Q6QLQ4 (CLC7A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Clec7a
Synonyms:	Bgr, Clecsf12, Dectin1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Subunit structure	Homodimer Probable. Interacts with SYK; participates in leukocyte activation in presence of fungal pathogens. Ref.10
Subcellular location	Cell membrane; Single-pass type II membrane protein. Note: Enriched on zymosan phagosomes. Enrichment does not depend on opsonization. Ref.1 Ref.5
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. Ref.1 Ref.2 Ref.4
Post-translational modification	N-glycosylated. Ref.1 Phosphorylated on tyrosine residues in response to glucan binding. Ref.4
Sequence similarities	Contains 1 C-type lectin domain.

Ontologies

Keywords
Biological process	Immunity Inflammatory response Innate immunity
Cellular component	Cell membrane Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Lectin Metal-binding
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell surface pattern recognition receptor signaling pathway Inferred from direct assay. Source: MGI cell-cell adhesion Inferred from direct assay. Source: MGI detection of yeast Inferred from direct assay. Source: MGI inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW phagocytosis, engulfment Inferred from direct assay. Source: MGI phagocytosis, recognition Inferred from direct assay. Source: MGI positive regulation of phagocytosis Inferred from direct assay. Source: MGI positive regulation of tumor necrosis factor production Inferred from direct assay. Source: MGI response to molecule of fungal origin Inferred from direct assay. Source: MGI
Cellular component	external side of plasma membrane Inferred from direct assay. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	(1->3)-beta-D-glucan binding Inferred from direct assay. Source: MGI (1->3)-beta-D-glucan receptor activity Inferred from direct assay. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW opsonin binding Inferred from direct assay. Source: MGI sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 244

244

C-type lectin domain family 7 member A

PRO_0000269493

Regions

Topological domain

1 – 49

49

Cytoplasmic Potential

Transmembrane

50 – 70

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

71 – 244

174

Extracellular Potential

Domain

126 – 241

116

C-type lectin

Motif

15 – 18

4

ITAM-like

Sites

Metal binding

156

1

Divalent metal cation

Metal binding

158

1

Divalent metal cation

Metal binding

162

1

Divalent metal cation

Metal binding

241

1

Divalent metal cation

Amino acid modifications

Modified residue

15

1

Phosphotyrosine Probable

Glycosylation

185

1

N-linked (GlcNAc...) Potential

Glycosylation

233

1

N-linked (GlcNAc...) Potential

Disulfide bond

119 ↔ 130

Ref.10

Disulfide bond

147 ↔ 240

Ref.10

Disulfide bond

219 ↔ 232

Ref.10

Experimental info

Mutagenesis

221

1

W → A: Loss of glucan binding. Abolishes activation of NF-kappa-B. Ref.5

Mutagenesis

223

1

H → A: Loss of glucan binding. Abolishes activation of NF-kappa-B. Ref.5

Mutagenesis

232

1

C → A: Abolishes cell surface expression. Ref.5

Sequence conflict

83

1

N → S in AAS37670. Ref.2

Sequence conflict

85

1

L → P in AAH27742. Ref.3

Sequence conflict

118

1

S → P in AAH27742. Ref.3

Sequence conflict

124

1

I → T in AAH27742. Ref.3

Sequence conflict

174 – 176

3

RIN → HIT in AAH27742. Ref.3

Sequence conflict

209

1

T → A in AAS37670. Ref.2

Sequence conflict

210

1

V → A in AAH27742. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

244

Helix Strand Turn

Details...

Beta strand

124 – 126

3

Beta strand

129 – 138

10

Helix

140 – 149

10

Helix

160 – 170

11

Helix

171 – 173

3

Beta strand

176 – 183

8

Beta strand

201 – 203

3

Beta strand

219 – 223

5

Beta strand

226 – 230

5

Beta strand

236 – 242

7

Sequences

	Sequence		Length	Mass (Da)
	Q6QLQ4 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: 55A71C04E68CA002	FASTA	244	27,621
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10779524] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY. Strain: BALB/c. Tissue: Dendritic cell.
[2]	"Immune recognition. A new receptor for beta-glucans." Brown G.D., Gordon S. Nature 413:36-37(2001) [PubMed: 11544516] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Mammary gland.
[4]	"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: 12719479] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY.
[5]	"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: 15213161] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-221; HIS-223 AND CYS-232.
[6]	"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: 15729357] [Abstract] Cited for: FUNCTION.
[7]	"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: 15845454] [Abstract] Cited for: FUNCTION, INTERACTION WITH SYK.
[8]	"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: 15731053] [Abstract] Cited for: FUNCTION.
[9]	"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: 16825490] [Abstract] Cited for: FUNCTION.
[10]	"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: 17473009] [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.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

Mouse recombinant soluble Dectin-1 CTLD from insect cells origin

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF262985 mRNA. Translation: AAF72710.1.
AY534909 mRNA. Translation: AAS37670.1.
BC027742 mRNA. Translation: AAH27742.1.

IPI

IPI00119904.

RefSeq

NP_064392.2. NM_020008.2.

UniGene

Mm.239516.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BPD	X-ray	1.50	A/B	113-244	[»]
2BPE	X-ray	2.25	A/B	113-244	[»]
2BPH	X-ray	2.20	A/B	113-244	[»]
2CL8	X-ray	2.80	A/B	113-244	[»]

ProteinModelPortal

Q6QLQ4.

SMR

Q6QLQ4. Positions 116-244.

ModBase

Search...

Protein-protein interaction databases

STRING

Q6QLQ4.

PTM databases

PhosphoSite

Q6QLQ4.

Proteomic databases

PRIDE

Q6QLQ4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

56644.

KEGG

mmu:56644.

UCSC

uc009efu.2. mouse.

Organism-specific databases

CTD

64581.

MGI

MGI:1861431. Clec7a.

Phylogenomic databases

GeneTree

ENSGT00600000084307.

HOGENOM

HBG283212.

HOVERGEN

HBG105854.

InParanoid

Q6QLQ4.

OrthoDB

EOG4BG8X9.

Gene expression databases

ArrayExpress

Q6QLQ4.

Bgee

Q6QLQ4.

CleanEx

MM_CLEC7A.

Genevestigator

Q6QLQ4.

Family and domain databases

InterPro

IPR002353. AntifreezeII.
IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]

Gene3D

G3DSA:3.10.100.10. C-type_lectin-like. 1 hit.

KO

K10074.

Pfam

PF00059. Lectin_C. 1 hit.
[Graphical view]

PRINTS

PR00356. ANTIFREEZEII.

SMART

SM00034. CLECT. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.

PROSITE

PS00615. C_TYPE_LECTIN_1. False negative.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

CLC7A_MOUSE

Accession

Primary (citable) accession number: Q6QLQ4
Secondary accession number(s): Q8K1L4, Q9JI50

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	December 12, 2006
Last modified:	January 25, 2012
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program