MIC1_TOXGO
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 25-MAY-2022, entry version 79.
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.
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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 AlphaFoldDB; O00834; -.
DR BMRB; O00834; -.
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 VEuPathDB; ToxoDB:TGARI_291890; -.
DR VEuPathDB; ToxoDB:TGCAST_291890; -.
DR VEuPathDB; ToxoDB:TGCOUG_291890; -.
DR VEuPathDB; ToxoDB:TGDOM2_291890; -.
DR VEuPathDB; ToxoDB:TGFOU_291890; -.
DR VEuPathDB; ToxoDB:TGGT1_291890; -.
DR VEuPathDB; ToxoDB:TGMAS_291890; -.
DR VEuPathDB; ToxoDB:TGME49_291890; -.
DR VEuPathDB; ToxoDB:TGP89_291890; -.
DR VEuPathDB; ToxoDB:TGPRC2_291890; -.
DR VEuPathDB; ToxoDB:TGRH88_015770; -.
DR VEuPathDB; ToxoDB:TGRUB_291890; -.
DR VEuPathDB; ToxoDB:TGVAND_291890; -.
DR VEuPathDB; ToxoDB:TGVEG_291890; -.
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 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 247..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 313..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007829|PDB:2JH1"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2JH1"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:2JH1"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:2JH1"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2JH1"
FT HELIX 128..142
FT /evidence="ECO:0007829|PDB:2JH1"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:2JH1"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:2JH1"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2JH1"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:2JH1"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:2BVB"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:2BVB"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:2BVB"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:2BVB"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:2BVB"
FT TURN 361..364
FT /evidence="ECO:0007829|PDB:2BVB"
FT STRAND 365..375
FT /evidence="ECO:0007829|PDB:2BVB"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:2BVB"
FT STRAND 384..394
FT /evidence="ECO:0007829|PDB:2BVB"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2BVB"
FT STRAND 400..408
FT /evidence="ECO:0007829|PDB:2BVB"
FT STRAND 411..424
FT /evidence="ECO:0007829|PDB:2BVB"
FT STRAND 427..435
FT /evidence="ECO:0007829|PDB:2BVB"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:2K2S"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:2BVB"
FT TURN 453..455
FT /evidence="ECO:0007829|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
