Rab GTPase family 7 (Rab7). Rab7 subfamily. Rab7 is a small Rab GTPase that regulates vesicular traffic from early to late endosomal stages of the endocytic pathway. The yeast Ypt7 and mammalian Rab7 are both involved in transport to the vacuole/lysosome, whereas Ypt7 is also required for homotypic vacuole fusion. Mammalian Rab7 is an essential participant in the autophagic pathway for sequestration and targeting of cytoplasmic components to the lytic compartment. Mammalian Rab7 is also proposed to function as a tumor suppressor. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
No pairwise interactions are available for this conserved domain.
Total Mutations Found: 121 Total Disease Mutations Found: 71 This domain occurred 116 times on human genes (209 proteins).
If you've navigated here from a protein, hovering over a position on the weblogo will display the corresponding protein position for that domain position.
The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs.
Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below.
Range on the Protein:
Protein ID Protein Position
Domain Position:
Feature Name:
Total Found:
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