CLC7A_BOVIN
ID CLC7A_BOVIN Reviewed; 247 AA.
AC Q49BZ4; Q3ZCG4; Q49BZ5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=C-type lectin domain family 7 member A;
DE AltName: Full=Dendritic cell-associated C-type lectin 1;
DE Short=DC-associated C-type lectin 1;
DE Short=Dectin-1;
DE AltName: CD_antigen=CD369;
GN Name=CLEC7A; Synonyms=DECTIN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=16797084; DOI=10.1016/j.vetimm.2006.04.007;
RA Willcocks S., Yamakawa Y., Stalker A., Coffey T.J., Goldammer T.,
RA Werling D.;
RT "Identification and gene expression of the bovine C-type lectin Dectin-1.";
RL Vet. Immunol. Immunopathol. 113:234-242(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lectin that functions as pattern recognizing receptor (PRR)
CC specific for beta-1,3-linked and beta-1,6-linked glucans, which
CC constitute cell wall constituents from pathogenic bacteria and fungi.
CC Necessary for the TLR2-mediated inflammatory response and activation of
CC NF-kappa-B: upon beta-glucan binding, recruits SYK via its ITAM motif
CC and promotes a signaling cascade that activates some CARD domain-BCL10-
CC MALT1 (CBM) signalosomes, leading to the activation of NF-kappa-B and
CC MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which
CC stimulate expression of genes encoding pro-inflammatory cytokines and
CC chemokines. Enhances cytokine production in macrophages and dendritic
CC cells. Mediates production of reactive oxygen species in the cell.
CC Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way
CC that does not involve their surface glycans and plays a role in T-cell
CC activation. Stimulates T-cell proliferation. Induces phosphorylation of
CC SCIMP after binding beta-glucans. {ECO:0000250|UniProtKB:Q6QLQ4}.
CC -!- SUBUNIT: Homodimer. Interacts with SYK; participates in leukocyte
CC activation in presence of fungal pathogens.
CC {ECO:0000250|UniProtKB:Q6QLQ4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6QLQ4};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6QLQ4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q49BZ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q49BZ4-2; Sequence=VSP_022047;
CC -!- TISSUE SPECIFICITY: Detected in bone marrow, monocytes, macrophages,
CC dendritic cells and natural killer cells.
CC {ECO:0000269|PubMed:16797084}.
CC -!- PTM: Phosphorylated on tyrosine residues in response to beta-glucan
CC binding. {ECO:0000250|UniProtKB:Q6QLQ4}.
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DR EMBL; AY937382; AAY22120.1; -; mRNA.
DR EMBL; AY937383; AAY22121.1; -; mRNA.
DR EMBL; BC102340; AAI02341.1; -; mRNA.
DR RefSeq; NP_001027022.1; NM_001031852.1. [Q49BZ4-1]
DR AlphaFoldDB; Q49BZ4; -.
DR SMR; Q49BZ4; -.
DR STRING; 9913.ENSBTAP00000019331; -.
DR PaxDb; Q49BZ4; -.
DR GeneID; 532865; -.
DR KEGG; bta:532865; -.
DR CTD; 64581; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q49BZ4; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001872; F:(1->3)-beta-D-glucan binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISS:UniProtKB.
DR GO; GO:0061760; P:antifungal innate immune response; ISS:UniProtKB.
DR GO; GO:0071226; P:cellular response to molecule of fungal origin; ISS:UniProtKB.
DR GO; GO:0016046; P:detection of fungus; IBA:GO_Central.
DR GO; GO:0032491; P:detection of molecule of fungal origin; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0051712; P:positive regulation of killing of cells of another organism; IBA:GO_Central.
DR GO; GO:0051251; P:positive regulation of lymphocyte activation; IBA:GO_Central.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; ISS:UniProtKB.
DR GO; GO:0090303; P:positive regulation of wound healing; IBA:GO_Central.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR042808; CLEC7A.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
DR PANTHER; PTHR47218; PTHR47218; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunity; Inflammatory response; Innate immunity; Lectin; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..247
FT /note="C-type lectin domain family 7 member A"
FT /id="PRO_0000269490"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 127..242
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 81..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 15..18
FT /note="ITAM-like"
FT BINDING 146..153
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT BINDING 159
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT BINDING 163
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT BINDING 195
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT BINDING 242
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 148..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 220..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 69..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16797084, ECO:0000303|Ref.2"
FT /id="VSP_022047"
FT CONFLICT 235
FT /note="V -> A (in Ref. 1; AAY22120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 27760 MW; 02F8D1AD5332E4AC CRC64;
MEYQSSVENL DEDGYTQLDF SSRNITRRSV VSEKGLCAAS SHWRLIAVTL GILCSVMLVI
TVVLSTSGIW RSSSGNNLLK SDSFPSRNKD NQSQPTQSSL EDSVIPTKAL TTTGVFSSSC
PPNWITHEDS CYLFSTLLDS WDGSKRQCFQ LGSHLLKIDS SKELEFISRQ VSSQPDHSFW
IGLSRRQTEE PWLWEDGSTL LSNLFQIRST VTEKDSSHNC AWIHVSDIYD QLCSVHSYSI
CEKKLSV
