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Protein

Antigen-presenting glycoprotein CD1d1

Gene

Cd1d1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei98GlycolipidCombined sources3 Publications1

GO - Molecular functioni

GO - Biological processi

  • antigen processing and presentation Source: MGI
  • antigen processing and presentation, endogenous lipid antigen via MHC class Ib Source: MGI
  • antigen processing and presentation, exogenous lipid antigen via MHC class Ib Source: MGI
  • innate immune response Source: UniProtKB-KW
  • NK T cell differentiation Source: CACAO
  • positive regulation of interferon-gamma biosynthetic process Source: MGI
  • positive regulation of interleukin-2 biosynthetic process Source: MGI
  • positive regulation of interleukin-4 biosynthetic process Source: MGI
  • positive regulation of macrophage activation Source: MGI
  • positive regulation of NK T cell activation Source: MGI
  • positive regulation of NK T cell differentiation Source: MGI
  • positive regulation of T cell mediated cytotoxicity Source: MGI
  • positive regulation of T cell proliferation Source: MGI
  • positive thymic T cell selection Source: MGI
  • regulation of immature T cell proliferation in thymus Source: CACAO
  • 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
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:107674. Cd1d1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 305ExtracellularSequence analysisAdd BLAST284
Transmembranei306 – 326HelicalSequence analysisAdd BLAST21
Topological domaini327 – 336CytoplasmicSequence analysis10

GO - Cellular componenti

  • cell surface Source: MGI
  • cytoplasm Source: MGI
  • early endosome Source: MGI
  • endosome membrane Source: UniProtKB-SubCell
  • external side of plasma membrane Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • late endosome Source: MGI
  • lysosomal membrane Source: UniProtKB-SubCell
  • lysosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001459122 – 336Antigen-presenting glycoprotein CD1d1Add BLAST315

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi25N-linked (GlcNAc...)Sequence analysis1
Glycosylationi38N-linked (GlcNAc...)3 Publications1
Glycosylationi60N-linked (GlcNAc...)3 Publications1
Disulfide bondi122 ↔ 186Combined sources5 Publications
Glycosylationi128N-linked (GlcNAc...)Sequence analysis1
Glycosylationi183N-linked (GlcNAc...)3 Publications1
Disulfide bondi226 ↔ 281Combined sources5 Publications

Post-translational modificationi

N-glycosylated.5 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP11609.
PaxDbiP11609.
PeptideAtlasiP11609.
PRIDEiP11609.

PTM databases

PhosphoSitePlusiP11609.
SwissPalmiP11609.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000028076.
CleanExiMM_CD1D1.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-6127N.
IntActiP11609. 1 interactor.
MINTiMINT-1864400.
STRINGi10090.ENSMUSP00000029717.

Structurei

Secondary structure

1336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 38Combined sources13
Beta strandi41 – 50Combined sources10
Beta strandi53 – 58Combined sources6
Beta strandi66 – 69Combined sources4
Turni70 – 75Combined sources6
Helixi78 – 105Combined sources28
Turni107 – 109Combined sources3
Beta strandi112 – 124Combined sources13
Beta strandi126 – 128Combined sources3
Beta strandi130 – 138Combined sources9
Beta strandi141 – 147Combined sources7
Beta strandi150 – 153Combined sources4
Helixi159 – 161Combined sources3
Helixi162 – 170Combined sources9
Helixi172 – 183Combined sources12
Helixi185 – 196Combined sources12
Helixi198 – 201Combined sources4
Beta strandi208 – 214Combined sources7
Beta strandi217 – 220Combined sources4
Beta strandi222 – 234Combined sources13
Beta strandi237 – 242Combined sources6
Beta strandi250 – 252Combined sources3
Beta strandi256 – 258Combined sources3
Turni259 – 261Combined sources3
Beta strandi263 – 271Combined sources9
Turni273 – 278Combined sources6
Beta strandi279 – 284Combined sources6
Helixi286 – 288Combined sources3
Beta strandi293 – 296Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4MNGX-ray3.01A/C204-297[»]
4MQ7X-ray2.60A205-297[»]
4MX7X-ray2.24A19-297[»]
4Y16X-ray2.60A19-297[»]
4Y2DX-ray3.05A/E19-297[»]
4Y4FX-ray3.19A/E19-297[»]
4Y4HX-ray3.10A/E19-297[»]
4Y4KX-ray2.90A19-297[»]
4ZAKX-ray2.82A19-297[»]
5EFIX-ray1.80A19-297[»]
5FKPX-ray1.80A19-297[»]
ProteinModelPortaliP11609.
SMRiP11609.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11609.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini207 – 297Ig-likeAdd BLAST91

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni171 – 174Glycolipid bindingCombined sources4 Publications4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi332 – 335Internalization signal4

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410ITUC. Eukaryota.
ENOG4111EG6. LUCA.
HOGENOMiHOG000111666.
HOVERGENiHBG004453.
InParanoidiP11609.
KOiK06448.
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.
PF16497. MHC_I_3. 1 hit.
[Graphical view]
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. 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)DescriptionActionsGraphical viewLength
Sequence conflicti219D → H in BAB22206 (PubMed:16141072).Curated1
Sequence conflicti219D → H in CAA31568 (PubMed:2460336).Curated1
Sequence conflicti240W → C in AAA37391 (PubMed:1702817).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

GeneIDi12479.
KEGGimmu:12479.
UCSCiuc012cre.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

CD1d1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4MNGX-ray3.01A/C204-297[»]
4MQ7X-ray2.60A205-297[»]
4MX7X-ray2.24A19-297[»]
4Y16X-ray2.60A19-297[»]
4Y2DX-ray3.05A/E19-297[»]
4Y4FX-ray3.19A/E19-297[»]
4Y4HX-ray3.10A/E19-297[»]
4Y4KX-ray2.90A19-297[»]
4ZAKX-ray2.82A19-297[»]
5EFIX-ray1.80A19-297[»]
5FKPX-ray1.80A19-297[»]
ProteinModelPortaliP11609.
SMRiP11609.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6127N.
IntActiP11609. 1 interactor.
MINTiMINT-1864400.
STRINGi10090.ENSMUSP00000029717.

PTM databases

PhosphoSitePlusiP11609.
SwissPalmiP11609.

Proteomic databases

MaxQBiP11609.
PaxDbiP11609.
PeptideAtlasiP11609.
PRIDEiP11609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi12479.
KEGGimmu:12479.
UCSCiuc012cre.1. mouse.

Organism-specific databases

CTDi12479.
MGIiMGI:107674. Cd1d1.

Phylogenomic databases

eggNOGiENOG410ITUC. Eukaryota.
ENOG4111EG6. LUCA.
HOGENOMiHOG000111666.
HOVERGENiHBG004453.
InParanoidiP11609.
KOiK06448.
PhylomeDBiP11609.
TreeFamiTF336723.

Miscellaneous databases

EvolutionaryTraceiP11609.
PROiP11609.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028076.
CleanExiMM_CD1D1.

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.
PF16497. MHC_I_3. 1 hit.
[Graphical view]
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 166 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.