Search Results
Overview
| Uniprot ID | P51149 |
|---|---|
| Protein Name | Ras-related protein Rab-7a |
| Gene Name | RAB7A |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 31 | LMNQYVNKKFSNQYK |
| 32 | MNQYVNKKFSNQYKA |
Function
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:38538795). In its active state, RAB7A binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Also plays a central role in growth-factor-mediated cell signaling, nutrient-transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA (PubMed:11179213, PubMed:12944476, PubMed:14617358, PubMed:20028791, PubMed:21255211). Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation. Involved in the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-independent autophagic pathway (By similarity). Required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). Required for vesicular trafficking and cell surface expression of ACE2 (PubMed:33147445). May play a role in PRPH neuronal intermediate filament assembly (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0097208 | alveolar lamellar body |
| Cellular Component | GO:0000421 | autophagosome membrane |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0010008 | endosome membrane |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005770 | late endosome |
| Cellular Component | GO:0031902 | late endosome membrane |
| Cellular Component | GO:0005811 | lipid droplet |
| Cellular Component | GO:0005765 | lysosomal membrane |
| Cellular Component | GO:0005764 | lysosome |
| Cellular Component | GO:0033162 | melanosome membrane |
| Cellular Component | GO:0031966 | mitochondrial membrane |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0045335 | phagocytic vesicle |
| Cellular Component | GO:0030670 | phagocytic vesicle membrane |
| Cellular Component | GO:0034045 | phagophore assembly site membrane |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0098830 | presynaptic endosome |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0030667 | secretory granule membrane |
| Cellular Component | GO:0030672 | synaptic vesicle membrane |
| Molecular Function | GO:0003925 | G protein activity |
| Molecular Function | GO:0019003 | GDP binding |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:1905394 | retromer complex binding |
| Molecular Function | GO:0031267 | small GTPase binding |
| Biological Process | GO:0000045 | autophagosome assembly |
| Biological Process | GO:0045453 | bone resorption |
| Biological Process | GO:0042632 | cholesterol homeostasis |
| Biological Process | GO:0045022 | early endosome to late endosome transport |
| Biological Process | GO:0006897 | endocytosis |
| Biological Process | GO:0008333 | endosome to lysosome transport |
| Biological Process | GO:0099638 | endosome to plasma membrane protein transport |
| Biological Process | GO:0007174 | epidermal growth factor catabolic process |
| Biological Process | GO:0016042 | lipid catabolic process |
| Biological Process | GO:0061724 | lipophagy |
| Biological Process | GO:0090120 | lysosome to ER cholesterol transport |
| Biological Process | GO:1903542 | negative regulation of exosomal secretion |
| Biological Process | GO:1905366 | negative regulation of intralumenal vesicle formation |
| Biological Process | GO:0090383 | phagosome acidification |
| Biological Process | GO:0090382 | phagosome maturation |
| Biological Process | GO:0090385 | phagosome-lysosome fusion |
| Biological Process | GO:1903543 | positive regulation of exosomal secretion |
| Biological Process | GO:0045732 | positive regulation of protein catabolic process |
| Biological Process | GO:0048524 | positive regulation of viral process |
| Biological Process | GO:0061462 | protein localization to lysosome |
| Biological Process | GO:0006622 | protein targeting to lysosome |
| Biological Process | GO:0022615 | protein to membrane docking |
| Biological Process | GO:0015031 | protein transport |
| Biological Process | GO:0009617 | response to bacterium |
| Biological Process | GO:0042147 | retrograde transport, endosome to Golgi |
| Biological Process | GO:0036466 | synaptic vesicle recycling via endosome |
| Biological Process | GO:0019076 | viral release from host cell |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.