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P11609

- CD1D1_MOUSE

UniProt

P11609 - CD1D1_MOUSE

Protein

Antigen-presenting glycoprotein CD1d1

Gene

Cd1d1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei98 – 981Glycolipid
    Binding sitei171 – 1711Glycolipid
    Binding sitei174 – 1741Glycolipid

    GO - Molecular functioni

    1. endogenous lipid antigen binding Source: MGI
    2. protein binding Source: MGI
    3. T cell receptor binding Source: MGI

    GO - Biological processi

    1. antigen processing and presentation Source: MGI
    2. antigen processing and presentation, exogenous lipid antigen via MHC class Ib Source: MGI
    3. innate immune response Source: UniProtKB-KW
    4. positive regulation of interferon-gamma biosynthetic process Source: MGI
    5. positive regulation of interleukin-2 biosynthetic process Source: MGI
    6. positive regulation of interleukin-4 biosynthetic process Source: MGI
    7. positive regulation of macrophage activation Source: MGI
    8. positive regulation of NK T cell activation Source: MGI
    9. positive regulation of NK T cell differentiation Source: MGI
    10. positive regulation of T cell mediated cytotoxicity Source: MGI
    11. positive thymic T cell selection Source: MGI
    12. regulation of immune response Source: MGI

    Keywords - Biological processi

    Immunity, Innate immunity

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Antigen-presenting glycoprotein CD1d1
    Alternative name(s):
    CD_antigen: CD1d.1
    Gene namesi
    Name:Cd1d1
    Synonyms:Cd1.1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:107674. Cd1d1.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Endosome membrane 1 Publication. Lysosome membrane 1 Publication
    Note: Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes.

    GO - Cellular componenti

    1. early endosome Source: MGI
    2. endosome membrane Source: UniProtKB-SubCell
    3. external side of plasma membrane Source: MGI
    4. integral component of membrane Source: UniProtKB-KW
    5. late endosome Source: MGI
    6. lysosomal membrane Source: UniProtKB-SubCell
    7. lysosome Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Endosome, Lysosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 336315Antigen-presenting glycoprotein CD1d1PRO_0000014591Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi38 – 381N-linked (GlcNAc...)3 Publications
    Glycosylationi60 – 601N-linked (GlcNAc...)3 Publications
    Disulfide bondi122 ↔ 186
    Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi183 – 1831N-linked (GlcNAc...)3 Publications
    Disulfide bondi226 ↔ 281

    Post-translational modificationi

    N-glycosylated.5 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP11609.
    PRIDEiP11609.

    PTM databases

    PhosphoSiteiP11609.

    Expressioni

    Tissue specificityi

    Expressed on cortical thymocytes, on certain T-cell leukemias, and in various other tissues.

    Gene expression databases

    ArrayExpressiP11609.
    BgeeiP11609.
    CleanExiMM_CD1D1.
    GenevestigatoriP11609.

    Interactioni

    Subunit structurei

    Heterodimer with B2M (beta-2-microglobulin). Interacts with MHC II and CD74.6 Publications

    Protein-protein interaction databases

    DIPiDIP-6127N.
    IntActiP11609. 1 interaction.
    MINTiMINT-1864400.

    Structurei

    Secondary structure

    1
    336
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 3813
    Beta strandi41 – 5010
    Beta strandi53 – 586
    Beta strandi66 – 694
    Turni70 – 756
    Helixi78 – 10528
    Turni107 – 1093
    Beta strandi112 – 12413
    Beta strandi126 – 1283
    Beta strandi130 – 1389
    Beta strandi141 – 1477
    Beta strandi150 – 1534
    Helixi159 – 1613
    Helixi162 – 1709
    Helixi172 – 18312
    Helixi185 – 19612
    Helixi198 – 2014
    Beta strandi208 – 2147
    Beta strandi217 – 2204
    Beta strandi222 – 23413
    Beta strandi237 – 2426
    Beta strandi250 – 2523
    Beta strandi263 – 2719
    Turni273 – 2786
    Beta strandi279 – 2846
    Helixi286 – 2883
    Beta strandi293 – 2964

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CD1X-ray2.67A/C22-336[»]
    1Z5LX-ray2.20A/C19-297[»]
    1ZHNX-ray2.80A25-297[»]
    2AKRX-ray1.90A/C19-297[»]
    2FIKX-ray1.80A19-297[»]
    2GAZX-ray2.61A19-297[»]
    2Q7YX-ray1.95A/C19-297[»]
    3ARBX-ray2.70A19-297[»]
    3ARDX-ray3.01A19-297[»]
    3AREX-ray2.80A19-297[»]
    3ARFX-ray2.90A19-297[»]
    3ARGX-ray3.00A19-297[»]
    3AU1X-ray2.50A19-297[»]
    3G08X-ray1.60A19-297[»]
    3GMLX-ray1.70A19-297[»]
    3GMMX-ray1.80A19-297[»]
    3GMNX-ray1.70A19-297[»]
    3GMOX-ray1.60A19-297[»]
    3GMPX-ray1.70A19-297[»]
    3GMQX-ray1.80A19-297[»]
    3GMRX-ray1.90A19-297[»]
    3HE6X-ray2.90A19-297[»]
    3HE7X-ray2.80A19-297[»]
    3ILPX-ray1.85A19-297[»]
    3ILQX-ray2.05C19-297[»]
    3MA7X-ray2.29A/C19-297[»]
    3O8XX-ray2.74A19-297[»]
    3O9WX-ray2.80A19-297[»]
    3QI9X-ray2.30A19-297[»]
    3QUXX-ray2.91A19-297[»]
    3QUYX-ray2.25A19-297[»]
    3QUZX-ray2.30A19-297[»]
    3RTQX-ray2.80A19-297[»]
    3RUGX-ray2.20A/C19-297[»]
    3RZCX-ray2.80A19-297[»]
    3SCMX-ray2.50A19-297[»]
    3SDAX-ray2.80A19-297[»]
    3SDCX-ray3.10A19-297[»]
    3SDDX-ray3.00A19-297[»]
    3T1FX-ray1.70A19-297[»]
    3TA3X-ray2.70A19-297[»]
    3TN0X-ray3.20A19-297[»]
    3TO4X-ray3.10A19-297[»]
    3TVMX-ray2.80A/E19-297[»]
    3UBXX-ray3.10A/D19-297[»]
    4APQX-ray3.00A19-297[»]
    4EI5X-ray3.10A/E19-297[»]
    4ELMX-ray3.48A/C19-297[»]
    4IRJX-ray3.00A19-297[»]
    4IRSX-ray2.80A19-297[»]
    ProteinModelPortaliP11609.
    SMRiP11609. Positions 25-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11609.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 305284ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini327 – 33610CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei306 – 32621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini207 – 29791Ig-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi332 – 3354Internalization signal

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG26626.
    GeneTreeiENSGT00480000042665.
    HOGENOMiHOG000111666.
    HOVERGENiHBG004453.
    InParanoidiP11609.
    KOiK06448.
    OrthoDBiEOG7DZ8K9.
    PhylomeDBiP11609.
    TreeFamiTF336723.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    [Graphical view]
    PfamiPF07654. C1-set. 1 hit.
    [Graphical view]
    SMARTiSM00407. IGc1. 1 hit.
    [Graphical view]
    SUPFAMiSSF54452. SSF54452. 1 hit.
    PROSITEiPS50835. IG_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11609-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRYLPWLLLW AFLQVWGQSE AQQKNYTFRC LQMSSFANRS WSRTDSVVWL    50
    GDLQTHRWSN DSATISFTKP WSQGKLSNQQ WEKLQHMFQV YRVSFTRDIQ 100
    ELVKMMSPKE DYPIEIQLSA GCEMYPGNAS ESFLHVAFQG KYVVRFWGTS 150
    WQTVPGAPSW LDLPIKVLNA DQGTSATVQM LLNDTCPLFV RGLLEAGKSD 200
    LEKQEKPVAW LSSVPSSADG HRQLVCHVSG FYPKPVWVMW MRGDQEQQGT 250
    HRGDFLPNAD ETWYLQATLD VEAGEEAGLA CRVKHSSLGG QDIILYWDAR 300
    QAPVGLIVFI VLIMLVVVGA VVYYIWRRRS AYQDIR 336
    Length:336
    Mass (Da):38,554
    Last modified:December 15, 1998 - v3
    Checksum:iE4A666E1942E0114
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti219 – 2191D → H in BAB22206. (PubMed:16141072)Curated
    Sequence conflicti219 – 2191D → H in CAA31568. (PubMed:2460336)Curated
    Sequence conflicti240 – 2401W → C in AAA37391. (PubMed:1702817)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63695 mRNA. Translation: AAA37391.1.
    AK002582 mRNA. Translation: BAB22206.1.
    X13170 Genomic DNA. Translation: CAA31568.1.
    CCDSiCCDS17449.1.
    PIRiI49581.
    S01297.
    RefSeqiNP_031665.2. NM_007639.3.
    UniGeneiMm.1894.

    Genome annotation databases

    EnsembliENSMUST00000029717; ENSMUSP00000029717; ENSMUSG00000028076.
    GeneIDi12479.
    KEGGimmu:12479.
    UCSCiuc012cre.1. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    CD1d1

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63695 mRNA. Translation: AAA37391.1 .
    AK002582 mRNA. Translation: BAB22206.1 .
    X13170 Genomic DNA. Translation: CAA31568.1 .
    CCDSi CCDS17449.1.
    PIRi I49581.
    S01297.
    RefSeqi NP_031665.2. NM_007639.3.
    UniGenei Mm.1894.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CD1 X-ray 2.67 A/C 22-336 [» ]
    1Z5L X-ray 2.20 A/C 19-297 [» ]
    1ZHN X-ray 2.80 A 25-297 [» ]
    2AKR X-ray 1.90 A/C 19-297 [» ]
    2FIK X-ray 1.80 A 19-297 [» ]
    2GAZ X-ray 2.61 A 19-297 [» ]
    2Q7Y X-ray 1.95 A/C 19-297 [» ]
    3ARB X-ray 2.70 A 19-297 [» ]
    3ARD X-ray 3.01 A 19-297 [» ]
    3ARE X-ray 2.80 A 19-297 [» ]
    3ARF X-ray 2.90 A 19-297 [» ]
    3ARG X-ray 3.00 A 19-297 [» ]
    3AU1 X-ray 2.50 A 19-297 [» ]
    3G08 X-ray 1.60 A 19-297 [» ]
    3GML X-ray 1.70 A 19-297 [» ]
    3GMM X-ray 1.80 A 19-297 [» ]
    3GMN X-ray 1.70 A 19-297 [» ]
    3GMO X-ray 1.60 A 19-297 [» ]
    3GMP X-ray 1.70 A 19-297 [» ]
    3GMQ X-ray 1.80 A 19-297 [» ]
    3GMR X-ray 1.90 A 19-297 [» ]
    3HE6 X-ray 2.90 A 19-297 [» ]
    3HE7 X-ray 2.80 A 19-297 [» ]
    3ILP X-ray 1.85 A 19-297 [» ]
    3ILQ X-ray 2.05 C 19-297 [» ]
    3MA7 X-ray 2.29 A/C 19-297 [» ]
    3O8X X-ray 2.74 A 19-297 [» ]
    3O9W X-ray 2.80 A 19-297 [» ]
    3QI9 X-ray 2.30 A 19-297 [» ]
    3QUX X-ray 2.91 A 19-297 [» ]
    3QUY X-ray 2.25 A 19-297 [» ]
    3QUZ X-ray 2.30 A 19-297 [» ]
    3RTQ X-ray 2.80 A 19-297 [» ]
    3RUG X-ray 2.20 A/C 19-297 [» ]
    3RZC X-ray 2.80 A 19-297 [» ]
    3SCM X-ray 2.50 A 19-297 [» ]
    3SDA X-ray 2.80 A 19-297 [» ]
    3SDC X-ray 3.10 A 19-297 [» ]
    3SDD X-ray 3.00 A 19-297 [» ]
    3T1F X-ray 1.70 A 19-297 [» ]
    3TA3 X-ray 2.70 A 19-297 [» ]
    3TN0 X-ray 3.20 A 19-297 [» ]
    3TO4 X-ray 3.10 A 19-297 [» ]
    3TVM X-ray 2.80 A/E 19-297 [» ]
    3UBX X-ray 3.10 A/D 19-297 [» ]
    4APQ X-ray 3.00 A 19-297 [» ]
    4EI5 X-ray 3.10 A/E 19-297 [» ]
    4ELM X-ray 3.48 A/C 19-297 [» ]
    4IRJ X-ray 3.00 A 19-297 [» ]
    4IRS X-ray 2.80 A 19-297 [» ]
    ProteinModelPortali P11609.
    SMRi P11609. Positions 25-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6127N.
    IntActi P11609. 1 interaction.
    MINTi MINT-1864400.

    PTM databases

    PhosphoSitei P11609.

    Proteomic databases

    PaxDbi P11609.
    PRIDEi P11609.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029717 ; ENSMUSP00000029717 ; ENSMUSG00000028076 .
    GeneIDi 12479.
    KEGGi mmu:12479.
    UCSCi uc012cre.1. mouse.

    Organism-specific databases

    CTDi 12479.
    MGIi MGI:107674. Cd1d1.

    Phylogenomic databases

    eggNOGi NOG26626.
    GeneTreei ENSGT00480000042665.
    HOGENOMi HOG000111666.
    HOVERGENi HBG004453.
    InParanoidi P11609.
    KOi K06448.
    OrthoDBi EOG7DZ8K9.
    PhylomeDBi P11609.
    TreeFami TF336723.

    Miscellaneous databases

    EvolutionaryTracei P11609.
    NextBioi 281370.
    PROi P11609.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11609.
    Bgeei P11609.
    CleanExi MM_CD1D1.
    Genevestigatori P11609.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    [Graphical view ]
    Pfami PF07654. C1-set. 1 hit.
    [Graphical view ]
    SMARTi SM00407. IGc1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54452. SSF54452. 1 hit.
    PROSITEi PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and expression of cDNA encoding the murine homologues of CD1."
      Balk S.P., Bleicher P.A., Terhorst C.
      J. Immunol. 146:768-774(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Kidney.
    3. "Mouse CD1 is distinct from and co-exists with TL in the same thymus."
      Bradbury A., Belt K.T., Neri T.M., Milstein C., Calabi F.
      EMBO J. 7:3081-3086(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-297.
      Tissue: Thymus.
    4. "CD1d endosomal trafficking is independently regulated by an intrinsic CD1d-encoded tyrosine motif and by the invariant chain."
      Jayawardena-Wolf J., Benlagha K., Chiu Y.-H., Mehr R., Bendelac A.
      Immunity 15:897-908(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CD74, GLYCOSYLATION.
    5. "Crystal structure of mouse CD1: an MHC-like fold with a large hydrophobic binding groove."
      Zeng Z., Castano A.R., Segelke B.W., Stura E.A., Peterson P.A., Wilson I.A.
      Science 277:339-345(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) OF 25-297 IN COMPLEX WITH B2M, DISULFIDE BONDS.
    6. "Structural basis for CD1d presentation of a sulfatide derived from myelin and its implications for autoimmunity."
      Zajonc D.M., Maricic I., Wu D., Halder R., Roy K., Wong C.-H., Kumar V., Wilson I.A.
      J. Exp. Med. 202:1517-1526(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-297 IN COMPLEX WITH B2M AND CIS-TETRACOSENOYL SULFATIDE, FUNCTION, GLYCOSYLATION.
    7. "Crystal structure of mouse CD1d bound to the self ligand phosphatidylcholine: a molecular basis for NKT cell activation."
      Giabbai B., Sidobre S., Crispin M.D.M., Sanchez-Ruiz Y., Bachi A., Kronenberg M., Wilson I.A., Degano M.
      J. Immunol. 175:977-984(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-297 IN COMPLEX WITH PHOSPHATIDYLCHOLINE AND B2M, GLYCOSYLATION AT ASN-38; ASN-60 AND ASN-183, DISULFIDE BONDS.
    8. "Structure and function of a potent agonist for the semi-invariant natural killer T cell receptor."
      Zajonc D.M., Cantu C. III, Mattner J., Zhou D., Savage P.B., Bendelac A., Wilson I.A., Teyton L.
      Nat. Immunol. 6:810-818(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-297 IN COMPLEX WITH GALACTOSYLCERAMIDE AND B2M, FUNCTION, GLYCOSYLATION AT ASN-38; ASN-60 AND ASN-183, DISULFIDE BONDS.
    9. "Design of natural killer T cell activators: structure and function of a microbial glycosphingolipid bound to mouse CD1d."
      Wu D., Zajonc D.M., Fujio M., Sullivan B.A., Kinjo Y., Kronenberg M., Wilson I.A., Wong C.-H.
      Proc. Natl. Acad. Sci. U.S.A. 103:3972-3977(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-297 IN COMPLEX WITH GLYCOSPHINGOLIPID AND B2M, GLYCOSYLATION AT ASN-38; ASN-60 AND ASN-183, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCD1D1_MOUSE
    AccessioniPrimary (citable) accession number: P11609
    Secondary accession number(s): Q91XK9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    During protein synthesis and maturation, CD1 family members bind endogenous lipids that are replaced by lipid or glycolipid antigens when the proteins are internalized and pass through endosomes, before trafficking back to the cell surface.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3