Protein Family Models

Rhomboid_N is the N-terminal cytoplasmic domain of the rhomboid intra-membraneous serine protease, otherwise known as Peptidase_S54, Pfam:PF01694. This N-terminal domain has similarity to other GlnB-like domains, some of which appear to have a binding role, eg to peptidoglycan. It is not clear exactly what the function of this domain is in the protease, but its presence is critical for maintaining a catalytically competent state for the protein [1]. [1]. 22963263. Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core. Sherratt AR, Blais DR, Ghasriani H, Pezacki JP, Goto NK;. Biochemistry. 2012;51:7794-7803. (from Pfam)

Date:

2024-10-16

This family contains integral membrane proteins that are related to Drosophila rhomboid protein Swiss:P20350. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease [2][3][4] (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite [5]. [1]. 2110920. rhomboid, a gene required for dorsoventral axis establishment and peripheral nervous system development in Drosophila melanogaster. Bier E, Jan LY, Jan YN;. Genes Dev 1990;4:190-203. [2]. 11672525. Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases. Urban S, Lee JR, Freeman M;. Cell 2001;107:173-182. [3]. 12620104. The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers. Koonin EV, Makarova KS, Rogozin IB, Davidovic L, Letellier MC, Pellegrini L;. Genome Biol 2003;4:R19. [4]. 15684070. Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity. Urban S, Wolfe MS;. Proc Natl Acad Sci U S A. 2005;102:1883-1888. [5]. 15753289. A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma. Brossier F, Jewett TJ, Sibley LD, Urban S;. Proc Natl Acad Sci U S A. 2005;102:4146-4151. (from Pfam)

Date:

2024-10-16

rhomboid family intramembrane serine protease GlpG cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains

Date:

2017-03-29

GlpG in E. coli is a rhomboid family intramembrane serine protease that has been extensively characterized as a proxy for rhomboid family proteases in animals. It efficiently cleaves eukaryote-derived model substrates. This multiple membrane-spanning protein excludes inappropriate substrates from access to its cleavage site, and shows activity against truncated versions, but not full-length versions, of the E. coli multidrug transporter MdfA. This finding suggests a housekeeping function in removing faulty proteins. In contrast, several eukaryotic rhomboid family proteases release peptide hormones for signaling functions, and the Shewanella and Vibrio protein rhombosortase appears to be part of a protein-sorting system, cleaving a C-terminal anchoring helix domain.

Gene:

glpG

Date:

2024-10-04