CLC6A_BOVIN
ID CLC6A_BOVIN Reviewed; 206 AA.
AC Q3LUH2; Q3LUH1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=C-type lectin domain family 6 member A;
DE AltName: Full=Dendritic cell-associated C-type lectin 2;
DE Short=DC-associated C-type lectin 2;
DE Short=Dectin-2;
GN Name=CLEC6A; Synonyms=DECTIN2;
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.
RX PubMed=16213030; DOI=10.1016/j.vetimm.2005.08.031;
RA Bonkobara M., Hoshino M., Yagihara H., Tamura K., Isotani M., Tanaka Y.,
RA Washizu T., Ariizumi K.;
RT "Identification and gene expression of bovine C-type lectin dectin-2.";
RL Vet. Immunol. Immunopathol. 110:179-186(2006).
CC -!- FUNCTION: Calcium-dependent lectin that acts as a pattern recognition
CC receptor (PRR) of the innate immune system: specifically recognizes and
CC binds alpha-mannans on C.albicans hypheas (By similarity). Binding of
CC C.albicans alpha-mannans to this receptor complex leads to
CC phosphorylation of the immunoreceptor tyrosine-based activation motif
CC (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B,
CC consequently driving maturation of antigen-presenting cells and shaping
CC antigen-specific priming of T-cells toward effector T-helper 1 and T-
CC helper 17 cell subtypes (By similarity). Recognizes also, in a mannose-
CC dependent manner, allergens from house dust mite and fungi, by
CC promoting cysteinyl leukotriene production. Recognizes soluble elements
CC from the eggs of Shistosoma mansoni altering adaptive immune responses
CC (By similarity). {ECO:0000250|UniProtKB:Q6EIG7,
CC ECO:0000250|UniProtKB:Q9JKF4}.
CC -!- SUBUNIT: Associated with FCER1G (By similarity). Heterodimer with
CC CLEC4D; this heterodimer forms a pattern recognition receptor (PRR)
CC against fungal infection (By similarity).
CC {ECO:0000250|UniProtKB:Q6EIG7, ECO:0000250|UniProtKB:Q9JKF4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6EIG7};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3LUH2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3LUH2-2; Sequence=VSP_041515;
CC -!- TISSUE SPECIFICITY: Expressed at the highest levels in lymph nodes, at
CC moderate levels in skin, small intestine, liver, and lung, and at lower
CC levels in abomasum and spleen, but is not in the brain. Abundantly
CC expressed by Langerhans cells compared to macrophages.
CC {ECO:0000269|PubMed:16213030}.
CC -!- DOMAIN: A short stretch of the intracellular domain (AA 8-14) proximal
CC to the transmembrane domain is required for association with Fc
CC receptor gamma chain. {ECO:0000250|UniProtKB:Q9JKF4}.
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DR EMBL; DQ176046; ABA08411.1; -; mRNA.
DR EMBL; DQ176047; ABA08412.1; -; mRNA.
DR RefSeq; NP_001029651.1; NM_001034479.1. [Q3LUH2-2]
DR AlphaFoldDB; Q3LUH2; -.
DR SMR; Q3LUH2; -.
DR STRING; 9913.ENSBTAP00000032278; -.
DR PaxDb; Q3LUH2; -.
DR Ensembl; ENSBTAT00000032346; ENSBTAP00000032279; ENSBTAG00000023635. [Q3LUH2-2]
DR GeneID; 514979; -.
DR KEGG; bta:514979; -.
DR CTD; 93978; -.
DR VEuPathDB; HostDB:ENSBTAG00000023635; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162938; -.
DR HOGENOM; CLU_049894_7_5_1; -.
DR InParanoid; Q3LUH2; -.
DR Reactome; R-BTA-5621480; Dectin-2 family.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000023635; Expressed in monocyte and 82 other tissues.
DR ExpressionAtlas; Q3LUH2; baseline and differential.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0005537; F:mannose binding; ISS:UniProtKB.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0061760; P:antifungal innate immune response; ISS:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; ISS:UniProtKB.
DR CDD; cd03590; CLECT_DC-SIGN_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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Alternative splicing; Calcium; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunity; Innate immunity; Lectin; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..206
FT /note="C-type lectin domain family 6 member A"
FT /id="PRO_0000410824"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 83..200
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 165..167
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 171
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 179
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 187..188
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 195
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..75
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7"
FT DISULFID 76..87
FT /evidence="ECO:0000250|UniProtKB:Q6EIG7,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 104..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 173..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 36..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16213030"
FT /id="VSP_041515"
SQ SEQUENCE 206 AA; 23738 MW; 6FC8B087C91AA963 CRC64;
MVREGNAESC FRMRLWCIAV LGLALLSACF IVSCVVTYYF THGNTGKRLS ELHTHHSNLT
CFSEGTRVTE KIWGCCPGTW KPFGSSCYFI SSEENFWAKS EQNCIGMGAH LVVINTETEQ
DFIIQQLNKT FSYFLGLSDP QGNGNWQWID QTPYKENVRF WHQNEPNFSA EECASVVFWD
GRGWGWNDVF CDSKRKSICE MKKIYL
