HA1L_MOUSE
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 25-MAY-2022, entry version 184.
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};
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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 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 AlphaFoldDB; P01897; -.
DR SMR; P01897; -.
DR IntAct; P01897; 1.
DR MINT; P01897; -.
DR GlyGen; P01897; 3 sites.
DR iPTMnet; P01897; -.
DR PhosphoSitePlus; P01897; -.
DR SwissPalm; P01897; -.
DR jPOST; P01897; -.
DR MaxQB; P01897; -.
DR PeptideAtlas; P01897; -.
DR PRIDE; P01897; -.
DR ProteomicsDB; 271382; -.
DR ABCD; P01897; 2 sequenced antibodies.
DR MGI; MGI:95912; H2-L.
DR InParanoid; P01897; -.
DR EvolutionaryTrace; P01897; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01897; protein.
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:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; TAS:MGI.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
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; 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 STRAND 39..42
FT /evidence="ECO:0007829|PDB:3ERY"
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 201..204
FT /evidence="ECO:0007829|PDB:1LD9"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1LD9"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1LD9"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1LD9"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1LD9"
FT STRAND 238..247
FT /evidence="ECO:0007829|PDB:1LD9"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1LDP"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1LD9"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:1LD9"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1LDP"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6L9M"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:1LD9"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1LD9"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:6L9M"
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
