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Protein

C-type lectin domain family 7 member A

Gene

Clec7a

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

Functioni

Lectin that functions as pattern receptor specific for beta-1,3-linked and beta-1,6-linked glucans, such as cell wall constituents from pathogenic bacteria and fungi. Necessary for the TLR2-mediated inflammatory response and for TLR2-mediated activation of NF-kappa-B. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation.8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi156 – 1561Divalent metal cation
Metal bindingi158 – 1581Divalent metal cation
Metal bindingi162 – 1621Divalent metal cation
Metal bindingi241 – 2411Divalent metal cation

GO - Molecular functioni

GO - Biological processi

  • cellular response to molecule of fungal origin Source: UniProtKB
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: UniProtKB
  • leukocyte activation involved in immune response Source: UniProtKB
  • phagocytosis, recognition Source: Ensembl
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-5607764. CLEC7A (Dectin-1) signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
C-type lectin domain family 7 member A
Alternative name(s):
Beta-glucan receptor
C-type lectin superfamily member 12
Dendritic cell-associated C-type lectin 1
Short name:
DC-associated C-type lectin 1
Short name:
Dectin-1
Gene namesi
Name:Clec7a
Synonyms:Bgr, Clecsf12, Dectin1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1861431. Clec7a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4949CytoplasmicSequence analysisAdd
BLAST
Transmembranei50 – 7021Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini71 – 244174ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi221 – 2211W → A: Loss of glucan binding. Abolishes activation of NF-kappa-B. 1 Publication
Mutagenesisi223 – 2231H → A: Loss of glucan binding. Abolishes activation of NF-kappa-B. 1 Publication
Mutagenesisi232 – 2321C → A: Abolishes cell surface expression. 1 Publication

Chemistry

ChEMBLiCHEMBL2034809.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244C-type lectin domain family 7 member APRO_0000269493Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphotyrosine1 Publication
Disulfide bondi119 ↔ 130PROSITE-ProRule annotation1 Publication
Disulfide bondi147 ↔ 240PROSITE-ProRule annotation1 Publication
Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence analysis
Disulfide bondi219 ↔ 232PROSITE-ProRule annotation1 Publication
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.1 Publication
Phosphorylated on tyrosine residues in response to glucan binding.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ6QLQ4.

PTM databases

iPTMnetiQ6QLQ4.
PhosphoSiteiQ6QLQ4.

Expressioni

Tissue specificityi

Detected in spleen (at protein level). Highly expressed in dendritic cells, spleen and thymus. Detected in epidermal Langerhans cells. Detected in macrophages, liver and lung.3 Publications

Gene expression databases

CleanExiMM_CLEC7A.
ExpressionAtlasiQ6QLQ4. baseline and differential.
GenevisibleiQ6QLQ4. MM.

Interactioni

Subunit structurei

Homodimer (Probable). Interacts with SYK; participates in leukocyte activation in presence of fungal pathogens.Curated2 Publications

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi124 – 1263Combined sources
Beta strandi129 – 13810Combined sources
Helixi140 – 14910Combined sources
Helixi160 – 17011Combined sources
Helixi171 – 1733Combined sources
Beta strandi176 – 1838Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi201 – 2033Combined sources
Helixi212 – 2143Combined sources
Beta strandi219 – 2235Combined sources
Beta strandi226 – 2305Combined sources
Beta strandi236 – 2427Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BPDX-ray1.50A/B113-244[»]
2BPEX-ray2.25A/B113-244[»]
2BPHX-ray2.20A/B113-244[»]
2CL8X-ray2.80A/B113-244[»]
ProteinModelPortaliQ6QLQ4.
SMRiQ6QLQ4. Positions 116-244.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6QLQ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini126 – 241116C-type lectinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi15 – 184ITAM-like

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00700000104266.
HOGENOMiHOG000220926.
HOVERGENiHBG105854.
InParanoidiQ6QLQ4.
TreeFamiTF336674.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6QLQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYHSHIENL DEDGYTQLDF STQDIHKRPR GSEKGSQAPS SPWRPIAVGL
60 70 80 90 100
GILCFVVVVV AAVLGALGEY GHNSGRNPEE KDNFLSRNKE NHKPTESSLD
110 120 130 140 150
EKVAPSKASQ TTGGFSQPCL PNWIMHGKSC YLFSFSGNSW YGSKRHCSQL
160 170 180 190 200
GAHLLKIDNS KEFEFIESQT SSHRINAFWI GLSRNQSEGP WFWEDGSAFF
210 220 230 240
PNSFQVRNTA PQESLLHNCV WIHGSEVYNQ ICNTSSYSIC EKEL
Length:244
Mass (Da):27,420
Last modified:October 3, 2012 - v3
Checksum:iC9435DD135D2F122
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371Q → R in AAF72710 (PubMed:10779524).Curated
Sequence conflicti37 – 371Q → R in AAS37670 (PubMed:11544516).Curated
Sequence conflicti37 – 371Q → R in AAH27742 (PubMed:15489334).Curated
Sequence conflicti68 – 714GEYG → AFWR in AAF72710 (PubMed:10779524).Curated
Sequence conflicti68 – 714GEYG → AFWR in AAS37670 (PubMed:11544516).Curated
Sequence conflicti68 – 714GEYG → AFWR in AAH27742 (PubMed:15489334).Curated
Sequence conflicti83 – 831N → S in AAS37670 (PubMed:11544516).Curated
Sequence conflicti85 – 851L → P in AAH27742 (PubMed:15489334).Curated
Sequence conflicti118 – 1181P → S in AAF72710 (PubMed:10779524).Curated
Sequence conflicti118 – 1181P → S in AAS37670 (PubMed:11544516).Curated
Sequence conflicti124 – 1241I → T in AAH27742 (PubMed:15489334).Curated
Sequence conflicti174 – 1763RIN → HIT in AAH27742 (PubMed:15489334).Curated
Sequence conflicti209 – 2102TA → AV in AAS37670 (PubMed:11544516).Curated
Sequence conflicti210 – 2101A → V in AAF72710 (PubMed:10779524).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF262985 mRNA. Translation: AAF72710.1.
AY534909 mRNA. Translation: AAS37670.1.
AC138620 Genomic DNA. No translation available.
BC027742 mRNA. Translation: AAH27742.1.
UniGeneiMm.239516.

Genome annotation databases

EnsembliENSMUST00000112076; ENSMUSP00000107707; ENSMUSG00000079293.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Mouse recombinant soluble Dectin-1 CTLD from insect cells origin

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF262985 mRNA. Translation: AAF72710.1.
AY534909 mRNA. Translation: AAS37670.1.
AC138620 Genomic DNA. No translation available.
BC027742 mRNA. Translation: AAH27742.1.
UniGeneiMm.239516.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BPDX-ray1.50A/B113-244[»]
2BPEX-ray2.25A/B113-244[»]
2BPHX-ray2.20A/B113-244[»]
2CL8X-ray2.80A/B113-244[»]
ProteinModelPortaliQ6QLQ4.
SMRiQ6QLQ4. Positions 116-244.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL2034809.

PTM databases

iPTMnetiQ6QLQ4.
PhosphoSiteiQ6QLQ4.

Proteomic databases

PRIDEiQ6QLQ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000112076; ENSMUSP00000107707; ENSMUSG00000079293.

Organism-specific databases

MGIiMGI:1861431. Clec7a.

Phylogenomic databases

GeneTreeiENSGT00700000104266.
HOGENOMiHOG000220926.
HOVERGENiHBG105854.
InParanoidiQ6QLQ4.
TreeFamiTF336674.

Enzyme and pathway databases

ReactomeiR-MMU-5607764. CLEC7A (Dectin-1) signaling.

Miscellaneous databases

EvolutionaryTraceiQ6QLQ4.
PROiQ6QLQ4.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CLEC7A.
ExpressionAtlasiQ6QLQ4. baseline and differential.
GenevisibleiQ6QLQ4. MM.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel, dendritic cell-associated molecule, dectin-1, by subtractive cDNA cloning."
    Ariizumi K., Shen G.-L., Shikano S., Xu S., Ritter R. III, Kumamoto T., Edelbaum D., Morita A., Bergstresser P.R., Takashima A.
    J. Biol. Chem. 275:20157-20167(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Dendritic cell.
  2. "Immune recognition. A new receptor for beta-glucans."
    Brown G.D., Gordon S.
    Nature 413:36-37(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  5. "Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2."
    Gantner B.N., Simmons R.M., Canavera S.J., Akira S., Underhill D.M.
    J. Exp. Med. 197:1107-1117(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY.
  6. "Characterization of beta-glucan recognition site on C-type lectin, dectin 1."
    Adachi Y., Ishii T., Ikeda Y., Hoshino A., Tamura H., Aketagawa J., Tanaka S., Ohno N.
    Infect. Immun. 72:4159-4171(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-221; HIS-223 AND CYS-232.
  7. "Dectin-1 mediates macrophage recognition of Candida albicans yeast but not filaments."
    Gantner B.N., Simmons R.M., Underhill D.M.
    EMBO J. 24:1277-1286(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Syk-dependent cytokine induction by Dectin-1 reveals a novel pattern recognition pathway for C type lectins."
    Rogers N.C., Slack E.C., Edwards A.D., Nolte M.A., Schulz O., Schweighoffer E., Williams D.L., Gordon S., Tybulewicz V.L., Brown G.D., Reis e Sousa C.
    Immunity 22:507-517(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SYK.
  9. "Innate immunity to the pathogenic fungus Coccidioides posadasii is dependent on Toll-like receptor 2 and Dectin-1."
    Viriyakosol S., Fierer J., Brown G.D., Kirkland T.N.
    Infect. Immun. 73:1553-1560(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The beta-glucan receptor dectin-1 functions together with TLR2 to mediate macrophage activation by mycobacteria."
    Yadav M., Schorey J.S.
    Blood 108:3168-3175(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function."
    Brown J., O'Callaghan C.A., Marshall A.S., Gilbert R.J., Siebold C., Gordon S., Brown G.D., Jones E.Y.
    Protein Sci. 16:1042-1052(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 113-244 IN COMPLEX WITH METAL ION AND BETA-GLUCAN ANALOG LAMINARIN, METAL-BINDING SITES, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiCLC7A_MOUSE
AccessioniPrimary (citable) accession number: Q6QLQ4
Secondary accession number(s): E9QPW2, Q8K1L4, Q9JI50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: October 3, 2012
Last modified: June 8, 2016
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.