CD1D1_MOUSE
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 03-AUG-2022, entry version 198.
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";
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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 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; P11609; -.
DR PeptideAtlas; P11609; -.
DR PRIDE; P11609; -.
DR ProteomicsDB; 265621; -.
DR ABCD; P11609; 2 sequenced antibodies.
DR DNASU; 12479; -.
DR GeneID; 12479; -.
DR KEGG; mmu:12479; -.
DR UCSC; uc012cre.1; mouse.
DR CTD; 12479; -.
DR MGI; MGI:107674; Cd1d1.
DR eggNOG; ENOG502SJH6; Eukaryota.
DR InParanoid; P11609; -.
DR OrthoDB; 827472at2759; -.
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 75 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001865; P:NK T cell differentiation; IMP:CACAO.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
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: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 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..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
