CD1D_SHEEP
ID CD1D_SHEEP Reviewed; 335 AA.
AC O62848;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Antigen-presenting glycoprotein CD1d;
DE AltName: CD_antigen=CD1d;
DE Flags: Precursor;
GN Name=CD1D;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9914336; DOI=10.1007/s002510050483;
RA Rhind S.M., Hopkins J., Dutia B.M.;
RT "Amino-terminal sequencing of sheep CD1 antigens and identification of a
RT sheep CD1D gene.";
RL Immunogenetics 49:225-230(1999).
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; AJ006722; CAA07200.1; -; mRNA.
DR RefSeq; NP_001116473.1; NM_001123001.1.
DR AlphaFoldDB; O62848; -.
DR SMR; O62848; -.
DR STRING; 9940.ENSOARP00000007771; -.
DR PRIDE; O62848; -.
DR GeneID; 100144424; -.
DR KEGG; oas:100144424; -.
DR CTD; 912; -.
DR eggNOG; ENOG502SJH6; Eukaryota.
DR OrthoDB; 827472at2759; -.
DR Proteomes; UP000002356; Unplaced.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..335
FT /note="Antigen-presenting glycoprotein CD1d"
FT /id="PRO_0000014598"
FT TOPO_DOM 18..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 185..295
FT /note="Ig-like"
FT MOTIF 331..334
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 169..172
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250|UniProtKB:P15813"
FT BINDING 169
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250"
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 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 224..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 335 AA; 38469 MW; 78199F7FF2E420C8 CRC64;
MGCLLFLVLL EFQKIWGSFE APQTSFPFRF LQISSFANHS WTRTDGLMWL GELQPYTWRN
ESSTIRFLKH WSQGTFSDQQ WEQLQHTFQV YRSSFTRDIR EFVKMLPGDY PFEIQISGGC
ELLPRNISES FLRAALQEKD VLSFQGMSWV SAPDAPPWSQ VVCKVLNEDQ GTKETVHWLL
HDICPELVKG LMQTGKSELE KQVKPEAWLS SGPSPGPDRL LLGCHVSGFY PKPVWVMWMR
GEQEEPGTQQ GDVMPNADST WYLRVTLEVA AGEAAGLSCR VKHSSLGDQD IILYWDGKRV
SRGLIVVLVI LVFVLLFVGG LVFWFRKHRR YQDIS
