ID HA1L_MOUSE Reviewed; 362 AA. AC P01897; Q31195; Q31196; Q31197; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 191. DE RecName: Full=H-2 class I histocompatibility antigen, L-D alpha chain; DE Flags: Precursor; GN Name=H2-L; 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=1705528; DOI=10.1016/0378-1119(91)90054-f; RA Joly E., Oldstone M.B.; RT "Generation of a functional cDNA encoding the LdH2 class-I molecule by RT using a single-LTR retroviral shuttle vector."; RL Gene 97:213-221(1991). RN [2] RP NUCLEOTIDE SEQUENCE (CLONE 27.5). RC STRAIN=BALB/cJ; TISSUE=Sperm; RX PubMed=7058332; DOI=10.1126/science.7058332; RA Moore K.W., Sher B.T., Sun Y.H., Eakle K.A., Hood L.E.; RT "DNA sequence of a gene encoding a BALB/c mouse Ld transplantation RT antigen."; RL Science 215:679-682(1982). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BALB/cJ; TISSUE=Sperm; RX PubMed=6604582; DOI=10.1016/0092-8674(83)90386-0; RA Zuniga M.C., Malissen B., McMillan M., Brayton P.R., Clark S.S., Forman J., RA Hood L.E.; RT "Expression and function of transplantation antigens with altered or RT deleted cytoplasmic domains."; RL Cell 34:535-544(1983). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-311 AND 339-348. RX PubMed=6952248; DOI=10.1073/pnas.79.6.1994; RA Evans G.A., Margulies D.H., Camerini-Otero R.D., Ozato K., Seidman J.G.; RT "Structure and expression of a mouse major histocompatibility antigen gene, RT H-2Ld."; RL Proc. Natl. Acad. Sci. U.S.A. 79:1994-1998(1982). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 205-362 (CLONE PH-2D-3). 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 [6] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-293. RX PubMed=9192660; DOI=10.1073/pnas.94.13.6880; RA Balendiran G.K., Solheim J.C., Young A.C., Hansen T.H., Nathenson S.G., RA Sacchettini J.C.; RT "The three-dimensional structure of an H-2Ld-peptide complex explains the RT unique interaction of Ld with beta-2 microglobulin and peptide."; RL Proc. Natl. Acad. Sci. U.S.A. 94:6880-6885(1997). 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 -!- SEQUENCE CAUTION: CC Sequence=CAA24126.1; Type=Erroneous initiation; Evidence={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; M33151; AAA39659.1; -; mRNA. DR EMBL; V00749; CAA24126.1; ALT_INIT; Genomic_DNA. DR EMBL; V00750; CAA24127.1; -; Genomic_DNA. DR EMBL; V00751; CAA24128.1; -; Genomic_DNA. DR EMBL; V00752; CAA24129.1; ALT_SEQ; Genomic_DNA. DR EMBL; L00129; AAA39662.1; -; Genomic_DNA. DR EMBL; J00394; AAA39578.1; -; mRNA. DR EMBL; L00128; AAA39661.1; -; Genomic_DNA. DR EMBL; L00127; AAA39661.1; JOINED; Genomic_DNA. DR PIR; B60854; B60854. DR PIR; C60854; C60854. DR PIR; I54069; HLMSLD. DR PDB; 1LD9; X-ray; 2.40 A; A/D=25-292. DR PDB; 1LDP; X-ray; 3.10 A; H=25-296. DR PDB; 2E7L; X-ray; 2.50 A; E/F=25-205. DR PDB; 2OI9; X-ray; 2.35 A; A=25-203. DR PDB; 3E2H; X-ray; 3.80 A; A=25-199. DR PDB; 3E3Q; X-ray; 2.95 A; A/B/H/L/P/U/Y/c=25-199. DR PDB; 3ERY; X-ray; 1.95 A; A/B=25-198. DR PDB; 3TF7; X-ray; 2.75 A; A/E=25-203. DR PDB; 3TFK; X-ray; 2.75 A; A=25-203. DR PDB; 3TJH; X-ray; 2.12 A; A=25-203. DR PDB; 3TPU; X-ray; 3.10 A; E/I/K/Q=25-203. DR PDB; 3UO1; X-ray; 1.64 A; P=70-78. DR PDB; 3UYR; X-ray; 1.70 A; P=70-77. DR PDB; 3V4U; X-ray; 1.64 A; P=70-78. DR PDB; 3V52; X-ray; 1.70 A; P=70-77. DR PDB; 3VJ6; X-ray; 1.90 A; P=3-11. DR PDB; 4MS8; X-ray; 1.92 A; A=25-203. DR PDB; 4MVB; X-ray; 3.09 A; C=25-203. DR PDB; 4MXQ; X-ray; 2.60 A; A=25-203. DR PDB; 4N0C; X-ray; 2.90 A; A/E=25-203. DR PDB; 4N5E; X-ray; 3.06 A; A=25-203. DR PDB; 4NHU; X-ray; 2.90 A; E/G=25-204. DR PDB; 5VCL; X-ray; 2.05 A; P=3-11. DR PDB; 6L9K; X-ray; 1.80 A; A=25-199. DR PDB; 6L9L; X-ray; 2.40 A; A/E=25-199. DR PDB; 6L9M; X-ray; 2.60 A; A/D/G/J=24-301. DR PDB; 6L9N; X-ray; 2.60 A; A/D/G/J=24-301. DR PDB; 8D5N; X-ray; 1.80 A; A/C=25-298. DR PDB; 8D5Q; X-ray; 2.50 A; C=25-203. DR PDBsum; 1LD9; -. DR PDBsum; 1LDP; -. DR PDBsum; 2E7L; -. DR PDBsum; 2OI9; -. DR PDBsum; 3E2H; -. DR PDBsum; 3E3Q; -. DR PDBsum; 3ERY; -. DR PDBsum; 3TF7; -. DR PDBsum; 3TFK; -. DR PDBsum; 3TJH; -. DR PDBsum; 3TPU; -. DR PDBsum; 3UO1; -. DR PDBsum; 3UYR; -. DR PDBsum; 3V4U; -. DR PDBsum; 3V52; -. DR PDBsum; 3VJ6; -. DR PDBsum; 4MS8; -. DR PDBsum; 4MVB; -. DR PDBsum; 4MXQ; -. DR PDBsum; 4N0C; -. DR PDBsum; 4N5E; -. DR PDBsum; 4NHU; -. DR PDBsum; 5VCL; -. DR PDBsum; 6L9K; -. DR PDBsum; 6L9L; -. DR PDBsum; 6L9M; -. DR PDBsum; 6L9N; -. DR PDBsum; 8D5N; -. DR PDBsum; 8D5Q; -. DR AlphaFoldDB; P01897; -. DR SMR; P01897; -. DR IntAct; P01897; 1. DR MINT; P01897; -. DR GlyCosmos; P01897; 3 sites, No reported glycans. DR GlyGen; P01897; 3 sites. DR iPTMnet; P01897; -. DR PhosphoSitePlus; P01897; -. DR SwissPalm; P01897; -. DR jPOST; P01897; -. DR MaxQB; P01897; -. DR PeptideAtlas; P01897; -. DR ProteomicsDB; 271382; -. DR Pumba; P01897; -. DR ABCD; P01897; 2 sequenced antibodies. DR AGR; MGI:95912; -. DR MGI; MGI:95912; H2-L. DR InParanoid; P01897; -. DR EvolutionaryTrace; P01897; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P01897; Protein. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. 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:0030881; F:beta-2-microglobulin 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:0051087; F:protein-folding chaperone binding; 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:0002250; P:adaptive immune response; ISO:MGI. DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI. DR GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IBA:GO_Central. DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; ISO:MGI. DR GO; GO:0002477; P:antigen processing and presentation of exogenous peptide antigen via MHC class Ib; ISO:MGI. DR GO; GO:0036037; P:CD8-positive, alpha-beta T cell activation; ISO:MGI. DR GO; GO:0006952; P:defense response; TAS:MGI. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0002519; P:natural killer cell tolerance induction; ISO:MGI. DR GO; GO:0032815; P:negative regulation of natural killer cell activation; ISO:MGI. DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; ISO:MGI. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI. DR GO; GO:0001815; P:positive regulation of antibody-dependent cellular cytotoxicity; ISO:MGI. DR GO; GO:2001187; P:positive regulation of CD8-positive, alpha-beta T cell activation; ISO:MGI. DR GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; ISO:MGI. DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:MGI. DR GO; GO:0032736; P:positive regulation of interleukin-13 production; ISO:MGI. DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISO:MGI. DR GO; GO:0032816; P:positive regulation of natural killer cell activation; ISO:MGI. DR GO; GO:0002729; P:positive regulation of natural killer cell cytokine production; ISO:MGI. DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:MGI. DR GO; GO:0002717; P:positive regulation of natural killer cell mediated immunity; ISO:MGI. DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; ISO:MGI. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISO:MGI. DR GO; GO:0032759; P:positive regulation of TRAIL production; ISO:MGI. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI. DR GO; GO:0042270; P:protection from natural killer cell mediated cytotoxicity; ISO:MGI. DR GO; GO:0002715; P:regulation of natural killer cell mediated immunity; ISO:MGI. DR CDD; cd21018; IgC1_MHC_Ia_H2Db_H2Ld; 1. DR CDD; cd12087; TM_EGFR-like; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 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 PANTHER; PTHR16675:SF242; CLASS IB MHC ANTIGEN QA-2-RELATED; 1. DR PANTHER; PTHR16675; MHC CLASS I-RELATED; 1. 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; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycoprotein; Immunity; Membrane; MHC I; KW Phosphoprotein; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..24 FT CHAIN 25..362 FT /note="H-2 class I histocompatibility antigen, L-D alpha FT chain" FT /id="PRO_0000018932" 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" 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 CARBOHYD 200 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 280 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000305" FT DISULFID 125..188 FT DISULFID 227..283 FT CONFLICT 17..24 FT /note="LAPTQTRA -> WPDSDPR (in Ref. 2, 3 and 4)" FT /evidence="ECO:0000305" FT CONFLICT 35 FT /note="Missing (in Ref. 2 and 3)" FT /evidence="ECO:0000305" FT CONFLICT 145 FT /note="C -> R (in Ref. 2, 3 and 4)" FT /evidence="ECO:0000305" FT CONFLICT 220 FT /note="K -> E (in Ref. 5)" FT /evidence="ECO:0000305" FT CONFLICT 292 FT /note="E -> H (in Ref. 4; CAA24129/AAA39661)" FT /evidence="ECO:0000305" FT CONFLICT 303 FT /note="S -> F (in Ref. 5)" FT /evidence="ECO:0000305" FT STRAND 27..38 FT /evidence="ECO:0007829|PDB:6L9K" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:8D5N" FT STRAND 45..52 FT /evidence="ECO:0007829|PDB:6L9K" FT STRAND 55..61 FT /evidence="ECO:0007829|PDB:6L9K" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:6L9K" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:6L9K" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:3V4U" FT HELIX 81..108 FT /evidence="ECO:0007829|PDB:6L9K" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:3ERY" FT STRAND 117..127 FT /evidence="ECO:0007829|PDB:6L9K" FT STRAND 131..142 FT /evidence="ECO:0007829|PDB:6L9K" FT STRAND 145..150 FT /evidence="ECO:0007829|PDB:6L9K" FT TURN 152..155 FT /evidence="ECO:0007829|PDB:1LD9" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:6L9K" FT HELIX 162..174 FT /evidence="ECO:0007829|PDB:6L9K" FT HELIX 176..185 FT /evidence="ECO:0007829|PDB:6L9K" FT HELIX 187..198 FT /evidence="ECO:0007829|PDB:6L9K" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:8D5N" FT STRAND 210..217 FT /evidence="ECO:0007829|PDB:8D5N" FT TURN 219..221 FT /evidence="ECO:0007829|PDB:1LD9" FT STRAND 223..235 FT /evidence="ECO:0007829|PDB:8D5N" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:8D5N" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:6L9M" FT TURN 249..251 FT /evidence="ECO:0007829|PDB:1LDP" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:8D5N" FT STRAND 265..273 FT /evidence="ECO:0007829|PDB:8D5N" FT TURN 275..277 FT /evidence="ECO:0007829|PDB:1LDP" FT HELIX 278..280 FT /evidence="ECO:0007829|PDB:8D5N" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:8D5N" FT STRAND 288..290 FT /evidence="ECO:0007829|PDB:1LD9" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:8D5N" SQ SEQUENCE 362 AA; 40711 MW; A5EFDEE31177BF22 CRC64; MGAMAPRTLL LLLAAALAPT QTRAGPHSMR YFETAVSRPG LGEPRYISVG YVDNKEFVRF DSDAENPRYE PQAPWMEQEG PEYWERITQI AKGQEQWFRV NLRTLLGYYN QSAGGTHTLQ WMYGCDVGSD GRLLRGYEQF AYDGCDYIAL NEDLKTWTAA DMAAQITRRK WEQAGAAEYY RAYLEGECVE WLHRYLKNGN ATLLRTDSPK AHVTHHPRSK GEVTLRCWAL GFYPADITLT WQLNGEELTQ DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCRVYHEGL PEPLTLRWEP PPSTDSYMVI VAVLGVLGAM AIIGAVVAFV MKRRRNTGGK GGDYALAPGS QSSEMSLRDC KA //