CLC4D_RAT
ID CLC4D_RAT Reviewed; 218 AA.
AC Q69FH1; Q2TUL6;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=C-type lectin domain family 4 member D;
DE AltName: Full=C-type lectin superfamily member 8;
DE AltName: CD_antigen=CD368;
GN Name=Clec4d; Synonyms=Clecsf8, Mcl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=PVG;
RX PubMed=15368084; DOI=10.1007/s00251-004-0714-x;
RA Flornes L.M., Bryceson Y.T., Spurkland A., Lorentzen J.C., Dissen E.,
RA Fossum S.;
RT "Identification of lectin-like receptors expressed by antigen presenting
RT cells and neutrophils and their mapping to a novel gene complex.";
RL Immunogenetics 56:506-517(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DA;
RA Flornes L.M., Dissen E., Fossum S.;
RT "Genes encoding lectin-like receptors associate with arthritis in the
RT rat.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=23921530; DOI=10.1002/eji.201343752;
RA Lobato-Pascual A., Saether P.C., Fossum S., Dissen E., Daws M.R.;
RT "Mincle, the receptor for mycobacterial cord factor, forms a functional
RT receptor complex with MCL and FcepsilonRI-gamma.";
RL Eur. J. Immunol. 43:3167-3174(2013).
CC -!- FUNCTION: Calcium-dependent lectin that acts as a pattern recognition
CC receptor (PRR) of the innate immune system: recognizes damage-
CC associated molecular patterns (DAMPs) of pathogen-associated molecular
CC patterns (PAMPs) of bacteria and fungi. The PAMPs include alpha-mannans
CC on C.albicans hypheas and mycobacterial trehalose 6,6'-dimycolate (TDM)
CC (By similarity). Interacts with signaling adapter Fc receptor gamma
CC chain/FCER1G, likely via CLEC4E, to form a functional complex in
CC myeloid cells (PubMed:23921530). Binding of mycobacterial TDM or
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. The heterodimer formed with CLEC6A is active
CC against fungal infection. Functions as an endocytic receptor. May be
CC involved in antigen uptake at the site of infection, either for
CC clearance of the antigen, or for processing and further presentation to
CC T-cells (By similarity). {ECO:0000250|UniProtKB:Q8WXI8,
CC ECO:0000269|PubMed:23921530}.
CC -!- SUBUNIT: Heterodimer with CLEC4E; disulfide-linked (PubMed:23921530).
CC CLEC4E acts as a bridge for interaction between CLEC4D and FCER1G to
CC form a functional complex (PubMed:23921530). Heterodimer with CLEC6A;
CC this heterodimer forms a pattern recognition receptor (PRR) against
CC fungal infection (By similarity). {ECO:0000250|UniProtKB:Q8WXI8,
CC ECO:0000269|PubMed:23921530}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23921530};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in myeloid cells (dendritic cells,
CC macrophages and neutrophils) and B-cells. {ECO:0000269|PubMed:15368084,
CC ECO:0000269|PubMed:23921530}.
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DR EMBL; AY339882; AAR02097.1; -; mRNA.
DR EMBL; AY494065; AAS76661.1; -; mRNA.
DR RefSeq; NP_001003707.1; NM_001003707.1.
DR AlphaFoldDB; Q69FH1; -.
DR SMR; Q69FH1; -.
DR STRING; 10116.ENSRNOP00000013536; -.
DR GlyGen; Q69FH1; 2 sites.
DR PaxDb; Q69FH1; -.
DR GeneID; 362432; -.
DR KEGG; rno:362432; -.
DR UCSC; RGD:1303339; rat.
DR CTD; 338339; -.
DR RGD; 1303339; Clec4d.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q69FH1; -.
DR OrthoDB; 1269095at2759; -.
DR PhylomeDB; Q69FH1; -.
DR Reactome; R-RNO-5621480; Dectin-2 family.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q69FH1; -.
DR Proteomes; UP000002494; Unplaced.
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:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0034987; F:immunoglobulin receptor binding; ISO:RGD.
DR GO; GO:0005537; F:mannose 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:0002250; P:adaptive immune response; ISO:RGD.
DR GO; GO:0061760; P:antifungal innate immune response; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0038094; P:Fc-gamma receptor signaling pathway; ISO:RGD.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0030887; P:positive regulation of myeloid dendritic cell activation; ISS:UniProtKB.
DR GO; GO:0002292; P:T cell differentiation involved in immune response; ISO:RGD.
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; 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; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunity; Innate immunity; Lectin; Membrane; Metal-binding; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..218
FT /note="C-type lectin domain family 4 member D"
FT /id="PRO_0000046618"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..47
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 89..206
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI8"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI8"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI8"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 110..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 180..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 218 AA; 25312 MW; 357E411CB748B9B0 CRC64;
MWLEESQMKS KGALHPRRIP WVCAVVSISF LSACFISTCV VTHYFLLWKR GSALKFSDYH
TRLTCILEEP QPGATGGTWT CCPVSWRAFQ SNCYFALNDN QTWHESERNC SGMSSHLVTI
NTEAEQDFVT QLLDEQFSYF LGLSYEKVEG QWQWVDKTPF NPNVVFWKVG EPKDSMEEDC
VVLVYDQDKW VWNDFPCHFE MGRICKLPGA TFDWNPSK
