CD1D_RAT
ID CD1D_RAT Reviewed; 336 AA.
AC Q63493;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Antigen-presenting glycoprotein CD1d;
DE AltName: CD_antigen=CD1d;
DE Flags: Precursor;
GN Name=Cd1d; Synonyms=Cd1d1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
RX PubMed=7517972;
RA Ichimiya S., Kikuchi K., Matsuura A.;
RT "Structural analysis of the rat homologue of CD1. Evidence for evolutionary
RT conservation of the CD1D class and widespread transcription by rat cells.";
RL J. Immunol. 153:1112-1123(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
RX PubMed=9601940; DOI=10.1007/s002510050396;
RA Katabami S., Matsuura A., Chen H., Imai K., Kikuchi K.;
RT "Structural organization of rat CD1 typifies evolutionarily conserved CD1D
RT class genes.";
RL Immunogenetics 48:22-31(1998).
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 -!- 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; D26439; BAA05455.2; -; mRNA.
DR PIR; I56235; I56235.
DR RefSeq; NP_058775.1; NM_017079.1.
DR AlphaFoldDB; Q63493; -.
DR SMR; Q63493; -.
DR STRING; 10116.ENSRNOP00000022150; -.
DR GlyGen; Q63493; 5 sites.
DR iPTMnet; Q63493; -.
DR PhosphoSitePlus; Q63493; -.
DR PaxDb; Q63493; -.
DR GeneID; 25109; -.
DR KEGG; rno:25109; -.
DR UCSC; RGD:2296; rat.
DR CTD; 12479; -.
DR RGD; 2296; Cd1d1.
DR eggNOG; ENOG502SJH6; Eukaryota.
DR InParanoid; Q63493; -.
DR OrthoDB; 827472at2759; -.
DR PhylomeDB; Q63493; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR PRO; PR:Q63493; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
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:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR GO; GO:0030883; F:endogenous lipid antigen binding; ISO:RGD.
DR GO; GO:0030884; F:exogenous lipid antigen binding; ISO:RGD.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0030882; F:lipid antigen binding; ISS:UniProtKB.
DR GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central.
DR GO; GO:0042608; F:T cell receptor binding; ISO:RGD.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR GO; GO:0048006; P:antigen processing and presentation, endogenous lipid antigen via MHC class Ib; ISO:RGD.
DR GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001865; P:NK T cell differentiation; ISO:RGD.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISO:RGD.
DR GO; GO:0043032; P:positive regulation of macrophage activation; ISO:RGD.
DR GO; GO:0051135; P:positive regulation of NK T cell activation; ISO:RGD.
DR GO; GO:0051138; P:positive regulation of NK T cell differentiation; ISO:RGD.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0045059; P:positive thymic T cell selection; ISO:RGD.
DR GO; GO:0033084; P:regulation of immature T cell proliferation in thymus; ISO:RGD.
DR GO; GO:0050776; P:regulation of immune response; ISO:RGD.
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..336
FT /note="Antigen-presenting glycoprotein CD1d"
FT /id="PRO_0000014595"
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..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 198..296
FT /note="Ig-like"
FT MOTIF 332..335
FT /note="Internalization signal"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250|UniProtKB:P15813"
FT BINDING 170..173
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250|UniProtKB:P15813"
FT BINDING 170
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 225..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 336 AA; 38542 MW; D794B944A7800B62 CRC64;
MLYLPCLLLW AFPQFWGQSE VQQNYTFGCL QISSFANRSW SRTDSVVWLG DLQTHRWSND
SDTISFTKPW SQGKFSNQQW EKLQHMFQVY RTSFTRDIKE IVKMMSPKED YPIEVQLSAG
CEMYPGNASE SFLHVAFQGE YVVRFHGTSW QKVPEAPSWL DLPIKMLNAD EGTRETVQIL
LNDTCPQFVR GLLEAGKPDL EKQEKPVAWL SRGPNPAHGH LQLVCHVSGF HPKPVWVMWM
RGDQEQGGTH RGDILPNADE TWYLQATLDV EAGDEAGLAC RVKHSSLEGQ DIILYWGGRQ
VSPVLIFLIV GVLVLVVCAV AYYIIRKRRR SYQDIM
