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P11609

- CD1D1_MOUSE

UniProt

P11609 - CD1D1_MOUSE

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Protein

Antigen-presenting glycoprotein CD1d1

Gene

Cd1d1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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. external side of plasma membrane Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
  4. late endosome Source: MGI
  5. lysosome Source: MGI
Complete GO annotation...

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

BgeeiP11609.
CleanExiMM_CD1D1.
ExpressionAtlasiP11609. baseline and differential.
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

        10         20         30         40         50
MRYLPWLLLW AFLQVWGQSE AQQKNYTFRC LQMSSFANRS WSRTDSVVWL
60 70 80 90 100
GDLQTHRWSN DSATISFTKP WSQGKLSNQQ WEKLQHMFQV YRVSFTRDIQ
110 120 130 140 150
ELVKMMSPKE DYPIEIQLSA GCEMYPGNAS ESFLHVAFQG KYVVRFWGTS
160 170 180 190 200
WQTVPGAPSW LDLPIKVLNA DQGTSATVQM LLNDTCPLFV RGLLEAGKSD
210 220 230 240 250
LEKQEKPVAW LSSVPSSADG HRQLVCHVSG FYPKPVWVMW MRGDQEQQGT
260 270 280 290 300
HRGDFLPNAD ETWYLQATLD VEAGEEAGLA CRVKHSSLGG QDIILYWDAR
310 320 330
QAPVGLIVFI VLIMLVVVGA VVYYIWRRRS AYQDIR
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

Bgeei P11609.
CleanExi MM_CD1D1.
ExpressionAtlasi P11609. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 146 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

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