UniProt functional annotation for O00834



	UniProt functional annotation for O00834

UniProt code: O00834.

Organism: Toxoplasma gondii.

Taxonomy: Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia; Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.

Function: 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. {ECO:0000269|PubMed:11157983, ECO:0000269|PubMed:11447133, ECO:0000269|PubMed:16166092, ECO:0000269|PubMed:17491595}.

Subunit: Monomer. Interacts directly with MIC4 and MIC6. Part of the MIC6-MIC1-MIC4 complex. {ECO:0000269|PubMed:11157983, ECO:0000269|PubMed:11447133, ECO:0000269|PubMed:16166092, ECO:0000269|PubMed:18818666}.

Subcellular location: Cytoplasmic vesicle, secretory vesicle, microneme {ECO:0000269|PubMed:11157983, ECO:0000269|PubMed:15684324, ECO:0000269|PubMed:18818666}.

Developmental stage: Expression is down-regulated during bradyzoite development. {ECO:0000269|PubMed:12455982}.

Domain: 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.

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.

Annotations taken from UniProtKB at the EBI.


Organism:		Toxoplasma gondii.
Taxonomy:		Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia; Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.



Function:		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. {ECO:0000269\|PubMed:11157983, ECO:0000269\|PubMed:11447133, ECO:0000269\|PubMed:16166092, ECO:0000269\|PubMed:17491595}.


Subunit:		Monomer. Interacts directly with MIC4 and MIC6. Part of the MIC6-MIC1-MIC4 complex. {ECO:0000269\|PubMed:11157983, ECO:0000269\|PubMed:11447133, ECO:0000269\|PubMed:16166092, ECO:0000269\|PubMed:18818666}.
Subcellular location:		Cytoplasmic vesicle, secretory vesicle, microneme {ECO:0000269\|PubMed:11157983, ECO:0000269\|PubMed:15684324, ECO:0000269\|PubMed:18818666}.
Developmental stage:		Expression is down-regulated during bradyzoite development. {ECO:0000269\|PubMed:12455982}.
Domain:		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.
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.