CLC4E_RAT
ID CLC4E_RAT Reviewed; 215 AA.
AC Q67EQ1; Q56TZ4;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=C-type lectin domain family 4 member E;
DE AltName: Full=C-type lectin superfamily member 9;
DE AltName: Full=Macrophage-inducible C-type lectin {ECO:0000303|PubMed:23921530};
DE Short=Mincle {ECO:0000303|PubMed:23921530};
GN Name=Clec4e {ECO:0000303|PubMed:23921530};
GN Synonyms=Clecsf9, Mincle {ECO:0000303|PubMed:23921530};
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=Lewis;
RA Lorentzen J.C., Flornes L.M., Dissen E., Fossum S.R.;
RT "Genes encoding lectin-like receptors are associated with arthritis in the
RT rat.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT, IDENTIFICATION IN COMPLEX WITH CLEC4D AND FCER1G, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
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 abnormal self and pathogen-
CC associated molecular patterns (PAMPs) of bacteria and fungi. The PAMPs
CC notably include mycobacterial trehalose 6,6'-dimycolate (TDM), a cell
CC wall glycolipid with potent adjuvant immunomodulatory functions.
CC Interacts with signaling adapter Fc receptor gamma chain/FCER1G to form
CC a functional complex in myeloid cells. Binding of mycobacterial
CC trehalose 6,6'-dimycolate (TDM) 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 (Th1)
CC and T-helper 17 (Th17) cell subtypes. Also recognizes alpha-mannose
CC residues on pathogenic fungi of the genus Malassezia and mediates
CC macrophage activation. Through recognition of DAMPs released upon
CC nonhomeostatic cell death, enables immune sensing of damaged self and
CC promotes inflammatory cell infiltration into the damaged tissue.
CC {ECO:0000250|UniProtKB:Q9R0Q8}.
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with
CC signaling adapter Fc receptor gamma chain/FCER1G to form a functional
CC complex; the interaction is direct (By similarity). Alternatively, acts
CC as a bridge for interaction between CLEC4D and FCER1G. A heterodimer of
CC CLEC4E and CLEC4D associates with signaling adapter Fc receptor gamma
CC chain/FCER1G to form a functional complex (PubMed:23921530). Interacts
CC with SAP130 nuclear protein that is released from necrotic cells; the
CC interaction is direct (By similarity). {ECO:0000250|UniProtKB:Q9R0Q8,
CC ECO:0000250|UniProtKB:Q9ULY5, ECO:0000269|PubMed:23921530}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23921530};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9R0Q8}.
CC Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q9R0Q8}.
CC -!- TISSUE SPECIFICITY: Expressed in dendritic cells, macrophages,
CC neutrophils and in B-cells. {ECO:0000269|PubMed:15368084,
CC ECO:0000269|PubMed:23921530}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Mincle;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_167";
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DR EMBL; AY363175; AAR18685.1; -; mRNA.
DR EMBL; AY581049; AAT92025.1; -; mRNA.
DR RefSeq; NP_001005897.1; NM_001005897.1.
DR AlphaFoldDB; Q67EQ1; -.
DR SMR; Q67EQ1; -.
DR STRING; 10116.ENSRNOP00000013562; -.
DR GlyGen; Q67EQ1; 1 site.
DR iPTMnet; Q67EQ1; -.
DR PhosphoSitePlus; Q67EQ1; -.
DR PaxDb; Q67EQ1; -.
DR GeneID; 450223; -.
DR KEGG; rno:450223; -.
DR UCSC; RGD:1359298; rat.
DR CTD; 26253; -.
DR RGD; 1359298; Clec4e.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q67EQ1; -.
DR OrthoDB; 1118305at2759; -.
DR PhylomeDB; Q67EQ1; -.
DR Reactome; R-RNO-5621480; Dectin-2 family.
DR PRO; PR:Q67EQ1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
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:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0030670; C:phagocytic vesicle membrane; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0051861; F:glycolipid binding; ISS:UniProtKB.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; 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; 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 1: Evidence at protein level;
KW Calcium; Cell membrane; Cell projection; Disulfide bond; Glycoprotein;
KW Immunity; Innate immunity; Lectin; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..215
FT /note="C-type lectin domain family 4 member E"
FT /id="PRO_0000046621"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..46
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 88..207
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 170..172
FT /note="Confers specificity for glucose/mannose-type
FT carbohydrates"
FT /evidence="ECO:0000250|UniProtKB:Q9ULY5"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULY5"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULY5"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULY5"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9ULY5"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9ULY5"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9ULY5"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9ULY5"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULY5"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 109..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 180..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 215 AA; 24911 MW; 417871E615D2A7F9 CRC64;
MNSTKSPASH HTERECFKNS QVLSWTMAGA SILFLSVCFI TRCVVTYHSF QIYGQKKLQP
HKTIKELSCY LEASGSVKNC CPLNWKHFQS SCYFFSTTTL SWLSSLKNCS DMGAHLVVIN
TWEEQEFLFR TKPRKKEFYI GLTDQVVEGQ WRWVDDTPFT ESLSFWDAGE PNNIVFVEDC
ATMRDSSNPR KNWNDVSCFF SMPWICEMPE ISPLD
