CD1D_SYLFL
ID CD1D_SYLFL Reviewed; 275 AA.
AC P23043;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Antigen-presenting glycoprotein CD1d;
DE AltName: Full=Leukocyte differentiation-like antigen Ta;
DE AltName: CD_antigen=CD1d;
DE Flags: Fragment;
GN Name=CD1D; Synonyms=CD1;
OS Sylvilagus floridanus (Cottontail rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Sylvilagus.
OX NCBI_TaxID=9988;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2478462; DOI=10.1007/bf02425277;
RA Calabi F., Belt K.T., Yu C.Y., Bradbury A., Mandy W.J., Milstein C.;
RT "The rabbit CD1 and the evolutionary conservation of the CD1 gene family.";
RL Immunogenetics 30:370-377(1989).
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. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts with
CC MHC II and CD74 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15813};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P15813}.
CC Basolateral cell membrane {ECO:0000250|UniProtKB:P15813}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:P15813}. Endosome
CC membrane {ECO:0000250|UniProtKB:P15813}; Single-pass type I membrane
CC protein {ECO:0000250|UniProtKB:P15813}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P15813}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P15813}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P15813}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P15813}. Note=Subject to intracellular
CC trafficking between the cell membrane, endosomes and lysosomes.
CC {ECO:0000250|UniProtKB:P15813}.
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; M26249; AAA31197.1; -; Genomic_DNA.
DR AlphaFoldDB; P23043; -.
DR SMR; P23043; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0030882; F:lipid antigen binding; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Immunity; Immunoglobulin domain; Innate immunity; Lysosome;
KW Membrane.
FT CHAIN <1..>275
FT /note="Antigen-presenting glycoprotein CD1d"
FT /id="PRO_0000072671"
FT DOMAIN 164..274
FT /note="Ig-like"
FT BINDING 77
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250|UniProtKB:P15813"
FT BINDING 148..151
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250|UniProtKB:P15813"
FT BINDING 148
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 203..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
FT NON_TER 275
SQ SEQUENCE 275 AA; 31047 MW; 8E7232CD5C0C31F4 CRC64;
LQRSFPFHGL QISSFVNSSQ TRTDCLAWLG ELQTHSWSND SDTIHFLKPW SQGTFNFQQW
EQVQNELWVY RLSVTRDIHD FVKLLKLTYP IELQVFAGCE MHPGNTSESF FHVAYQGMHV
LSFRGTLWET APGTPPFVKL VVKELNLDHG TREMIQELLN NTCPQFVSGL IEAGRSELEK
QVKPEAWLSS GPSPGPGRLL LVCRVSGFYP KPVQVMWMRG DQEQPHTRQG DFLPNADGTW
YLRVTLDVAA GDAAGLSCRV KHSSLGGQDI YPVLG
