| IED ID | IndEnz0005000081 |
| Enzyme Type ID | lipase000081 |
| Protein Name |
Ras-related protein Rab-7a EC 3.6.5.2 |
| Gene Name | Rab7a Rab7 |
| Organism | Paramecium octaurelia |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Ciliophora Intramacronucleata Oligohymenophorea Peniculida Parameciidae Paramecium Paramecium octaurelia |
| Enzyme Sequence | MASQKKQLFKIIILGDSGVGKTSLMNQYVNARFTQQYRATVGADFMAKEVMIDDRMVTLQIWDTAGQERFQSLGGAFYRGADCCVLVYDITNPKSFDSLDSWRDEFLMQGQPKDPEHFPFVVLGNKLDKATERKVQESKAQQWCKSHGNIQFFEVSAKDATNIEQAFQDIAKAAASQEKDEEIFFPTTVTLTKQSQKPQAKQGGCC |
| Enzyme Length | 206 |
| Uniprot Accession Number | Q95UJ0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P51149};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P51149}; |
| DNA Binding | |
| EC Number | 3.6.5.2 |
| Enzyme Function | FUNCTION: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, 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 (By similarity). Involved in lipophagy, a cytosolic lipase-independent autophagic pathway (By similarity). Plays a role in phagocyte formation and acidification (PubMed:22030555). {ECO:0000250|UniProtKB:P51149, ECO:0000250|UniProtKB:P51150, ECO:0000269|PubMed:22030555}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 15..22; /note=GTP; /evidence=ECO:0000250|UniProtKB:Q9NRW1; NP_BIND 34..40; /note=GTP; /evidence=ECO:0000250; NP_BIND 63..67; /note=GTP; /evidence=ECO:0000250|UniProtKB:Q9NRW1; NP_BIND 125..128; /note=GTP; /evidence=ECO:0000250|UniProtKB:Q9NRW1; NP_BIND 157..158; /note=GTP; /evidence=ECO:0000250 |
| Features | Chain (1); Lipidation (2); Modified residue (8); Motif (1); Nucleotide binding (5) |
| Keywords | Autophagy;Cytoplasmic vesicle;Endosome;GTP-binding;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Lipoprotein;Lysosome;Membrane;Nucleotide-binding;Phosphoprotein;Prenylation |
| Interact With | |
| Induction | INDUCTION: Expression increases two-fold during phagocytosis (at protein level). {ECO:0000269|PubMed:22030555}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:12799062, ECO:0000269|PubMed:22030555}; Peripheral membrane protein {ECO:0000269|PubMed:12799062, ECO:0000269|PubMed:22030555}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lipid droplet {ECO:0000250|UniProtKB:P51150}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P51150}. |
| Modified Residue | MOD_RES 17; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:22030555; MOD_RES 23; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:22030555; MOD_RES 34; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:22030555; MOD_RES 40; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:22030555; MOD_RES 64; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:22030555; MOD_RES 72; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:22030555; MOD_RES 78; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:22030555; MOD_RES 88; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:22030555 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 37..45; /note=Effector region; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 23,217 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:19669; RHEA:19670 |
| Cross Reference Brenda |