[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY. STRAIN=BALB/c; TISSUE=Dendritic cell; DOI=10.1074/jbc.M909512199; PubMed=10779524 [NCBI, ExPASy, EBI, Israel, Japan] Ariizumi K., Shen G.-L., Shikano S., Xu S., Ritter R. III, Kumamoto T., Edelbaum D., Morita A., Bergstresser P.R., Takashima A.; "Identification of a novel, dendritic cell-associated molecule, dectin-1, by subtractive cDNA cloning."; J. Biol. Chem. 275:20157-20167(2000).
[2]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. DOI=10.1038/35092620; PubMed=11544516 [NCBI, ExPASy, EBI, Israel, Japan] Brown G.D., Gordon S.; "Immune recognition. A new receptor for beta-glucans."; Nature 413:36-37(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Czech II; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	FUNCTION, PHOSPHORYLATION, AND TISSUE SPECIFICITY. DOI=10.1084/jem.20021787; PubMed=12719479 [NCBI, ExPASy, EBI, Israel, Japan] Gantner B.N., Simmons R.M., Canavera S.J., Akira S., Underhill D.M.; "Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2."; J. Exp. Med. 197:1107-1117(2003).
[5]	FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-221; HIS-223 AND CYS-232. DOI=10.1128/IAI.72.7.4159-4171.2004; PubMed=15213161 [NCBI, ExPASy, EBI, Israel, Japan] Adachi Y., Ishii T., Ikeda Y., Hoshino A., Tamura H., Aketagawa J., Tanaka S., Ohno N.; "Characterization of beta-glucan recognition site on C-type lectin, dectin 1."; Infect. Immun. 72:4159-4171(2004).
[6]	FUNCTION. DOI=10.1038/sj.emboj.7600594; PubMed=15729357 [NCBI, ExPASy, EBI, Israel, Japan] Gantner B.N., Simmons R.M., Underhill D.M.; "Dectin-1 mediates macrophage recognition of Candida albicans yeast but not filaments."; EMBO J. 24:1277-1286(2005).
[7]	FUNCTION. DOI=10.1016/j.immuni.2005.03.004; PubMed=15845454 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Syk-dependent cytokine induction by Dectin-1 reveals a novel pattern recognition pathway for C type lectins."; Immunity 22:507-517(2005).
[8]	FUNCTION. DOI=10.1128/IAI.73.3.1553-1560.2005; PubMed=15731053 [NCBI, ExPASy, EBI, Israel, Japan] Viriyakosol S., Fierer J., Brown G.D., Kirkland T.N.; "Innate immunity to the pathogenic fungus Coccidioides posadasii is dependent on Toll-like receptor 2 and Dectin-1."; Infect. Immun. 73:1553-1560(2005).
[9]	FUNCTION. DOI=10.1182/blood-2006-05-024406; PubMed=16825490 [NCBI, ExPASy, EBI, Israel, Japan] Yadav M., Schorey J.S.; "The beta-glucan receptor dectin-1 functions together with TLR2 to mediate macrophage activation by mycobacteria."; Blood 108:3168-3175(2006).
[10]	X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 113-244, AND SUBUNIT. Brown J., O'Callaghan C.A., Marshall A.S.J., Gilbert R.J.C., Siebold C., Gordon S., Brown G.D., Jones E.Y.; "Structure and function of the fungal beta-glucan binding immune receptor dectin-1."; Submitted (AUG-2006) to the PDB data bank.

Comments

FUNCTION: 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.
SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. Note=Enriched on zymosan phagosomes. Enrichment does not depend on opsonization.
TISSUE SPECIFICITY: 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.
PTM: N-glycosylated.
PTM: Phosphorylated on tyrosine residues in response to glucan binding.
SIMILARITY: Contains 1 C-type lectin domain.
WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; Note=Mouse recombinant soluble Dectin-1 CTLD from insect cells origin; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_793";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF262985; AAF72710.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY534909; AAS37670.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027742; AAH27742.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00119904; -.

NP_064392.2; -.

3D structure databases

PDB

2BPD; X-ray; 1.50 A; A/B=113-244.	[ExPASy / RCSB / EBI]
2BPE; X-ray; 2.25 A; A/B=113-244.	[ExPASy / RCSB / EBI]
2BPH; X-ray; 2.20 A; A/B=113-244.	[ExPASy / RCSB / EBI]
2CL8; X-ray; 2.80 A; A/B=113-244.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2BPD; -.
2BPE; -.
2BPH; -.
2CL8; -.

ModBase

Q6QLQ4.

PTM databases

PhosphoSite

Q6QLQ4; -.

Organism-specific databases

MGI

MGI:1861431; Clec7a.

Gene expression databases

ArrayExpress

Q6QLQ4; -.

Bgee

Q6QLQ4; -.

CleanEx

MM_CLEC7A; -.

Ontologies

GO:0009897;	Cellular component: external side of plasma membrane (inferred from direct assay from MGI).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0001846;	Molecular function: opsonin binding (inferred from direct assay from MGI).
GO:0005529;	Molecular function: sugar binding (inferred from electronic annotation from UniProtKB-KW).
GO:0001874;	Molecular function: zymosan receptor activity (inferred from direct assay from MGI).
GO:0002752;	Biological process: cell surface pattern recognition receptor signaling pathway (inferred from direct assay from MGI).
GO:0016337;	Biological process: cell-cell adhesion (inferred from direct assay from MGI).
GO:0001879;	Biological process: detection of yeast (inferred from direct assay from MGI).
GO:0006954;	Biological process: inflammatory response (inferred from electronic annotation from UniProtKB-KW).
GO:0045087;	Biological process: innate immune response (inferred from electronic annotation from UniProtKB-KW).
GO:0006911;	Biological process: phagocytosis, engulfment (inferred from direct assay from MGI).
GO:0006910;	Biological process: phagocytosis, recognition (inferred from direct assay from MGI).
GO:0050766;	Biological process: positive regulation of phagocytosis (inferred from direct assay from MGI).
GO:0032760;	Biological process: positive regulation of tumor necrosis factor production (inferred from direct assay from MGI).
GO:0002238;	Biological process: response to molecule of fungal origin (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR002353; AntifreezeII.
IPR001304; C-type_lectin.
IPR018378; C-type_lectin_CS.
IPR013600; Ly49.
Graphical view of domain structure.

Pfam

PF00059; Lectin_C; 1.
PF08391; Ly49; 1.
Pfam graphical view of domain structure.

PRINTS

PR00356; ANTIFREEZEII.

SMART

SM00034; CLECT; 1.
SMART graphical view of domain structure.

PROSITE

PS00615; C_TYPE_LECTIN_1; FALSE_NEG.
PS50041; C_TYPE_LECTIN_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSMUSG00000079293; Mus musculus. [Contig view]

GeneID

56644; -.

KEGG

mmu:56644; -.

Phylogenomic databases

HOVERGEN

Q6QLQ4; -.

Other

SOURCE

Clec7a; Mus musculus.

ProtoNet

Q6QLQ4.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Disulfide bond; Glycoprotein; Immune response; Inflammatory response; Innate immunity; Lectin; Membrane; Phosphoprotein; Receptor; Signal-anchor; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 244`	`244`	`C-type lectin domain family 7 member A.`	`PRO_0000269493`
`TOPO_DOM`	`1 49`	`49`	`Cytoplasmic (Potential).`
`TRANSMEM`	`50 70`	`21`	`Signal-anchor for type II membrane protein (Potential).`
`TOPO_DOM`	`71 244`	`174`	`Extracellular (Potential).`
`DOMAIN`	`126 241`	`116`	`C-type lectin.`
`MOTIF`	`15 18`	`4`	`ITAM-like.`
`MOD_RES`	`15 15`		`Phosphotyrosine (Probable).`
`CARBOHYD`	`185 185`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`233 233`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`147 240`		`By similarity.`
`DISULFID`	`219 232`		`By similarity.`
`MUTAGEN`	`221 221`		`W->A: Loss of glucan binding. Abolishes activation of NF-kappa-B.`
`MUTAGEN`	`223 223`		`H->A: Loss of glucan binding. Abolishes activation of NF-kappa-B.`
`MUTAGEN`	`232 232`		`C->A: Abolishes cell surface expression.`
`CONFLICT`	`83 83`		`N -> S (in Ref. 2; AAS37670).`
`CONFLICT`	`85 85`		`L -> P (in Ref. 3; AAH27742).`
`CONFLICT`	`118 118`		`S -> P (in Ref. 3; AAH27742).`
`CONFLICT`	`124 124`		`I -> T (in Ref. 3; AAH27742).`
`CONFLICT`	`174 176`		`RIN -> HIT (in Ref. 3; AAH27742).`
`CONFLICT`	`209 209`		`T -> A (in Ref. 2; AAS37670).`
`CONFLICT`	`210 210`		`V -> A (in Ref. 3; AAH27742).`
`STRAND`	`124 126`	`3`
`STRAND`	`129 138`	`10`
`HELIX`	`140 149`	`10`
`HELIX`	`160 170`	`11`
`HELIX`	`171 173`	`3`
`STRAND`	`176 183`	`8`
`STRAND`	`201 203`	`3`
`STRAND`	`219 223`	`5`
`STRAND`	`226 230`	`5`
`STRAND`	`236 242`	`7`

Sequence information

Length: 244 AA [This is the length of the unprocessed precursor]

Molecular weight: 27621 Da [This is the MW of the unprocessed precursor]

CRC64: 55A71C04E68CA002 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKYHSHIENL DEDGYTQLDF STQDIHKRPR GSEKGSRAPS SPWRPIAVGL GILCFVVVVV 

        70         80         90        100        110        120 
AAVLGALAFW RHNSGRNPEE KDNFLSRNKE NHKPTESSLD EKVAPSKASQ TTGGFSQSCL 

       130        140        150        160        170        180 
PNWIMHGKSC YLFSFSGNSW YGSKRHCSQL GAHLLKIDNS KEFEFIESQT SSHRINAFWI 

       190        200        210        220        230        240 
GLSRNQSEGP WFWEDGSAFF PNSFQVRNTV PQESLLHNCV WIHGSEVYNQ ICNTSSYSIC 


EKEL

Q6QLQ4 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools