ID CD1D1_MOUSE Reviewed; 336 AA. AC P11609; Q91XK9; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 3. DT 08-NOV-2023, entry version 203. DE RecName: Full=Antigen-presenting glycoprotein CD1d1; DE AltName: CD_antigen=CD1d.1; DE Flags: Precursor; GN Name=Cd1d1; Synonyms=Cd1.1; 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 [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] 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). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CD74, AND GLYCOSYLATION. RX PubMed=11754812; DOI=10.1016/s1074-7613(01)00240-0; RA Jayawardena-Wolf J., Benlagha K., Chiu Y.-H., Mehr R., Bendelac A.; RT "CD1d endosomal trafficking is independently regulated by an intrinsic RT CD1d-encoded tyrosine motif and by the invariant chain."; RL Immunity 15:897-908(2001). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Liver, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) OF 25-297 IN COMPLEX WITH B2M, AND RP DISULFIDE BONDS. RX PubMed=9219685; DOI=10.1126/science.277.5324.339; RA Zeng Z., Castano A.R., Segelke B.W., Stura E.A., Peterson P.A., RA Wilson I.A.; RT "Crystal structure of mouse CD1: an MHC-like fold with a large hydrophobic RT binding groove."; RL Science 277:339-345(1997). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-297 IN COMPLEX WITH B2M AND RP CIS-TETRACOSENOYL SULFATIDE, FUNCTION, AND GLYCOSYLATION. RX PubMed=16314439; DOI=10.1084/jem.20051625; RA Zajonc D.M., Maricic I., Wu D., Halder R., Roy K., Wong C.-H., Kumar V., RA Wilson I.A.; RT "Structural basis for CD1d presentation of a sulfatide derived from myelin RT and its implications for autoimmunity."; RL J. Exp. Med. 202:1517-1526(2005). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-297 IN COMPLEX WITH RP PHOSPHATIDYLCHOLINE AND B2M, GLYCOSYLATION AT ASN-38; ASN-60 AND ASN-183, RP AND DISULFIDE BONDS. RX PubMed=16002697; DOI=10.4049/jimmunol.175.2.977; RA Giabbai B., Sidobre S., Crispin M.D.M., Sanchez-Ruiz Y., Bachi A., RA Kronenberg M., Wilson I.A., Degano M.; RT "Crystal structure of mouse CD1d bound to the self ligand RT phosphatidylcholine: a molecular basis for NKT cell activation."; RL J. Immunol. 175:977-984(2005). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-297 IN COMPLEX WITH RP GALACTOSYLCERAMIDE AND B2M, FUNCTION, GLYCOSYLATION AT ASN-38; ASN-60 AND RP ASN-183, AND DISULFIDE BONDS. RX PubMed=16007091; DOI=10.1038/ni1224; RA Zajonc D.M., Cantu C. III, Mattner J., Zhou D., Savage P.B., Bendelac A., RA Wilson I.A., Teyton L.; RT "Structure and function of a potent agonist for the semi-invariant natural RT killer T cell receptor."; RL Nat. Immunol. 6:810-818(2005). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-297 IN COMPLEX WITH RP GLYCOSPHINGOLIPID AND B2M, GLYCOSYLATION AT ASN-38; ASN-60 AND ASN-183, AND RP DISULFIDE BONDS. RX PubMed=16537470; DOI=10.1073/pnas.0600285103; RA Wu D., Zajonc D.M., Fujio M., Sullivan B.A., Kinjo Y., Kronenberg M., RA Wilson I.A., Wong C.-H.; RT "Design of natural killer T cell activators: structure and function of a RT microbial glycosphingolipid bound to mouse CD1d."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3972-3977(2006). 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:0000269|PubMed:11754812, ECO:0000269|PubMed:16007091, CC ECO:0000269|PubMed:16314439}. CC -!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts with CC MHC II and CD74. {ECO:0000269|PubMed:11754812, CC ECO:0000269|PubMed:16002697, ECO:0000269|PubMed:16007091, CC ECO:0000269|PubMed:16314439, ECO:0000269|PubMed:16537470, CC ECO:0000269|PubMed:9219685}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11754812}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:11754812}. CC Endosome membrane {ECO:0000269|PubMed:11754812}. Lysosome membrane CC {ECO:0000269|PubMed:11754812}. Note=Subject to intracellular CC trafficking between the cell membrane, endosomes and lysosomes. CC {ECO:0000269|PubMed:11754812}. CC -!- TISSUE SPECIFICITY: Expressed on cortical thymocytes, on certain T-cell CC leukemias, and in various other tissues. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11754812, CC ECO:0000269|PubMed:16002697, ECO:0000269|PubMed:16007091, CC ECO:0000269|PubMed:16314439, ECO:0000269|PubMed:16537470}. 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. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=CD1d1; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_TCRant_00004"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M63695; AAA37391.1; -; mRNA. DR EMBL; AK002582; BAB22206.1; -; mRNA. DR EMBL; X13170; CAA31568.1; -; Genomic_DNA. DR CCDS; CCDS17449.1; -. DR PIR; I49581; I49581. DR PIR; S01297; S01297. DR RefSeq; NP_031665.2; NM_007639.3. DR PDB; 1CD1; X-ray; 2.67 A; A/C=22-336. DR PDB; 1Z5L; X-ray; 2.20 A; A/C=19-297. DR PDB; 1ZHN; X-ray; 2.80 A; A=25-297. DR PDB; 2AKR; X-ray; 1.90 A; A/C=19-297. DR PDB; 2FIK; X-ray; 1.80 A; A=19-297. DR PDB; 2GAZ; X-ray; 2.61 A; A=19-297. DR PDB; 2Q7Y; X-ray; 1.95 A; A/C=19-297. DR PDB; 3ARB; X-ray; 2.70 A; A=19-297. DR PDB; 3ARD; X-ray; 3.01 A; A=19-297. DR PDB; 3ARE; X-ray; 2.80 A; A=19-297. DR PDB; 3ARF; X-ray; 2.90 A; A=19-297. DR PDB; 3ARG; X-ray; 3.00 A; A=19-297. DR PDB; 3AU1; X-ray; 2.50 A; A=19-297. DR PDB; 3G08; X-ray; 1.60 A; A=19-297. DR PDB; 3GML; X-ray; 1.70 A; A=19-297. DR PDB; 3GMM; X-ray; 1.80 A; A=19-297. DR PDB; 3GMN; X-ray; 1.70 A; A=19-297. DR PDB; 3GMO; X-ray; 1.60 A; A=19-297. DR PDB; 3GMP; X-ray; 1.70 A; A=19-297. DR PDB; 3GMQ; X-ray; 1.80 A; A=19-297. DR PDB; 3GMR; X-ray; 1.90 A; A=19-297. DR PDB; 3HE6; X-ray; 2.90 A; A=19-297. DR PDB; 3HE7; X-ray; 2.80 A; A=19-297. DR PDB; 3ILP; X-ray; 1.85 A; A=19-297. DR PDB; 3ILQ; X-ray; 2.05 A; C=19-297. DR PDB; 3MA7; X-ray; 2.29 A; A/C=19-297. DR PDB; 3O8X; X-ray; 2.74 A; A=19-297. DR PDB; 3O9W; X-ray; 2.80 A; A=19-297. DR PDB; 3QI9; X-ray; 2.30 A; A=19-297. DR PDB; 3QUX; X-ray; 2.91 A; A=19-297. DR PDB; 3QUY; X-ray; 2.25 A; A=19-297. DR PDB; 3QUZ; X-ray; 2.30 A; A=19-297. DR PDB; 3RTQ; X-ray; 2.80 A; A=19-297. DR PDB; 3RUG; X-ray; 2.20 A; A/C=19-297. DR PDB; 3RZC; X-ray; 2.80 A; A=19-297. DR PDB; 3SCM; X-ray; 2.50 A; A=19-297. DR PDB; 3SDA; X-ray; 2.80 A; A=19-297. DR PDB; 3SDC; X-ray; 3.10 A; A=19-297. DR PDB; 3SDD; X-ray; 3.00 A; A=19-297. DR PDB; 3T1F; X-ray; 1.70 A; A=19-297. DR PDB; 3TA3; X-ray; 2.70 A; A=19-297. DR PDB; 3TN0; X-ray; 3.20 A; A=19-297. DR PDB; 3TO4; X-ray; 3.10 A; A=19-297. DR PDB; 3TVM; X-ray; 2.80 A; A/E=19-297. DR PDB; 3UBX; X-ray; 3.10 A; A/D=19-297. DR PDB; 4APQ; X-ray; 3.00 A; A=19-297. DR PDB; 4EI5; X-ray; 3.10 A; A/E=19-297. DR PDB; 4ELM; X-ray; 3.48 A; A/C=19-297. DR PDB; 4IRJ; X-ray; 3.00 A; A=19-297. DR PDB; 4IRS; X-ray; 2.80 A; A=19-297. DR PDB; 4MNG; X-ray; 3.01 A; A/C=204-297. DR PDB; 4MQ7; X-ray; 2.60 A; A=205-297. DR PDB; 4MX7; X-ray; 2.24 A; A=19-297. DR PDB; 4Y16; X-ray; 2.60 A; A=19-297. DR PDB; 4Y2D; X-ray; 3.05 A; A/E=19-297. DR PDB; 4Y4F; X-ray; 3.19 A; A/E=19-297. DR PDB; 4Y4H; X-ray; 3.10 A; A/E=19-297. DR PDB; 4Y4K; X-ray; 2.90 A; A=19-297. DR PDB; 4ZAK; X-ray; 2.82 A; A=19-297. DR PDB; 5EFI; X-ray; 1.80 A; A=19-297. DR PDB; 5FKP; X-ray; 1.80 A; A=19-297. DR PDB; 5TW2; X-ray; 1.75 A; A=19-297. DR PDB; 5TW5; X-ray; 1.85 A; A=19-297. DR PDB; 5VCJ; X-ray; 3.16 A; A=19-297. DR PDB; 6BNK; X-ray; 3.20 A; A/E=19-297. DR PDB; 6BNL; X-ray; 2.60 A; A/E=19-297. DR PDB; 6C5M; X-ray; 2.45 A; A=19-297. DR PDB; 6C69; X-ray; 1.94 A; A=19-297. DR PDB; 6C6A; X-ray; 2.45 A; A=19-297. DR PDB; 6C6C; X-ray; 2.08 A; A=19-297. DR PDB; 6C6E; X-ray; 2.18 A; A=19-297. DR PDB; 6C6F; X-ray; 1.67 A; A=19-297. DR PDB; 6C6H; X-ray; 2.00 A; A=19-297. DR PDB; 6C6J; X-ray; 1.79 A; A=19-297. DR PDB; 6CW6; X-ray; 2.85 A; A=19-297. DR PDB; 6CW9; X-ray; 2.00 A; A=24-297. DR PDB; 6CWB; X-ray; 2.85 A; A=19-297. DR PDB; 6CWE; X-ray; 2.20 A; A=19-297. DR PDB; 6CX5; X-ray; 2.40 A; A=19-297. DR PDB; 6CX7; X-ray; 2.60 A; A=19-297. DR PDB; 6CX9; X-ray; 2.36 A; A=19-297. DR PDB; 6CXA; X-ray; 2.65 A; A=19-297. DR PDB; 6CXE; X-ray; 2.05 A; A=19-297. DR PDB; 6CXF; X-ray; 2.50 A; A=19-297. DR PDB; 6CYW; X-ray; 1.95 A; A=19-297. DR PDB; 6MIV; X-ray; 2.05 A; A=19-297. DR PDB; 6MIY; X-ray; 2.75 A; A/E=19-297. DR PDB; 6MJ4; X-ray; 2.00 A; A=19-297. DR PDB; 6MJ6; X-ray; 2.45 A; A=19-297. DR PDB; 6MJA; X-ray; 2.35 A; A=19-297. DR PDB; 6MJI; X-ray; 2.30 A; A=19-297. DR PDB; 6MJJ; X-ray; 1.93 A; A=19-297. DR PDB; 6MJQ; X-ray; 3.00 A; A/E=19-297. DR PDB; 6MSS; X-ray; 3.00 A; C=19-297. DR PDB; 6OJP; X-ray; 2.17 A; A=19-297. DR PDB; 6OMG; X-ray; 2.10 A; A=19-297. DR PDB; 6OOR; X-ray; 2.45 A; A=19-297. DR PDB; 6XNG; X-ray; 2.79 A; A=19-297. DR PDB; 7M72; X-ray; 2.40 A; A=19-297. DR PDBsum; 1CD1; -. DR PDBsum; 1Z5L; -. DR PDBsum; 1ZHN; -. DR PDBsum; 2AKR; -. DR PDBsum; 2FIK; -. DR PDBsum; 2GAZ; -. DR PDBsum; 2Q7Y; -. DR PDBsum; 3ARB; -. DR PDBsum; 3ARD; -. DR PDBsum; 3ARE; -. DR PDBsum; 3ARF; -. DR PDBsum; 3ARG; -. DR PDBsum; 3AU1; -. DR PDBsum; 3G08; -. DR PDBsum; 3GML; -. DR PDBsum; 3GMM; -. DR PDBsum; 3GMN; -. DR PDBsum; 3GMO; -. DR PDBsum; 3GMP; -. DR PDBsum; 3GMQ; -. DR PDBsum; 3GMR; -. DR PDBsum; 3HE6; -. DR PDBsum; 3HE7; -. DR PDBsum; 3ILP; -. DR PDBsum; 3ILQ; -. DR PDBsum; 3MA7; -. DR PDBsum; 3O8X; -. DR PDBsum; 3O9W; -. DR PDBsum; 3QI9; -. DR PDBsum; 3QUX; -. DR PDBsum; 3QUY; -. DR PDBsum; 3QUZ; -. DR PDBsum; 3RTQ; -. DR PDBsum; 3RUG; -. DR PDBsum; 3RZC; -. DR PDBsum; 3SCM; -. DR PDBsum; 3SDA; -. DR PDBsum; 3SDC; -. DR PDBsum; 3SDD; -. DR PDBsum; 3T1F; -. DR PDBsum; 3TA3; -. DR PDBsum; 3TN0; -. DR PDBsum; 3TO4; -. DR PDBsum; 3TVM; -. DR PDBsum; 3UBX; -. DR PDBsum; 4APQ; -. DR PDBsum; 4EI5; -. DR PDBsum; 4ELM; -. DR PDBsum; 4IRJ; -. DR PDBsum; 4IRS; -. DR PDBsum; 4MNG; -. DR PDBsum; 4MQ7; -. DR PDBsum; 4MX7; -. DR PDBsum; 4Y16; -. DR PDBsum; 4Y2D; -. DR PDBsum; 4Y4F; -. DR PDBsum; 4Y4H; -. DR PDBsum; 4Y4K; -. DR PDBsum; 4ZAK; -. DR PDBsum; 5EFI; -. DR PDBsum; 5FKP; -. DR PDBsum; 5TW2; -. DR PDBsum; 5TW5; -. DR PDBsum; 5VCJ; -. DR PDBsum; 6BNK; -. DR PDBsum; 6BNL; -. DR PDBsum; 6C5M; -. DR PDBsum; 6C69; -. DR PDBsum; 6C6A; -. DR PDBsum; 6C6C; -. DR PDBsum; 6C6E; -. DR PDBsum; 6C6F; -. DR PDBsum; 6C6H; -. DR PDBsum; 6C6J; -. DR PDBsum; 6CW6; -. DR PDBsum; 6CW9; -. DR PDBsum; 6CWB; -. DR PDBsum; 6CWE; -. DR PDBsum; 6CX5; -. DR PDBsum; 6CX7; -. DR PDBsum; 6CX9; -. DR PDBsum; 6CXA; -. DR PDBsum; 6CXE; -. DR PDBsum; 6CXF; -. DR PDBsum; 6CYW; -. DR PDBsum; 6MIV; -. DR PDBsum; 6MIY; -. DR PDBsum; 6MJ4; -. DR PDBsum; 6MJ6; -. DR PDBsum; 6MJA; -. DR PDBsum; 6MJI; -. DR PDBsum; 6MJJ; -. DR PDBsum; 6MJQ; -. DR PDBsum; 6MSS; -. DR PDBsum; 6OJP; -. DR PDBsum; 6OMG; -. DR PDBsum; 6OOR; -. DR PDBsum; 6XNG; -. DR PDBsum; 7M72; -. DR AlphaFoldDB; P11609; -. DR SMR; P11609; -. DR DIP; DIP-6127N; -. DR IntAct; P11609; 1. DR STRING; 10090.ENSMUSP00000029717; -. DR ChEMBL; CHEMBL4523182; -. DR GlyConnect; 2130; 1 N-Linked glycan (1 site). DR GlyCosmos; P11609; 5 sites, 1 glycan. DR GlyGen; P11609; 5 sites, 1 N-linked glycan (1 site). DR iPTMnet; P11609; -. DR PhosphoSitePlus; P11609; -. DR SwissPalm; P11609; -. DR jPOST; P11609; -. DR MaxQB; P11609; -. DR PaxDb; 10090-ENSMUSP00000029717; -. DR PeptideAtlas; P11609; -. DR ProteomicsDB; 265621; -. DR Pumba; P11609; -. DR ABCD; P11609; 2 sequenced antibodies. DR DNASU; 12479; -. DR GeneID; 12479; -. DR KEGG; mmu:12479; -. DR UCSC; uc012cre.1; mouse. DR AGR; MGI:107674; -. DR CTD; 12479; -. DR MGI; MGI:107674; Cd1d1. DR eggNOG; ENOG502SJH6; Eukaryota. DR InParanoid; P11609; -. DR OrthoDB; 4632172at2759; -. DR PhylomeDB; P11609; -. DR TreeFam; TF336723; -. DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR BioGRID-ORCS; 12479; 1 hit in 80 CRISPR screens. DR EvolutionaryTrace; P11609; -. DR PRO; PR:P11609; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P11609; Protein. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005769; C:early endosome; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. 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:0005770; C:late endosome; IDA:MGI. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; IDA:MGI. DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI. DR GO; GO:0030883; F:endogenous lipid antigen binding; IDA:MGI. DR GO; GO:0030884; F:exogenous lipid antigen binding; ISO:MGI. DR GO; GO:0042393; F:histone binding; ISO:MGI. DR GO; GO:0030882; F:lipid antigen binding; ISO:MGI. DR GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central. DR GO; GO:0042608; F:T cell receptor binding; IDA:MGI. DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI. DR GO; GO:0048006; P:antigen processing and presentation, endogenous lipid antigen via MHC class Ib; ISO:MGI. DR GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IDA:MGI. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0001865; P:NK T cell differentiation; IMP:CACAO. 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:0043032; P:positive regulation of macrophage activation; IDA:MGI. DR GO; GO:0051135; P:positive regulation of NK T cell activation; IDA:MGI. DR GO; GO:0051138; P:positive regulation of NK T cell differentiation; IMP:MGI. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:MGI. DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI. DR GO; GO:0032729; P:positive regulation of type II interferon production; IMP:MGI. DR GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI. DR GO; GO:0033084; P:regulation of immature T cell proliferation in thymus; IMP:CACAO. DR GO; GO:0050776; P:regulation of immune response; IMP:MGI. DR CDD; cd21029; IgC1_CD1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 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 PANTHER; PTHR16675:SF175; ANTIGEN-PRESENTING GLYCOPROTEIN CD1D; 1. DR PANTHER; PTHR16675; MHC CLASS I-RELATED; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF16497; MHC_I_3; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 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..21 FT /evidence="ECO:0000255" FT CHAIN 22..336 FT /note="Antigen-presenting glycoprotein CD1d1" FT /id="PRO_0000014591" 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 BINDING 98 FT /ligand="a D-galactosylceramide" FT /ligand_id="ChEBI:CHEBI:36498" FT /evidence="ECO:0000269|PubMed:16002697, FT ECO:0000269|PubMed:16314439, ECO:0000269|PubMed:16537470, FT ECO:0007744|PDB:1Z5L, ECO:0007744|PDB:2AKR, FT ECO:0007744|PDB:2FIK" FT BINDING 171..174 FT /ligand="a D-galactosylceramide" FT /ligand_id="ChEBI:CHEBI:36498" FT /evidence="ECO:0000269|PubMed:16002697, FT ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16314439, FT ECO:0000269|PubMed:16537470, ECO:0007744|PDB:1Z5L, FT ECO:0007744|PDB:1ZHN, ECO:0007744|PDB:2AKR, FT ECO:0007744|PDB:2FIK" 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:0000269|PubMed:16002697, FT ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16537470" FT CARBOHYD 60 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16002697, FT ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16537470" 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:0000269|PubMed:16002697, FT ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16537470" FT DISULFID 122..186 FT /evidence="ECO:0000269|PubMed:16002697, FT ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16314439, FT ECO:0000269|PubMed:16537470, ECO:0000269|PubMed:9219685, FT ECO:0007744|PDB:1CD1, ECO:0007744|PDB:1Z5L, FT ECO:0007744|PDB:1ZHN, ECO:0007744|PDB:2AKR, FT ECO:0007744|PDB:2FIK" FT DISULFID 226..281 FT /evidence="ECO:0000269|PubMed:16002697, FT ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16314439, FT ECO:0000269|PubMed:16537470, ECO:0000269|PubMed:9219685, FT ECO:0007744|PDB:1CD1, ECO:0007744|PDB:1Z5L, FT ECO:0007744|PDB:1ZHN, ECO:0007744|PDB:2AKR, FT ECO:0007744|PDB:2FIK" FT CONFLICT 219 FT /note="D -> H (in Ref. 2; BAB22206 and 3; CAA31568)" FT /evidence="ECO:0000305" FT CONFLICT 240 FT /note="W -> C (in Ref. 1; AAA37391)" FT /evidence="ECO:0000305" FT STRAND 26..38 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 41..50 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 53..58 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:3G08" FT TURN 70..75 FT /evidence="ECO:0007829|PDB:3G08" FT HELIX 78..105 FT /evidence="ECO:0007829|PDB:3G08" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:6C6F" FT STRAND 112..124 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:3GML" FT STRAND 130..138 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 141..147 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 150..153 FT /evidence="ECO:0007829|PDB:3G08" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:3G08" FT HELIX 162..170 FT /evidence="ECO:0007829|PDB:3G08" FT HELIX 172..183 FT /evidence="ECO:0007829|PDB:3G08" FT HELIX 185..196 FT /evidence="ECO:0007829|PDB:3G08" FT HELIX 198..201 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 208..214 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 217..220 FT /evidence="ECO:0007829|PDB:1CD1" FT STRAND 222..234 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 237..242 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:3TA3" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:4Y4H" FT TURN 259..261 FT /evidence="ECO:0007829|PDB:4Y4H" FT STRAND 263..271 FT /evidence="ECO:0007829|PDB:3G08" FT TURN 273..278 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 279..284 FT /evidence="ECO:0007829|PDB:3G08" FT HELIX 286..288 FT /evidence="ECO:0007829|PDB:3G08" FT STRAND 293..296 FT /evidence="ECO:0007829|PDB:3G08" SQ SEQUENCE 336 AA; 38554 MW; E4A666E1942E0114 CRC64; MRYLPWLLLW AFLQVWGQSE AQQKNYTFRC LQMSSFANRS WSRTDSVVWL GDLQTHRWSN DSATISFTKP WSQGKLSNQQ WEKLQHMFQV YRVSFTRDIQ ELVKMMSPKE DYPIEIQLSA GCEMYPGNAS ESFLHVAFQG KYVVRFWGTS WQTVPGAPSW LDLPIKVLNA DQGTSATVQM LLNDTCPLFV RGLLEAGKSD LEKQEKPVAW LSSVPSSADG HRQLVCHVSG FYPKPVWVMW MRGDQEQQGT HRGDFLPNAD ETWYLQATLD VEAGEEAGLA CRVKHSSLGG QDIILYWDAR QAPVGLIVFI VLIMLVVVGA VVYYIWRRRS AYQDIR //