ID CLC4E_HUMAN Reviewed; 219 AA.
AC Q9ULY5; B2R6Q6;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 169.
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:24101491};
DE Short=MINCLE {ECO:0000303|PubMed:24101491};
GN Name=CLEC4E {ECO:0000303|PubMed:24101491, ECO:0000312|HGNC:HGNC:14555};
GN Synonyms=CLECSF9, MINCLE {ECO:0000303|PubMed:24101491};
GN ORFNames=UNQ218/PRO244;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Monocytic leukemia;
RX PubMed=10528209;
RA Matsumoto M., Shimada T., Kaisho T., Sanjo H., Tanaka T., Copeland N.G.,
RA Gilbert D.J., Jenkins N.A., Akira S.;
RT "A novel LPS-inducible C-type lectin is a transcriptional target of NF-IL6
RT in macrophages.";
RL J. Immunol. 163:5039-5048(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION AS RECEPTOR FOR CANDIDA ALBICANS, AND SUBUNIT.
RX PubMed=18509109; DOI=10.1093/glycob/cwn046;
RA Bugarcic A., Hitchens K., Beckhouse A.G., Wells C.A., Ashman R.B.,
RA Blanchard H.;
RT "Human and mouse macrophage-inducible C-type lectin (Mincle) bind Candida
RT albicans.";
RL Glycobiology 18:679-685(2008).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18490740; DOI=10.4049/jimmunol.180.11.7404;
RA Wells C.A., Salvage-Jones J.A., Li X., Hitchens K., Butcher S.,
RA Murray R.Z., Beckhouse A.G., Lo Y.L., Manzanero S., Cobbold C.,
RA Schroder K., Ma B., Orr S., Stewart L., Lebus D., Sobieszczuk P.,
RA Hume D.A., Stow J., Blanchard H., Ashman R.B.;
RT "The macrophage-inducible C-type lectin, mincle, is an essential component
RT of the innate immune response to Candida albicans.";
RL J. Immunol. 180:7404-7413(2008).
RN [9]
RP INTERACTION WITH FCER1G.
RX PubMed=18776906; DOI=10.1038/ni.1651;
RA Yamasaki S., Ishikawa E., Sakuma M., Hara H., Ogata K., Saito T.;
RT "Mincle is an ITAM-coupled activating receptor that senses damaged cells.";
RL Nat. Immunol. 9:1179-1188(2008).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23602766; DOI=10.1016/j.immuni.2013.03.010;
RA Miyake Y., Toyonaga K., Mori D., Kakuta S., Hoshino Y., Oyamada A.,
RA Yamada H., Ono K., Suyama M., Iwakura Y., Yoshikai Y., Yamasaki S.;
RT "C-type lectin MCL is an FcRgamma-coupled receptor that mediates the
RT adjuvanticity of mycobacterial cord factor.";
RL Immunity 38:1050-1062(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 74-219 IN COMPLEX WITH CALCIUM,
RP FUNCTION, MUTAGENESIS OF 169-GLU--ASN-171; ASN-172; ARG-183 AND
RP 198-PHE-LEU-199, SUBCELLULAR LOCATION, AND MOTIF.
RX PubMed=24101491; DOI=10.1073/pnas.1312649110;
RA Furukawa A., Kamishikiryo J., Mori D., Toyonaga K., Okabe Y., Toji A.,
RA Kanda R., Miyake Y., Ose T., Yamasaki S., Maenaka K.;
RT "Structural analysis for glycolipid recognition by the C-type lectins
RT Mincle and MCL.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:17438-17443(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
CC (PubMed:18509109, PubMed:23602766). The PAMPs notably include
CC mycobacterial trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid
CC with potent adjuvant immunomodulatory functions (PubMed:23602766,
CC PubMed:24101491). Interacts with signaling adapter Fc receptor gamma
CC chain/FCER1G to form a functional complex in myeloid cells (By
CC similarity). Binding of mycobacterial trehalose 6,6'-dimycolate (TDM)
CC to this receptor complex leads to phosphorylation of the immunoreceptor
CC tyrosine-based activation motif (ITAM) of FCER1G, triggering activation
CC of SYK, CARD9 and NF-kappa-B, consequently driving maturation of
CC antigen-presenting cells and shaping antigen-specific priming of T-
CC cells toward effector T-helper 1 and T-helper 17 cell subtypes (By
CC similarity). Also recognizes alpha-mannose residues on pathogenic fungi
CC of the genus Malassezia and mediates macrophage activation (By
CC similarity). Through recognition of DAMPs released upon nonhomeostatic
CC cell death, enables immune sensing of damaged self and promotes
CC inflammatory cell infiltration into the damaged tissue (By similarity).
CC {ECO:0000250|UniProtKB:Q9R0Q8, ECO:0000269|PubMed:18509109,
CC ECO:0000269|PubMed:23602766, ECO:0000269|PubMed:24101491}.
CC -!- SUBUNIT: Monomer and homodimer (PubMed:18509109). 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 FCER1G to form a functional complex
CC (By similarity). Interacts with SAP130 nuclear protein that is released
CC from necrotic cells; the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:Q67EQ1, ECO:0000250|UniProtKB:Q9R0Q8,
CC ECO:0000269|PubMed:18509109}.
CC -!- INTERACTION:
CC Q9ULY5; Q07325: CXCL9; NbExp=3; IntAct=EBI-12807010, EBI-3911467;
CC Q9ULY5; Q92520: FAM3C; NbExp=3; IntAct=EBI-12807010, EBI-2876774;
CC Q9ULY5; Q16617: NKG7; NbExp=4; IntAct=EBI-12807010, EBI-3919611;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18490740,
CC ECO:0000305|PubMed:24101491}; Single-pass type II membrane protein
CC {ECO:0000305}. Cell projection, phagocytic cup
CC {ECO:0000250|UniProtKB:Q9R0Q8}.
CC -!- TISSUE SPECIFICITY: Expressed in monocytes and macrophages.
CC {ECO:0000269|PubMed:23602766}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Mincle;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_00134";
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DR EMBL; AB024718; BAA83755.1; -; mRNA.
DR EMBL; AY358499; AAQ88863.1; -; mRNA.
DR EMBL; AK312671; BAG35553.1; -; mRNA.
DR EMBL; AC092746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88618.1; -; Genomic_DNA.
DR EMBL; BC000715; AAH00715.1; -; mRNA.
DR CCDS; CCDS8594.1; -.
DR RefSeq; NP_055173.1; NM_014358.3.
DR PDB; 3WH2; X-ray; 1.30 A; A=74-219.
DR PDB; 3WH3; X-ray; 1.32 A; A=74-219.
DR PDBsum; 3WH2; -.
DR PDBsum; 3WH3; -.
DR AlphaFoldDB; Q9ULY5; -.
DR SMR; Q9ULY5; -.
DR BioGRID; 117639; 365.
DR CORUM; Q9ULY5; -.
DR IntAct; Q9ULY5; 6.
DR STRING; 9606.ENSP00000299663; -.
DR ChEMBL; CHEMBL4105898; -.
DR DrugBank; DB04540; Cholesterol.
DR GuidetoPHARMACOLOGY; 2929; -.
DR UniLectin; Q9ULY5; -.
DR GlyCosmos; Q9ULY5; 2 sites, No reported glycans.
DR GlyGen; Q9ULY5; 2 sites.
DR iPTMnet; Q9ULY5; -.
DR PhosphoSitePlus; Q9ULY5; -.
DR BioMuta; CLEC4E; -.
DR DMDM; 59797976; -.
DR EPD; Q9ULY5; -.
DR MassIVE; Q9ULY5; -.
DR PaxDb; 9606-ENSP00000299663; -.
DR PeptideAtlas; Q9ULY5; -.
DR ProteomicsDB; 85152; -.
DR Antibodypedia; 23066; 367 antibodies from 28 providers.
DR DNASU; 26253; -.
DR Ensembl; ENST00000299663.8; ENSP00000299663.3; ENSG00000166523.8.
DR GeneID; 26253; -.
DR KEGG; hsa:26253; -.
DR MANE-Select; ENST00000299663.8; ENSP00000299663.3; NM_014358.4; NP_055173.1.
DR UCSC; uc001quo.2; human.
DR AGR; HGNC:14555; -.
DR CTD; 26253; -.
DR DisGeNET; 26253; -.
DR GeneCards; CLEC4E; -.
DR HGNC; HGNC:14555; CLEC4E.
DR HPA; ENSG00000166523; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 609962; gene.
DR neXtProt; NX_Q9ULY5; -.
DR OpenTargets; ENSG00000166523; -.
DR PharmGKB; PA26586; -.
DR VEuPathDB; HostDB:ENSG00000166523; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000160666; -.
DR HOGENOM; CLU_049894_7_5_1; -.
DR InParanoid; Q9ULY5; -.
DR OMA; CPLNWEH; -.
DR OrthoDB; 2881452at2759; -.
DR PhylomeDB; Q9ULY5; -.
DR TreeFam; TF333341; -.
DR PathwayCommons; Q9ULY5; -.
DR Reactome; R-HSA-5621480; Dectin-2 family.
DR SignaLink; Q9ULY5; -.
DR BioGRID-ORCS; 26253; 10 hits in 1138 CRISPR screens.
DR GenomeRNAi; 26253; -.
DR Pharos; Q9ULY5; Tchem.
DR PRO; PR:Q9ULY5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9ULY5; Protein.
DR Bgee; ENSG00000166523; Expressed in monocyte and 116 other cell types or tissues.
DR ExpressionAtlas; Q9ULY5; baseline and differential.
DR Genevisible; Q9ULY5; HS.
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:0016020; C:membrane; IDA: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; IDA: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; IDA:UniProtKB.
DR GO; GO:0061760; P:antifungal innate immune response; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0038094; P:Fc-gamma receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0002292; P:T cell differentiation involved in immune response; IEA:Ensembl.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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 PANTHER; PTHR22802:SF402; C-TYPE LECTIN DOMAIN FAMILY 4 MEMBER E; 1.
DR PANTHER; PTHR22802; C-TYPE LECTIN SUPERFAMILY MEMBER; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Immunity; Innate immunity; Lectin; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..219
FT /note="C-type lectin domain family 4 member E"
FT /id="PRO_0000046619"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 87..206
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 169..171
FT /note="Confers specificity for glucose/mannose-type
FT carbohydrates"
FT /evidence="ECO:0000303|PubMed:24101491"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24101491"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24101491"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24101491"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24101491"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24101491"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24101491"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24101491"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24101491"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 108..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 179..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MUTAGEN 169..171
FT /note="EPN->QPD,EPD: Impairs binding to trehalose-6,6'-
FT dimycolate."
FT /evidence="ECO:0000269|PubMed:24101491"
FT MUTAGEN 172
FT /note="N->Q: Impairs trehalose-6,6'-dimycolate (TDM)-
FT induced NF-kappa-B activation."
FT /evidence="ECO:0000269|PubMed:24101491"
FT MUTAGEN 183
FT /note="R->V: Reduces trehalose-6,6'-dimycolate (TDM)-
FT induced NF-kappa-B activation."
FT /evidence="ECO:0000269|PubMed:24101491"
FT MUTAGEN 198..199
FT /note="FL->AA: Reduces trehalose-6,6'-dimycolate (TDM)-
FT induced NF-kappa-B activation."
FT /evidence="ECO:0000269|PubMed:24101491"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3WH2"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3WH2"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:3WH2"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:3WH2"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:3WH2"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3WH2"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:3WH2"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:3WH2"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:3WH2"
SQ SEQUENCE 219 AA; 25073 MW; C5D48DD7427D7FC5 CRC64;
MNSSKSSETQ CTERGCFSSQ MFLWTVAGIP ILFLSACFIT RCVVTFRIFQ TCDEKKFQLP
ENFTELSCYN YGSGSVKNCC PLNWEYFQSS CYFFSTDTIS WALSLKNCSA MGAHLVVINS
QEEQEFLSYK KPKMREFFIG LSDQVVEGQW QWVDGTPLTK SLSFWDVGEP NNIATLEDCA
TMRDSSNPRQ NWNDVTCFLN YFRICEMVGI NPLNKGKSL
//
