ID MIC1_TOXGO Reviewed; 456 AA. AC O00834; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 12-AUG-2020, entry version 73. DE RecName: Full=Micronemal protein 1; DE Flags: Precursor; GN Name=MIC1 {ECO:0000312|EMBL:CAA96466.1}; OS Toxoplasma gondii. OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia; OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma. OX NCBI_TaxID=5811; RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA96466.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, AND MOTIF. RC STRAIN=RH {ECO:0000312|EMBL:CAA96466.1}; RX PubMed=9027753; DOI=10.1016/s0166-6851(96)02773-9; RA Fourmaux M.N., Mercereau-Puijalon O., Achbarou A., Biderre C., Briche I., RA Loyens A., Odberg-Ferragut C., Camus D., Dubremetz J.F.; RT "The MIC1 microneme protein of Toxoplasma gondii contains a duplicated RT receptor-like domain and binds to host cell surface."; RL Mol. Biochem. Parasitol. 83:201-210(1996). RN [2] {ECO:0000305} RP PROTEIN SEQUENCE OF 26-36, FUNCTION, AND INTERACTION WITH MIC4. RC STRAIN=RH {ECO:0000269|PubMed:11447133}; RX PubMed=11447133; DOI=10.1093/glycob/11.7.541; RA Lourenco E.V., Pereira S.R., Faca V.M., Coelho-Castelo A.A., Mineo J.R., RA Roque-Barreira M.-C., Greene L.J., Panunto-Castelo A.; RT "Toxoplasma gondii micronemal protein MIC1 is a lactose-binding lectin."; RL Glycobiology 11:541-547(2001). RN [3] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MIC4 AND MIC6. RC STRAIN=RH {ECO:0000269|PubMed:11157983}; RX PubMed=11157983; DOI=10.1083/jcb.152.3.563; RA Reiss M., Viebig N., Brecht S., Fourmaux M.-N., Soete M., Di Cristina M., RA Dubremetz J.F., Soldati D.; RT "Identification and characterization of an escorter for two secretory RT adhesins in Toxoplasma gondii."; RL J. Cell Biol. 152:563-578(2001). RN [4] {ECO:0000305} RP DEVELOPMENTAL STAGE. RX PubMed=12455982; DOI=10.1128/ec.1.3.329-340.2002; RA Cleary M.D., Singh U., Blader I.J., Brewer J.L., Boothroyd J.C.; RT "Toxoplasma gondii asexual development: identification of developmentally RT regulated genes and distinct patterns of gene expression."; RL Eukaryot. Cell 1:329-340(2002). RN [5] {ECO:0000305} RP SUBCELLULAR LOCATION. RX PubMed=15684324; DOI=10.1084/jem.20041672; RA Cerede O., Dubremetz J.F., Soete M., Deslee D., Vial H., Bout D., RA Lebrun M.; RT "Synergistic role of micronemal proteins in Toxoplasma gondii virulence."; RL J. Exp. Med. 201:453-463(2005). RN [6] {ECO:0000305} RP NMR RESONANCE ASSIGNMENTS. RX PubMed=15772760; DOI=10.1007/s10858-004-8237-1; RA Saouros S., Chen H.A., Simpson P., Cota E., Edwards-Jones B., RA Soldati-Favre D., Matthews S.; RT "Complete resonance assignments of the C-terminal domain from MIC1: a RT micronemal protein from Toxoplasma gondii."; RL J. Biomol. NMR 31:177-178(2005). RN [7] {ECO:0000305} RP STRUCTURE BY NMR OF 320-456, FUNCTION, INTERACTION WITH MIC4 AND MIC6, RP SUBUNIT, DOMAIN, AND DISULFIDE BOND. RX PubMed=16166092; DOI=10.1074/jbc.c500365200; RA Saouros S., Edwards-Jones B., Reiss M., Sawmynaden K., Cota E., Simpson P., RA Dowse T.J., Jakle U., Ramboarina S., Shivarattan T., Matthews S., RA Soldati-Favre D.; RT "A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 RT assists the folding, assembly, and transport of a cell adhesion complex."; RL J. Biol. Chem. 280:38583-38591(2005). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-262, DISULFIDE BONDS, DOMAIN, RP FUNCTION, AND MUTAGENESIS OF THR-126 AND THR-220. RX PubMed=17491595; DOI=10.1038/sj.emboj.7601704; RA Blumenschein T.M.A., Friedrich N., Childs R.A., Saouros S., Carpenter E.P., RA Campanero-Rhodes M.A., Simpson P., Chai W., Koutroukides T., Blackman M.J., RA Feizi T., Soldati-Favre D., Matthews S.; RT "Atomic resolution insight into host cell recognition by Toxoplasma RT gondii."; RL EMBO J. 26:2808-2820(2007). RN [9] RP STRUCTURE BY NMR OF 320-455 IN COMPLEX WITH MIC6, SUBUNIT, SUBCELLULAR RP LOCATION, DISULFIDE BOND, AND DOMAIN. RX PubMed=18818666; DOI=10.1038/embor.2008.179; RA Sawmynaden K., Saouros S., Friedrich N., Marchant J., Simpson P., RA Bleijlevens B., Blackman M.J., Soldati-Favre D., Matthews S.; RT "Structural insights into microneme protein assembly reveal a new mode of RT EGF domain recognition."; RL EMBO Rep. 9:1149-1155(2008). CC -!- FUNCTION: Adhesin. Required for attachment of the parasite to the host CC cell prior to invasion. Ensures correct folding of MIC6 and transport CC of the MIC6-MIC1-MIC4 complex into the micronemes. CC {ECO:0000269|PubMed:11157983, ECO:0000269|PubMed:11447133, CC ECO:0000269|PubMed:16166092, ECO:0000269|PubMed:17491595}. CC -!- SUBUNIT: Monomer. Interacts directly with MIC4 and MIC6. Part of the CC MIC6-MIC1-MIC4 complex. {ECO:0000269|PubMed:11157983, CC ECO:0000269|PubMed:11447133, ECO:0000269|PubMed:16166092, CC ECO:0000269|PubMed:18818666}. CC -!- INTERACTION: CC O00834; Q9XYH7: MIC6; NbExp=3; IntAct=EBI-8078093, EBI-8078076; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, microneme CC {ECO:0000269|PubMed:11157983, ECO:0000269|PubMed:15684324, CC ECO:0000269|PubMed:18818666}. CC -!- DEVELOPMENTAL STAGE: Expression is down-regulated during bradyzoite CC development. {ECO:0000269|PubMed:12455982}. CC -!- DOMAIN: The galectin-like domain has been demonstrated not to bind CC lactose, glucose, maltose, mannose, heparin, fucose, L-arabinose, N- CC acetyl-D-galactosamine, or N-acetyl-D-glucosamine. It interacts CC directly with the second and the third EGF-like domain of MIC6, and CC with part of the acidic domain. CC -!- DOMAIN: The MAR (micronemal adhesive repeat) domain was at first CC proposed to be TSR1-like (thrombospondin type 1-like repeat) by CC PubMed:9027753, but PubMed:17491595 found that this domain represents a CC previously unknown protein fold. This domain is jointly responsible for CC interacting with MIC4 and for host-cell adhesion. 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; Z71786; CAA96466.1; -; Genomic_DNA. DR PDB; 2BVB; NMR; -; A=320-456. DR PDB; 2JH1; X-ray; 1.90 A; A=17-262. DR PDB; 2JH7; X-ray; 2.07 A; A=17-262. DR PDB; 2JHD; X-ray; 2.30 A; A=17-262. DR PDB; 2K2S; NMR; -; A=320-455. DR PDB; 3F53; X-ray; 2.00 A; A=17-262. DR PDB; 3F5A; X-ray; 2.00 A; A=17-262. DR PDB; 3F5E; X-ray; 2.00 A; A=17-262. DR PDBsum; 2BVB; -. DR PDBsum; 2JH1; -. DR PDBsum; 2JH7; -. DR PDBsum; 2JHD; -. DR PDBsum; 2K2S; -. DR PDBsum; 3F53; -. DR PDBsum; 3F5A; -. DR PDBsum; 3F5E; -. DR SMR; O00834; -. DR IntAct; O00834; 1. DR MINT; O00834; -. DR TCDB; 9.B.87.3.1; the selenoprotein p receptor (selp-receptor) family. DR UniLectin; O00834; -. DR PRIDE; O00834; -. DR EvolutionaryTrace; O00834; -. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0020009; C:microneme; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.710; -; 1. DR InterPro; IPR038686; MIC1_C_sf. DR InterPro; IPR024691; MIC1_galectin-like_dom. DR InterPro; IPR019562; Micronemal-adhesive-rpt_sia-bd. DR InterPro; IPR008117; Microneme_MIC1. DR Pfam; PF10564; MAR_sialic_bdg; 2. DR Pfam; PF11476; TgMIC1; 1. DR PRINTS; PR01744; MIC1MICRNEME. PE 1: Evidence at protein level; KW 3D-structure; Cell adhesion; Cytoplasmic vesicle; KW Direct protein sequencing; Disulfide bond; Lectin; Signal; Virulence. FT SIGNAL 1..16 FT /evidence="ECO:0000255, ECO:0000312|EMBL:CAA96466.1" FT CHAIN 17..456 FT /note="Micronemal protein 1" FT /evidence="ECO:0000269|PubMed:9027753" FT /id="PRO_5000147686" FT REGION 17..262 FT /note="MAR domain" FT REGION 124..126 FT /note="Interaction with host sialylated oligosaccharide FT chains" FT REGION 216..220 FT /note="Interaction with host sialylated oligosaccharide FT chains" FT REGION 320..456 FT /note="Galectin-like" FT MOTIF 103..107 FT /note="CXXCG" FT /evidence="ECO:0000269|PubMed:9027753" FT MOTIF 193..197 FT /note="CXXCG" FT /evidence="ECO:0000269|PubMed:9027753" FT DISULFID 45..85 FT DISULFID 53..61 FT DISULFID 103..113 FT DISULFID 107..143 FT DISULFID 154..179 FT DISULFID 193..203 FT DISULFID 197..242 FT DISULFID 236..252 FT DISULFID 354..425 FT /evidence="ECO:0000269|PubMed:16166092" FT MUTAGEN 126 FT /note="T->A: Abolishes binding to host cell surface." FT /evidence="ECO:0000269|PubMed:17491595" FT MUTAGEN 220 FT /note="T->A: Abolishes binding to host cell surface." FT /evidence="ECO:0000269|PubMed:17491595" FT HELIX 36..54 FT /evidence="ECO:0000244|PDB:2JH1" FT HELIX 58..60 FT /evidence="ECO:0000244|PDB:2JH1" FT HELIX 64..66 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 67..72 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 82..87 FT /evidence="ECO:0000244|PDB:2JH1" FT HELIX 88..90 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 91..94 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 100..104 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 110..117 FT /evidence="ECO:0000244|PDB:2JH1" FT TURN 119..121 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 124..126 FT /evidence="ECO:0000244|PDB:2JH1" FT HELIX 128..142 FT /evidence="ECO:0000244|PDB:2JH1" FT HELIX 145..157 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 161..168 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 171..181 FT /evidence="ECO:0000244|PDB:2JH1" FT HELIX 182..184 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 186..194 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 198..206 FT /evidence="ECO:0000244|PDB:2JH1" FT HELIX 214..216 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 218..220 FT /evidence="ECO:0000244|PDB:2JH1" FT HELIX 222..230 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 240..243 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 246..249 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 251..254 FT /evidence="ECO:0000244|PDB:2JH1" FT STRAND 324..332 FT /evidence="ECO:0000244|PDB:2BVB" FT STRAND 337..343 FT /evidence="ECO:0000244|PDB:2BVB" FT STRAND 345..350 FT /evidence="ECO:0000244|PDB:2BVB" FT TURN 352..354 FT /evidence="ECO:0000244|PDB:2BVB" FT STRAND 356..360 FT /evidence="ECO:0000244|PDB:2BVB" FT TURN 361..364 FT /evidence="ECO:0000244|PDB:2BVB" FT STRAND 365..375 FT /evidence="ECO:0000244|PDB:2BVB" FT STRAND 377..379 FT /evidence="ECO:0000244|PDB:2BVB" FT STRAND 384..394 FT /evidence="ECO:0000244|PDB:2BVB" FT STRAND 396..398 FT /evidence="ECO:0000244|PDB:2BVB" FT STRAND 400..408 FT /evidence="ECO:0000244|PDB:2BVB" FT STRAND 411..424 FT /evidence="ECO:0000244|PDB:2BVB" FT STRAND 427..435 FT /evidence="ECO:0000244|PDB:2BVB" FT STRAND 437..439 FT /evidence="ECO:0000244|PDB:2K2S" FT STRAND 441..446 FT /evidence="ECO:0000244|PDB:2BVB" FT TURN 453..455 FT /evidence="ECO:0000244|PDB:2BVB" SQ SEQUENCE 456 AA; 48672 MW; 3F1255FC0C587AF7 CRC64; MGQALFLTVL LPVLFGVGPE AYGEASHSHS PASGRYIQQM LDQRCQEIAA ELCQSGLRKM CVPSSRIVAR NAVGITHQNT LQWRCFDTAS LLESNQENNG VNCVDDCGHT IPCPGGVHRQ NSNHATRHEI LSKLVEEGVQ RFCSPYQASA NKYCNDKFPG TIARRSKGFG NNVEVAWRCY EKASLLYSVY AECASNCGTT WYCPGGRRGT STELDKRHYT EEEGIRQAIG SVDSPCSEVE VCLPKDENPP LCLDESGQIS RTGGGPPSQP PEMQQPADRS DERGGGKEQS PGGEAQPDHP TKGGNIDLPE KSTSPEKTPK TEIHGDSTKA TLEEGQQLTL TFISTKLDVA VGSCHSLVAN FLDGFLKFQT GSNSAFDVVE VEEPAGPAVL TIGLGHKGRL AVVLDYTRLN AALGSAAYVV EDSGCSSSEE VSFQGVGSGA TLVVTTLGES PTAVSA //