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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)DescriptionActionsGraphical viewLength
Mutagenesisi126T → A: Abolishes binding to host cell surface. 1 Publication1
Mutagenesisi220T → A: Abolishes binding to host cell surface. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisImportedAdd BLAST16
ChainiPRO_500014768617 – 456Micronemal protein 11 PublicationAdd BLAST440

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Proteomic databases

PRIDEiO00834.

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 interactor.
MINTiMINT-6801851.
STRINGi5811.TGME49_091890.

Structurei

Secondary structure

1456
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 54Combined sources19
Helixi58 – 60Combined sources3
Helixi64 – 66Combined sources3
Beta strandi67 – 72Combined sources6
Beta strandi82 – 87Combined sources6
Helixi88 – 90Combined sources3
Beta strandi91 – 94Combined sources4
Beta strandi100 – 104Combined sources5
Beta strandi110 – 117Combined sources8
Turni119 – 121Combined sources3
Beta strandi124 – 126Combined sources3
Helixi128 – 142Combined sources15
Helixi145 – 157Combined sources13
Beta strandi161 – 168Combined sources8
Beta strandi171 – 181Combined sources11
Helixi182 – 184Combined sources3
Beta strandi186 – 194Combined sources9
Beta strandi198 – 206Combined sources9
Helixi214 – 216Combined sources3
Beta strandi218 – 220Combined sources3
Helixi222 – 230Combined sources9
Beta strandi240 – 243Combined sources4
Beta strandi246 – 249Combined sources4
Beta strandi251 – 254Combined sources4
Beta strandi324 – 332Combined sources9
Beta strandi337 – 343Combined sources7
Beta strandi345 – 350Combined sources6
Turni352 – 354Combined sources3
Beta strandi356 – 360Combined sources5
Turni361 – 364Combined sources4
Beta strandi365 – 375Combined sources11
Beta strandi377 – 379Combined sources3
Beta strandi384 – 394Combined sources11
Beta strandi396 – 398Combined sources3
Beta strandi400 – 408Combined sources9
Beta strandi411 – 424Combined sources14
Beta strandi427 – 435Combined sources9
Beta strandi437 – 439Combined sources3
Beta strandi441 – 446Combined sources6
Turni453 – 455Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00834.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni17 – 262MAR domainAdd BLAST246
Regioni124 – 126Interaction with host sialylated oligosaccharide chains3
Regioni216 – 220Interaction with host sialylated oligosaccharide chains5
Regioni320 – 456Galectin-likeAdd BLAST137

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi103 – 107CXXCG1 Publication5
Motifi193 – 197CXXCG1 Publication5

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PRIDEiO00834.

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...

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: November 2, 2016
This is version 64 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.