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Protein

Micronemal protein 1

Gene

MIC1

Organism
Toxoplasma gondii
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Adhesin. Required for attachment of the parasite to the host cell prior to invasion. Ensures correct folding of MIC6 and transport of the MIC6-MIC1-MIC4 complex into the micronemes.4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Virulence

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Micronemal protein 1
Gene namesi
Name:MIC1Imported
OrganismiToxoplasma gondii
Taxonomic identifieri5811 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi126 – 1261T → A: Abolishes binding to host cell surface. 1 Publication
Mutagenesisi220 – 2201T → A: Abolishes binding to host cell surface. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisImportedAdd
BLAST
Chaini17 – 456440Micronemal protein 11 PublicationPRO_5000147686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 ↔ 85
Disulfide bondi53 ↔ 61
Disulfide bondi103 ↔ 113
Disulfide bondi107 ↔ 143
Disulfide bondi154 ↔ 179
Disulfide bondi193 ↔ 203
Disulfide bondi197 ↔ 242
Disulfide bondi236 ↔ 252
Disulfide bondi354 ↔ 4251 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Developmental stagei

Expression is down-regulated during bradyzoite development.1 Publication

Interactioni

Subunit structurei

Monomer. Interacts directly with MIC4 and MIC6. Part of the MIC6-MIC1-MIC4 complex.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MIC6Q9XYH73EBI-8078093,EBI-8078076

Protein-protein interaction databases

IntActiO00834. 1 interaction.
MINTiMINT-6801851.
STRINGi5811.TGME49_091890.

Structurei

Secondary structure

1
456
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 5419Combined sources
Helixi58 – 603Combined sources
Helixi64 – 663Combined sources
Beta strandi67 – 726Combined sources
Beta strandi82 – 876Combined sources
Helixi88 – 903Combined sources
Beta strandi91 – 944Combined sources
Beta strandi100 – 1045Combined sources
Beta strandi110 – 1178Combined sources
Turni119 – 1213Combined sources
Beta strandi124 – 1263Combined sources
Helixi128 – 14215Combined sources
Helixi145 – 15713Combined sources
Beta strandi161 – 1688Combined sources
Beta strandi171 – 18111Combined sources
Helixi182 – 1843Combined sources
Beta strandi186 – 1949Combined sources
Beta strandi198 – 2069Combined sources
Helixi214 – 2163Combined sources
Beta strandi218 – 2203Combined sources
Helixi222 – 2309Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi246 – 2494Combined sources
Beta strandi251 – 2544Combined sources
Beta strandi324 – 3329Combined sources
Beta strandi337 – 3437Combined sources
Beta strandi345 – 3506Combined sources
Turni352 – 3543Combined sources
Beta strandi356 – 3605Combined sources
Turni361 – 3644Combined sources
Beta strandi365 – 37511Combined sources
Beta strandi377 – 3793Combined sources
Beta strandi384 – 39411Combined sources
Beta strandi396 – 3983Combined sources
Beta strandi400 – 4089Combined sources
Beta strandi411 – 42414Combined sources
Beta strandi427 – 4359Combined sources
Beta strandi437 – 4393Combined sources
Beta strandi441 – 4466Combined sources
Turni453 – 4553Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BVBNMR-A320-456[»]
2JH1X-ray1.90A17-262[»]
2JH7X-ray2.07A17-262[»]
2JHDX-ray2.30A17-262[»]
2K2SNMR-A320-455[»]
3F53X-ray2.00A17-262[»]
3F5AX-ray2.00A17-262[»]
3F5EX-ray2.00A17-262[»]
ProteinModelPortaliO00834.
SMRiO00834. Positions 28-261, 320-456.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00834.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 262246MAR domainAdd
BLAST
Regioni124 – 1263Interaction with host sialylated oligosaccharide chains
Regioni216 – 2205Interaction with host sialylated oligosaccharide chains
Regioni320 – 456137Galectin-likeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi103 – 1075CXXCG1 Publication
Motifi193 – 1975CXXCG1 Publication

Domaini

The galectin-like domain has been demonstrated not to bind lactose, glucose, maltose, mannose, heparin, fucose, L-arabinose, N-acetyl-D-galactosamine, or N-acetyl-D-glucosamine. It interacts directly with the second and the third EGF-like domain of MIC6, and with part of the acidic domain.
The MAR (micronemal adhesive repeat) domain was at first proposed to be TSR1-like (thrombospondin type 1-like repeat) by PubMed:9027753, but PubMed:17491595 found that this domain represents a previously unknown protein fold. This domain is jointly responsible for interacting with MIC4 and for host-cell adhesion.

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR024691. MIC1_galectin-like_dom.
IPR019562. Micronemal-adhesive-rpt_sia-bd.
IPR008117. Microneme_MIC1.
[Graphical view]
PfamiPF10564. MAR_sialic_bdg. 2 hits.
PF11476. TgMIC1. 1 hit.
[Graphical view]
PRINTSiPR01744. MIC1MICRNEME.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O00834-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQALFLTVL LPVLFGVGPE AYGEASHSHS PASGRYIQQM LDQRCQEIAA
60 70 80 90 100
ELCQSGLRKM CVPSSRIVAR NAVGITHQNT LQWRCFDTAS LLESNQENNG
110 120 130 140 150
VNCVDDCGHT IPCPGGVHRQ NSNHATRHEI LSKLVEEGVQ RFCSPYQASA
160 170 180 190 200
NKYCNDKFPG TIARRSKGFG NNVEVAWRCY EKASLLYSVY AECASNCGTT
210 220 230 240 250
WYCPGGRRGT STELDKRHYT EEEGIRQAIG SVDSPCSEVE VCLPKDENPP
260 270 280 290 300
LCLDESGQIS RTGGGPPSQP PEMQQPADRS DERGGGKEQS PGGEAQPDHP
310 320 330 340 350
TKGGNIDLPE KSTSPEKTPK TEIHGDSTKA TLEEGQQLTL TFISTKLDVA
360 370 380 390 400
VGSCHSLVAN FLDGFLKFQT GSNSAFDVVE VEEPAGPAVL TIGLGHKGRL
410 420 430 440 450
AVVLDYTRLN AALGSAAYVV EDSGCSSSEE VSFQGVGSGA TLVVTTLGES

PTAVSA
Length:456
Mass (Da):48,672
Last modified:July 1, 1997 - v1
Checksum:i3F1255FC0C587AF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71786 Genomic DNA. Translation: CAA96466.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71786 Genomic DNA. Translation: CAA96466.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BVBNMR-A320-456[»]
2JH1X-ray1.90A17-262[»]
2JH7X-ray2.07A17-262[»]
2JHDX-ray2.30A17-262[»]
2K2SNMR-A320-455[»]
3F53X-ray2.00A17-262[»]
3F5AX-ray2.00A17-262[»]
3F5EX-ray2.00A17-262[»]
ProteinModelPortaliO00834.
SMRiO00834. Positions 28-261, 320-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO00834. 1 interaction.
MINTiMINT-6801851.
STRINGi5811.TGME49_091890.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO00834.

Family and domain databases

InterProiIPR024691. MIC1_galectin-like_dom.
IPR019562. Micronemal-adhesive-rpt_sia-bd.
IPR008117. Microneme_MIC1.
[Graphical view]
PfamiPF10564. MAR_sialic_bdg. 2 hits.
PF11476. TgMIC1. 1 hit.
[Graphical view]
PRINTSiPR01744. MIC1MICRNEME.
ProtoNetiSearch...

Publicationsi

  1. "The MIC1 microneme protein of Toxoplasma gondii contains a duplicated receptor-like domain and binds to host cell surface."
    Fourmaux M.N., Mercereau-Puijalon O., Achbarou A., Biderre C., Briche I., Loyens A., Odberg-Ferragut C., Camus D., Dubremetz J.F.
    Mol. Biochem. Parasitol. 83:201-210(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, MOTIF.
    Strain: RHImported.
  2. Cited for: PROTEIN SEQUENCE OF 26-36, FUNCTION, INTERACTION WITH MIC4.
    Strain: RH1 Publication.
  3. "Identification and characterization of an escorter for two secretory adhesins in Toxoplasma gondii."
    Reiss M., Viebig N., Brecht S., Fourmaux M.-N., Soete M., Di Cristina M., Dubremetz J.F., Soldati D.
    J. Cell Biol. 152:563-578(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MIC4 AND MIC6.
    Strain: RH1 Publication.
  4. "Toxoplasma gondii asexual development: identification of developmentally regulated genes and distinct patterns of gene expression."
    Cleary M.D., Singh U., Blader I.J., Brewer J.L., Boothroyd J.C.
    Eukaryot. Cell 1:329-340(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  5. "Synergistic role of micronemal proteins in Toxoplasma gondii virulence."
    Cerede O., Dubremetz J.F., Soete M., Deslee D., Vial H., Bout D., Lebrun M.
    J. Exp. Med. 201:453-463(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Complete resonance assignments of the C-terminal domain from MIC1: a micronemal protein from Toxoplasma gondii."
    Saouros S., Chen H.A., Simpson P., Cota E., Edwards-Jones B., Soldati-Favre D., Matthews S.
    J. Biomol. NMR 31:177-178(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NMR RESONANCE ASSIGNMENTS.
  7. "A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex."
    Saouros S., Edwards-Jones B., Reiss M., Sawmynaden K., Cota E., Simpson P., Dowse T.J., Jakle U., Ramboarina S., Shivarattan T., Matthews S., Soldati-Favre D.
    J. Biol. Chem. 280:38583-38591(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 320-456, FUNCTION, INTERACTION WITH MIC4 AND MIC6, SUBUNIT, DOMAIN, DISULFIDE BOND.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-262, DISULFIDE BONDS, DOMAIN, FUNCTION, MUTAGENESIS OF THR-126 AND THR-220.
  9. "Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition."
    Sawmynaden K., Saouros S., Friedrich N., Marchant J., Simpson P., Bleijlevens B., Blackman M.J., Soldati-Favre D., Matthews S.
    EMBO Rep. 9:1149-1155(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 320-455 IN COMPLEX WITH MIC6, SUBUNIT, SUBCELLULAR LOCATION, DISULFIDE BOND, DOMAIN.

Entry informationi

Entry nameiMIC1_TOXGO
AccessioniPrimary (citable) accession number: O00834
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: July 1, 1997
Last modified: December 9, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.