [8]
RP UBIQUITINATION, INTERACTION WITH MURID HERPESVIRUS 4 K3, AND MUTAGENESIS OF
RP LYS-55; LYS-92; LYS-155; LYS-170; LYS-197; LYS-210; LYS-220; LYS-267;
RP LYS-277; LYS-332; THR-337; LYS-340; 350-SER--SER-356 AND 360-CYS-LYS-361.
RX PubMed=17502423; DOI=10.1083/jcb.200611063;
RA Wang X., Herr R.A., Chua W.J., Lybarger L., Wiertz E.J., Hansen T.H.;
RT "Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic
RT tail can induce ERAD of MHC-I by viral E3 ligase mK3.";
RL J. Cell Biol. 177:613-624(2007).
RN [9]
RP UBIQUITINATION AT SER-353, INTERACTION WITH MURID HERPESVIRUS 4 K3, AND
RP MUTAGENESIS OF LYS-332; THR-337; LYS-340; 350-SER--SER-352; SER-356 AND
RP 360-CYS-LYS-361.
RX PubMed=19951915; DOI=10.1083/jcb.200908036;
RA Wang X., Herr R.A., Rabelink M., Hoeben R.C., Wiertz E.J., Hansen T.H.;
RT "Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation
RT substrates.";
RL J. Cell Biol. 187:655-668(2009).
RN [10]
RP UBIQUITINATION, INTERACTION WITH MURID HERPESVIRUS 4 K3, AND MUTAGENESIS OF
RP LYS-332; THR-337; LYS-340; 350-SER--SER-352; SER-356 AND 360-CYS-LYS-361.
RX PubMed=19531064; DOI=10.1111/j.1600-0854.2009.00946.x;
RA Herr R.A., Harris J., Fang S., Wang X., Hansen T.H.;
RT "Role of the RING-CH domain of viral ligase mK3 in ubiquitination of non-
RT lysine and lysine MHC I residues.";
RL Traffic 10:1301-1317(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-296.
RX PubMed=7506996; DOI=10.1016/0092-8674(94)90171-6;
RA Young A.C.M., Zhang W., Sacchettini J.C., Nathenson S.G.;
RT "The three-dimensional structure of H-2Db at 2.4-A resolution: implications
RT for antigen-determinant selection.";
RL Cell 76:39-50(1994).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 24-304, AND DISULFIDE BONDS.
RX PubMed=10993729; DOI=10.1006/jmbi.2000.4501;
RA Tissot A.C., Ciatto C., Mittl P.R., Grutter M.G., Pluckthun A.;
RT "Viral escape at the molecular level explained by quantitative T-cell
RT receptor/peptide/MHC interactions and the crystal structure of a
RT peptide/MHC complex.";
RL J. Mol. Biol. 302:873-885(2000).
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). Interacts with murid herpesvirus 4 protein K3 (mK3).
CC {ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064,
CC ECO:0000269|PubMed:19951915}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- PTM: Polyubiquitinated in case of infection by murid herpesvirus 4, by
CC the viral E3 ligase K3 (mK3). This modification causes the protein to
CC be targeted for rapid degradation by the endoplasmic reticulum-
CC associated degradation (ERAD) system. Ubiquitination occurs on lysine,
CC as well as serine and threonine residues present in the cytoplasmic
CC tail. Serine and threonine residues are subject to ubiquitination via
CC ester bonds instead of the usual isopeptide linkage.
CC {ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064,
CC ECO:0000269|PubMed:19951915}.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39580.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M18523; AAA53200.1; -; Genomic_DNA.
DR EMBL; L36068; AAA89206.1; -; mRNA.
DR EMBL; U47325; AAB17603.1; -; mRNA.
DR EMBL; K00129; AAA39580.1; ALT_INIT; mRNA.
DR CCDS; CCDS57074.1; -.
DR PIR; B60854; B60854.
DR PIR; I56002; HLMSDB.
DR RefSeq; NP_034510.3; NM_010380.3.
DR PDB; 1BZ9; X-ray; 2.80 A; A=26-299.
DR PDB; 1CE6; X-ray; 2.90 A; A=25-298.
DR PDB; 1FFN; X-ray; 2.70 A; A/D=26-298.
DR PDB; 1FFO; X-ray; 2.65 A; A/D=26-298.
DR PDB; 1FFP; X-ray; 2.60 A; A/D=26-298.
DR PDB; 1FG2; X-ray; 2.75 A; A/D/G/J=25-304.
DR PDB; 1HOC; X-ray; 2.40 A; A=25-296.
DR PDB; 1INQ; X-ray; 2.20 A; A=25-299.
DR PDB; 1JPF; X-ray; 2.18 A; A=25-304.
DR PDB; 1JPG; X-ray; 2.20 A; A=25-304.
DR PDB; 1JUF; X-ray; 2.00 A; A=25-299.
DR PDB; 1N3N; X-ray; 3.00 A; A/C/E/G=25-304.
DR PDB; 1N5A; X-ray; 2.85 A; A/D/G/J=25-300.
DR PDB; 1QLF; X-ray; 2.65 A; A=25-300.
DR PDB; 1S7U; X-ray; 2.20 A; A/D/G/J=25-362.
DR PDB; 1S7V; X-ray; 2.20 A; A/D=25-362.
DR PDB; 1S7W; X-ray; 2.40 A; A/D/G/J=25-362.
DR PDB; 1S7X; X-ray; 2.41 A; A/D/G/J=25-362.
DR PDB; 1WBX; X-ray; 1.90 A; A=25-300.
DR PDB; 1WBY; X-ray; 2.30 A; A=25-300.
DR PDB; 1YN6; X-ray; 2.20 A; A=26-298.
DR PDB; 1YN7; X-ray; 2.20 A; A=26-298.
DR PDB; 1ZHB; X-ray; 2.70 A; A/D/G/J=25-300.
DR PDB; 2CII; X-ray; 2.55 A; A=25-299.
DR PDB; 2F74; X-ray; 2.70 A; A/D=25-300.
DR PDB; 2VE6; X-ray; 2.65 A; A/D/G/J=25-301.
DR PDB; 2ZOK; X-ray; 2.10 A; A/C/E/G=25-299.
DR PDB; 2ZOL; X-ray; 2.70 A; A/C=25-299.
DR PDB; 3BUY; X-ray; 2.60 A; A=26-300.
DR PDB; 3CC5; X-ray; 1.91 A; A/D=25-300.
DR PDB; 3CCH; X-ray; 2.60 A; A/D/G/J=25-300.
DR PDB; 3CH1; X-ray; 2.30 A; A/D/G/J=25-300.
DR PDB; 3CPL; X-ray; 2.50 A; A/C=25-299.
DR PDB; 3FTG; X-ray; 2.60 A; A=25-304.
DR PDB; 3L3H; X-ray; 2.70 A; A=26-300.
DR PDB; 3PQY; X-ray; 3.19 A; A/F/K/P=26-300.
DR PDB; 3QUK; X-ray; 2.41 A; A/D=25-362.
DR PDB; 3QUL; X-ray; 2.00 A; A/D/G/J=25-362.
DR PDB; 3TBS; X-ray; 2.49 A; A/D=25-362.
DR PDB; 3TBT; X-ray; 2.30 A; A/D/G/J=25-362.
DR PDB; 3TBV; X-ray; 2.10 A; A/C/E/G=25-362.
DR PDB; 3TBW; X-ray; 2.15 A; A/C/E/G=25-362.
DR PDB; 3TBY; X-ray; 2.50 A; A/D/G/J=25-362.
DR PDB; 3WS3; X-ray; 2.34 A; A/C=26-298.
DR PDB; 3WS6; X-ray; 1.98 A; A/B=26-300.
DR PDB; 4HUU; X-ray; 2.00 A; A/D=25-304.
DR PDB; 4HUV; X-ray; 2.50 A; A/D=25-304.
DR PDB; 4HUW; X-ray; 3.16 A; A/C/E/G=25-304.
DR PDB; 4HUX; X-ray; 2.20 A; A=25-304.
DR PDB; 4HV8; X-ray; 2.00 A; A/C=25-304.
DR PDB; 4IHO; X-ray; 2.80 A; A/D=25-300.
DR PDB; 4L8B; X-ray; 2.20 A; A=25-304.
DR PDB; 4L8C; X-ray; 2.80 A; A/C/E/G=25-304.
DR PDB; 4L8D; X-ray; 1.90 A; A/C=25-304.
DR PDB; 4NSK; X-ray; 2.60 A; A=25-300.
DR PDB; 4PG2; X-ray; 2.80 A; A=25-299.
DR PDB; 5E8N; X-ray; 2.25 A; A/D/G/J=25-300.
DR PDB; 5E8O; X-ray; 1.98 A; A/D=25-300.
DR PDB; 5E8P; X-ray; 2.00 A; A/D=25-300.
DR PDB; 5JWD; X-ray; 2.50 A; A=25-298.
DR PDB; 5JWE; X-ray; 2.40 A; A/C/E/G=25-300.
DR PDB; 5M00; X-ray; 1.95 A; A=25-300.
DR PDB; 5M01; X-ray; 1.95 A; A=25-300.
DR PDB; 5M02; X-ray; 1.75 A; A=25-300.
DR PDB; 5MZM; X-ray; 2.40 A; A/D=25-300.
DR PDB; 5OPI; X-ray; 3.30 A; A=25-300.
DR PDB; 5SWS; X-ray; 2.86 A; A=25-304.
DR PDB; 5SWZ; X-ray; 2.65 A; A/F/K/P=25-304.
DR PDB; 5TIL; X-ray; 2.83 A; A/D=25-300.
DR PDB; 5TJE; X-ray; 3.20 A; A/C=25-300.
DR PDB; 5WLG; X-ray; 2.10 A; A/F=25-302.
DR PDB; 5WLI; X-ray; 2.20 A; A/D/G/J=25-302.
DR PDB; 6G9Q; X-ray; 1.89 A; A=25-300.
DR PDB; 6G9R; X-ray; 2.70 A; A/C/E/G=25-300.
DR PDB; 6GB5; X-ray; 2.30 A; A/C=25-362.
DR PDB; 6GB7; X-ray; 2.15 A; A/C/E/G=25-362.
DR PDB; 6H6D; X-ray; 2.40 A; A/D=25-362.
DR PDB; 6MP0; X-ray; 2.00 A; A=25-300.
DR PDB; 6MP1; X-ray; 2.21 A; A=25-300.
DR PDB; 6WZY; X-ray; 1.50 A; A=25-302.
DR PDB; 6X00; X-ray; 1.55 A; A=25-304.
DR PDB; 7JWI; X-ray; 3.02 A; A=1-362.
DR PDB; 7JWJ; X-ray; 3.25 A; A=1-362.
DR PDB; 7P0A; X-ray; 2.43 A; A/D=25-300.
DR PDB; 7P0T; X-ray; 2.60 A; A/D=25-300.
DR PDBsum; 1BZ9; -.
DR PDBsum; 1CE6; -.
DR PDBsum; 1FFN; -.
DR PDBsum; 1FFO; -.
DR PDBsum; 1FFP; -.
DR PDBsum; 1FG2; -.
DR PDBsum; 1HOC; -.
DR PDBsum; 1INQ; -.
DR PDBsum; 1JPF; -.
DR PDBsum; 1JPG; -.
DR PDBsum; 1JUF; -.
DR PDBsum; 1N3N; -.
DR PDBsum; 1N5A; -.
DR PDBsum; 1QLF; -.
DR PDBsum; 1S7U; -.
DR PDBsum; 1S7V; -.
DR PDBsum; 1S7W; -.
DR PDBsum; 1S7X; -.
DR PDBsum; 1WBX; -.
DR PDBsum; 1WBY; -.
DR PDBsum; 1YN6; -.
DR PDBsum; 1YN7; -.
DR PDBsum; 1ZHB; -.
DR PDBsum; 2CII; -.
DR PDBsum; 2F74; -.
DR PDBsum; 2VE6; -.
DR PDBsum; 2ZOK; -.
DR PDBsum; 2ZOL; -.
DR PDBsum; 3BUY; -.
DR PDBsum; 3CC5; -.
DR PDBsum; 3CCH; -.
DR PDBsum; 3CH1; -.
DR PDBsum; 3CPL; -.
DR PDBsum; 3FTG; -.
DR PDBsum; 3L3H; -.
DR PDBsum; 3PQY; -.
DR PDBsum; 3QUK; -.
DR PDBsum; 3QUL; -.
DR PDBsum; 3TBS; -.
DR PDBsum; 3TBT; -.
DR PDBsum; 3TBV; -.
DR PDBsum; 3TBW; -.
DR PDBsum; 3TBY; -.
DR PDBsum; 3WS3; -.
DR PDBsum; 3WS6; -.
DR PDBsum; 4HUU; -.
DR PDBsum; 4HUV; -.
DR PDBsum; 4HUW; -.
DR PDBsum; 4HUX; -.
DR PDBsum; 4HV8; -.
DR PDBsum; 4IHO; -.
DR PDBsum; 4L8B; -.
DR PDBsum; 4L8C; -.
DR PDBsum; 4L8D; -.
DR PDBsum; 4NSK; -.
DR PDBsum; 4PG2; -.
DR PDBsum; 5E8N; -.
DR PDBsum; 5E8O; -.
DR PDBsum; 5E8P; -.
DR PDBsum; 5JWD; -.
DR PDBsum; 5JWE; -.
DR PDBsum; 5M00; -.
DR PDBsum; 5M01; -.
DR PDBsum; 5M02; -.
DR PDBsum; 5MZM; -.
DR PDBsum; 5OPI; -.
DR PDBsum; 5SWS; -.
DR PDBsum; 5SWZ; -.
DR PDBsum; 5TIL; -.
DR PDBsum; 5TJE; -.
DR PDBsum; 5WLG; -.
DR PDBsum; 5WLI; -.
DR PDBsum; 6G9Q; -.
DR PDBsum; 6G9R; -.
DR PDBsum; 6GB5; -.
DR PDBsum; 6GB7; -.
DR PDBsum; 6H6D; -.
DR PDBsum; 6MP0; -.
DR PDBsum; 6MP1; -.
DR PDBsum; 6WZY; -.
DR PDBsum; 6X00; -.
DR PDBsum; 7JWI; -.
DR PDBsum; 7JWJ; -.
DR PDBsum; 7P0A; -.
DR PDBsum; 7P0T; -.
DR AlphaFoldDB; P01899; -.
DR SMR; P01899; -.
DR BioGRID; 200150; 5.
DR DIP; DIP-6121N; -.
DR MINT; P01899; -.
DR STRING; 10090.ENSMUSP00000134570; -.
DR iPTMnet; P01899; -.
DR PhosphoSitePlus; P01899; -.
DR SwissPalm; P01899; -.
DR EPD; P01899; -.
DR jPOST; P01899; -.
DR PaxDb; P01899; -.
DR PRIDE; P01899; -.
DR ProteomicsDB; 270921; -.
DR DNASU; 14964; -.
DR Ensembl; ENSMUST00000172785; ENSMUSP00000134570; ENSMUSG00000073411.
DR GeneID; 14964; -.
DR KEGG; mmu:14964; -.
DR UCSC; uc008chg.1; mouse.
DR CTD; 14964; -.
DR MGI; MGI:95896; H2-D1.
DR VEuPathDB; HostDB:ENSMUSG00000073411; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR GeneTree; ENSGT00980000198488; -.
DR HOGENOM; CLU_047501_1_1_1; -.
DR OMA; WDGEKER; -.
DR OrthoDB; 1390181at2759; -.
DR PhylomeDB; P01899; -.
DR TreeFam; TF336617; -.
DR BioGRID-ORCS; 14964; 6 hits in 79 CRISPR screens.
DR ChiTaRS; H2-D1; mouse.
DR EvolutionaryTrace; P01899; -.
DR Proteomes; UP000000589; Chromosome 17.
DR Bgee; ENSMUSG00000073411; Expressed in peripheral lymph node and 257 other tissues.
DR ExpressionAtlas; P01899; baseline and differential.
DR Genevisible; P01899; MM.
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; Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:7225204"
FT CHAIN 25..362
FT /note="H-2 class I histocompatibility antigen, D-B alpha
FT chain"
FT /id="PRO_0000018923"
FT TOPO_DOM 25..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..362
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..309
FT /note="Connecting peptide"
FT REGION 340..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 353
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01900"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01900"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3980466,
FT ECO:0000269|PubMed:7118212"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3980466"
FT DISULFID 125..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:10993729"
FT DISULFID 227..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:10993729"
FT CROSSLNK 353
FT /note="Glycyl serine ester (Ser-Gly) (interchain with G-
FT Cter in ubiquitin); alternate"
FT /evidence="ECO:0000305|PubMed:19951915"
FT MUTAGEN 55
FT /note="K->R: In K-less, no effect on ubiquitination; when
FT associated with R-92, R-155, R-170, R-197, R-210, R-220, R-
FT 267 and R-277."
FT /evidence="ECO:0000269|PubMed:17502423"
FT MUTAGEN 92
FT /note="K->R: In K-less, no effect on ubiquitination; when
FT associated with R-55, R-155, R-170, R-197, R-210, R-220, R-
FT 267 and R-277."
FT /evidence="ECO:0000269|PubMed:17502423"
FT MUTAGEN 155
FT /note="K->R: In K-less, no effect on ubiquitination; when
FT associated with R-55, R-92, R-170, R-197, R-210, R-220, R-
FT 267 and R-277."
FT /evidence="ECO:0000269|PubMed:17502423"
FT MUTAGEN 170
FT /note="K->R: In K-less, no effect on ubiquitination; when
FT associated with R-55, R-92, R-155, R-197, R-210, R-220, R-
FT 267 and R-277."
FT /evidence="ECO:0000269|PubMed:17502423"
FT MUTAGEN 197
FT /note="K->R: In K-less, no effect on ubiquitination; when
FT associated with R-55, R-92, R-155, R-170, R-210, R-220, R-
FT 267 and R-277."
FT /evidence="ECO:0000269|PubMed:17502423"
FT MUTAGEN 210
FT /note="K->R: In K-less, no effect on ubiquitination; when
FT associated with R-55, R-92, R-155, R-170, R-197, R-220, R-
FT 267 and R-277."
FT /evidence="ECO:0000269|PubMed:17502423"
FT MUTAGEN 220
FT /note="K->R: In K-less, no effect on ubiquitination; when
FT associated with R-55, R-92, R-155, R-170, R-197, R-210, R-
FT 267 and R-277."
FT /evidence="ECO:0000269|PubMed:17502423"
FT MUTAGEN 267
FT /note="K->R: In K-less, no effect on ubiquitination; when
FT associated with R-55, R-92, R-155, R-170, R-197, R-210, R-
FT 220 and R-277."
FT /evidence="ECO:0000269|PubMed:17502423"
FT MUTAGEN 277
FT /note="K->R: In K-less, no effect on ubiquitination; when
FT associated with R-55, R-92, R-155, R-170, R-197, R-210, R-
FT 220 and R-267."
FT /evidence="ECO:0000269|PubMed:17502423"
FT MUTAGEN 332
FT /note="K->R: In Ld KCST-less, strongly impairs
FT ubiquitination; when associated with I-337; R-340; 350-A--
FT A-356 and 360-R-R-361. In Ld tail 1S, restores
FT ubiquitination; when associated I-337; R-340; 350-A--A-352;
FT A-356 and 360-R-R-361."
FT /evidence="ECO:0000269|PubMed:17502423,
FT ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915"
FT MUTAGEN 337
FT /note="T->I: In Ld KCST-less, strongly impairs
FT ubiquitination; when associated with R-332; R-340; 350-A--
FT A-356 and 360-R-R-361. In Ld tail 1S, restores
FT ubiquitination; when associated R-332; R-340; 350-A--A-352;
FT A-356 and 360-R-R-361."
FT /evidence="ECO:0000269|PubMed:17502423,
FT ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915"
FT MUTAGEN 340
FT /note="K->R: In Ld KCST-less, strongly impairs
FT ubiquitination; when associated with R-332; I-337; 350-A--
FT A-356 and 360-R-R-361. In Ld tail 1S, restores
FT ubiquitination; when associated R-332; I-337; 350-A--A-352;
FT A-356 and 360-R-R-361."
FT /evidence="ECO:0000269|PubMed:17502423,
FT ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915"
FT MUTAGEN 350..356
FT /note="SQSSEMS->AQGAEMA: In Ld KCST-less, strongly impairs
FT ubiquitination; when associated with R-332; I-337 and 360-
FT R-R-361."
FT /evidence="ECO:0000269|PubMed:17502423"
FT MUTAGEN 350..352
FT /note="SQS->AQG: In Ld tail 1S, restores ubiquitination;
FT when associated R-332; I-337; R-340; A-356 and 360-R-R-
FT 361."
FT /evidence="ECO:0000269|PubMed:19531064,
FT ECO:0000269|PubMed:19951915"
FT MUTAGEN 356
FT /note="S->A: In Ld tail 1S, restores ubiquitination; when
FT associated R-332; I-337; R-340 and A-356."
FT /evidence="ECO:0000269|PubMed:19531064,
FT ECO:0000269|PubMed:19951915"
FT MUTAGEN 360..361
FT /note="CK->RR: In Ld KCST-less, strongly impairs
FT ubiquitination; when associated with R-332; I-337; R-340
FT and 350-A--A-356. In Ld tail 1S, restores ubiquitination;
FT when associated R-332; I-337; R-340; 350-A--A-352; A-356
FT and 360-R-R-361."
FT /evidence="ECO:0000269|PubMed:17502423,
FT ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:6WZY"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:6WZY"
FT HELIX 81..108
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6G9Q"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 131..142
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1BZ9"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:6WZY"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:6WZY"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:6WZY"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:6WZY"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:5M01"
FT STRAND 222..235
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3CC5"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1YN6"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:5M02"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:6WZY"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6WZY"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:6WZY"
SQ SEQUENCE 362 AA; 40836 MW; 6EE6AEF97263FA71 CRC64;
MGAMAPRTLL LLLAAALAPT QTRAGPHSMR YFETAVSRPG LEEPRYISVG YVDNKEFVRF
DSDAENPRYE PRAPWMEQEG PEYWERETQK AKGQEQWFRV SLRNLLGYYN QSAGGSHTLQ
QMSGCDLGSD WRLLRGYLQF AYEGRDYIAL NEDLKTWTAA DMAAQITRRK WEQSGAAEHY
KAYLEGECVE WLHRYLKNGN ATLLRTDSPK AHVTHHPRSK GEVTLRCWAL GFYPADITLT
WQLNGEELTQ DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCRVYHEGL PEPLTLRWEP
PPSTDSYMVI VAVLGVLGAM AIIGAVVAFV MKRRRNTGGK GGDYALAPGS QSSEMSLRDC
KA
