This domain is found in a number proteins including Rhophilin Q61085 and BRO1 P48582. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1 (PUBMED:15935782).
The BRO1 domain is a protein domain of ~390 residues in length. It occurs in a number of eukaryotic proteins, such as yeast BRO1 and human PDCD6IP/Alix, which are involved in protein targeting to the vacuole or lysosome. The BRO1 domain of fungal and mammalian proteins binds with multivesicular body components (ESCRT-III proteins) such as yeast Snf7 and mammalian CHMP4b, and can function to target BRO1 domain-containing proteins to endosomes [ (PUBMED:15935782) (PUBMED:14583093) (PUBMED:15944343) ].
The BRO1 domain has a boomerang shape composed of 14 alpha-helices and 3 beta-sheets. It contains a TPR-like substructure in the central part [ (PUBMED:15935782) ]. The C terminus is less conserved.
Family alignment:
There are 5823 BRO1 domains in 5818 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing BRO1 domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with BRO1 domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing BRO1 domain in the selected taxonomic class.
Structural basis for endosomal targeting by the Bro1 domain.
Dev Cell. 2005; 8: 937-47
Display abstract
Proteins delivered to the lysosome or the yeast vacuole via late endosomesare sorted by the ESCRT complexes and by associated proteins, includingAlix and its yeast homolog Bro1. Alix, Bro1, and several other lateendosomal proteins share a conserved 160 residue Bro1 domain whoseboundaries, structure, and function have not been characterized. Thecrystal structure of the Bro1 domain of Bro1 reveals a folded core of 367residues. The extended Bro1 domain is necessary and sufficient for bindingto the ESCRT-III subunit Snf7 and for the recruitment of Bro1 to lateendosomes. The structure resembles a boomerang with its concave facefilled in and contains a triple tetratricopeptide repeat domain as asubstructure. Snf7 binds to a conserved hydrophobic patch on Bro1 that isrequired for protein complex formation and for the protein-sortingfunction of Bro1. These results define a conserved mechanism whereby Bro1domain-containing proteins are targeted to endosomes by Snf7 and itsorthologs.
HD-PTP: A novel protein tyrosine phosphatase gene on human chromosome3p21.3.
Biochem Biophys Res Commun. 2000; 278: 671-8
Display abstract
A human cDNA encoding a novel protein tyrosine phosphatase has beenisolated. The phosphatase has unique features in its domain structure: a"Zn-hand" domain containing several SH3-binding motifs, a tyrosinephosphatase domain, a C-terminal PEST motif, and an N-terminal domainsimilar to yeast BRO1, an apoptosis-related mammalian AIP1 and to aRHO-binding protein, Rhophilin. The gene is located at chromosome 3p21.3,an area frequently deleted in many types of cancer, especially within thefunctionally defined narrow region. The gene may be a human homolog of therat PTP-TD14 gene reported by others, which can suppress H-ras-mediatedtransformation. We identified a hemizygous missense mutation in a lungcancer cell line. Thus, the phosphatase gene may be a candidate for one ofthe tumor suppressor genes located on 3p21.3.