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 23-FEB-2022, entry version 158. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q9ULY5; -. DR BioGRID; 117639; 72. 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 GlyGen; Q9ULY5; 2 sites. DR iPTMnet; Q9ULY5; -. DR PhosphoSitePlus; Q9ULY5; -. DR BioMuta; CLEC4E; -. DR DMDM; 59797976; -. DR EPD; Q9ULY5; -. DR MassIVE; Q9ULY5; -. DR PaxDb; Q9ULY5; -. DR PeptideAtlas; Q9ULY5; -. DR PRIDE; Q9ULY5; -. DR ProteomicsDB; 85152; -. DR Antibodypedia; 23066; 305 antibodies from 25 providers. DR DNASU; 26253; -. DR Ensembl; ENST00000299663; ENSP00000299663; ENSG00000166523. 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 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; FWICEMP; -. DR OrthoDB; 1118305at2759; -. DR PhylomeDB; Q9ULY5; -. DR TreeFam; TF333341; -. DR PathwayCommons; Q9ULY5; -. DR Reactome; R-HSA-5621480; Dectin-2 family. DR SignaLink; Q9ULY5; -. DR BioGRID-ORCS; 26253; 4 hits in 1024 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 128 other 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:0006955; P:immune response; IBA:GO_Central. 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; -; 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 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 METAL 117 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000269|PubMed:24101491" FT METAL 119 FT /note="Calcium 1" FT /evidence="ECO:0000269|PubMed:24101491" FT METAL 123 FT /note="Calcium 1" FT /evidence="ECO:0000269|PubMed:24101491" FT METAL 169 FT /note="Calcium 2" FT /evidence="ECO:0000269|PubMed:24101491" FT METAL 171 FT /note="Calcium 2" FT /evidence="ECO:0000269|PubMed:24101491" FT METAL 193 FT /note="Calcium 2" FT /evidence="ECO:0000269|PubMed:24101491" FT METAL 194 FT /note="Calcium 2; via carbonyl oxygen" FT /evidence="ECO:0000269|PubMed:24101491" FT METAL 206 FT /note="Calcium 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 //