CD1D2_MOUSE
ID CD1D2_MOUSE Reviewed; 336 AA.
AC P11610;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Antigen-presenting glycoprotein CD1d2;
DE AltName: CD_antigen=CD1d.2;
DE Flags: Precursor;
GN Name=Cd1d2; Synonyms=Cd1.2;
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=1702817;
RA Balk S.P., Bleicher P.A., Terhorst C.;
RT "Isolation and expression of cDNA encoding the murine homologues of CD1.";
RL J. Immunol. 146:768-774(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-297.
RC TISSUE=Thymus;
RX PubMed=2460336; DOI=10.1002/j.1460-2075.1988.tb03173.x;
RA Bradbury A., Belt K.T., Neri T.M., Milstein C., Calabi F.;
RT "Mouse CD1 is distinct from and co-exists with TL in the same thymus.";
RL EMBO J. 7:3081-3086(1988).
CC -!- FUNCTION: Antigen-presenting protein that binds self and non-self
CC glycolipids and presents them to T-cell receptors on natural killer T-
CC cells.
CC -!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts with
CC MHC II and CD74.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11609};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11609}.
CC Endosome membrane {ECO:0000250|UniProtKB:P11609}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P11609}. Note=Subject to intracellular
CC trafficking between the cell membrane, endosomes and lysosomes.
CC {ECO:0000250|UniProtKB:P11609}.
CC -!- TISSUE SPECIFICITY: Expressed on cortical thymocytes, on certain T-cell
CC leukemias, and in various other tissues.
CC -!- MISCELLANEOUS: During protein synthesis and maturation, CD1 family
CC members bind endogenous lipids that are replaced by lipid or glycolipid
CC antigens when the proteins are internalized and pass through endosomes,
CC before trafficking back to the cell surface. {ECO:0000250}.
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DR EMBL; M63697; AAA37392.1; -; mRNA.
DR EMBL; X15036; CAA33141.1; -; Genomic_DNA.
DR PIR; I49582; I49582.
DR PIR; S01298; S01298.
DR RefSeq; NP_031666.2; NM_007640.2.
DR PDB; 6BMH; X-ray; 2.30 A; A/C/E/G=22-297.
DR PDB; 6BMK; X-ray; 2.43 A; A/C=22-297.
DR PDBsum; 6BMH; -.
DR PDBsum; 6BMK; -.
DR AlphaFoldDB; P11610; -.
DR SMR; P11610; -.
DR STRING; 10090.ENSMUSP00000039583; -.
DR ChEMBL; CHEMBL4523997; -.
DR GlyGen; P11610; 5 sites.
DR PhosphoSitePlus; P11610; -.
DR jPOST; P11610; -.
DR MaxQB; P11610; -.
DR PaxDb; P11610; -.
DR PRIDE; P11610; -.
DR ProteomicsDB; 281262; -.
DR DNASU; 12480; -.
DR GeneID; 12480; -.
DR KEGG; mmu:12480; -.
DR CTD; 12480; -.
DR MGI; MGI:107675; Cd1d2.
DR eggNOG; ENOG502SJH6; Eukaryota.
DR InParanoid; P11610; -.
DR PhylomeDB; P11610; -.
DR BioGRID-ORCS; 12480; 0 hits in 53 CRISPR screens.
DR PRO; PR:P11610; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P11610; protein.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030883; F:endogenous lipid antigen binding; IBA:GO_Central.
DR GO; GO:0030884; F:exogenous lipid antigen binding; IBA:GO_Central.
DR GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central.
DR GO; GO:0048006; P:antigen processing and presentation, endogenous lipid antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IDA:MGI.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:MGI.
DR GO; GO:0051135; P:positive regulation of NK T cell activation; IDA:MGI.
DR GO; GO:0001916; P:positive regulation of 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; 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 Pfam; PF07654; C1-set; 1.
DR Pfam; PF16497; MHC_I_3; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Endosome; Glycoprotein;
KW Immunity; Immunoglobulin domain; Innate immunity; Lysosome; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..336
FT /note="Antigen-presenting glycoprotein CD1d2"
FT /id="PRO_0000014592"
FT TOPO_DOM 22..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 207..297
FT /note="Ig-like"
FT MOTIF 332..335
FT /note="Internalization signal"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250|UniProtKB:P15813"
FT BINDING 171..174
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250|UniProtKB:P15813"
FT BINDING 171
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 226..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 64
FT /note="T -> I (in Ref. 2; CAA33141)"
FT /evidence="ECO:0000305"
FT STRAND 26..38
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6BMH"
FT TURN 70..75
FT /evidence="ECO:0007829|PDB:6BMH"
FT HELIX 78..106
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 114..125
FT /evidence="ECO:0007829|PDB:6BMH"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 129..147
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:6BMH"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6BMH"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:6BMH"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:6BMH"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:6BMH"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 221..234
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:6BMH"
FT TURN 273..278
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:6BMH"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:6BMH"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:6BMH"
SQ SEQUENCE 336 AA; 38477 MW; BC25978B2E5BAB8C CRC64;
MRYLPCLLLW AFLQVWGQSE VQQKNYTFRC LQTSSFANIS WSRTDSLILL GDLQTHRWSN
DSATISFTKP WSQGKLSNQQ WEKLQHMFQV YRVSFTRDIQ ELVKMMSPKE DYPIEIQLST
GCEMYPGNAS ESFFHVAFQG KYAVRFRGTS WQRVLGAPSW LDLPIKVLNA DQGTSATVQT
LLNDTWPQFA RGLLEAGKSD LEKQEKPVAW LSSVPSSAHG HLQLVCHVSG FYPKPVWVMW
MRGDQEQQGT HRGDFLPNAD ETWYLQATLD VEAGEEAGLA CRVKHSSLGG QDIILYWDAR
QAPVGLIVFI VLIMLVVVGA VVYYIWRRRS AYQDIR
