Rab7a
entrez
29448
canonical
uniprot
P09527
canonical
ensembl
ENSRNOG00000012247
resolver
ensembl
ENSRNOG00055012878
resolver
ensembl
ENSRNOG00060024690
resolver
ensembl
ENSRNOG00065015249
resolver
ensp
ENSRNOP00000016432
resolver
ensp
ENSRNOP00000080334
resolver
ensp
ENSRNOP00055017902
resolver
ensp
ENSRNOP00060035568
resolver
ensp
ENSRNOP00065019826
resolver
enst
ENSRNOT00000016432
resolver
enst
ENSRNOT00055022061
resolver
enst
ENSRNOT00060042959
resolver
enst
ENSRNOT00065025300
resolver
genesymbol
Rab7a
resolver
genesymbol_syn
Rab7
resolver
uniprot
Q4AEF6
resolver
uniprot_entry
RAB7A_RAT
resolver
uniprot_sec
Q4AEF6
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP. Regulated by GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity. Inhibited by GDP dissociation inhibitors (GDIs). {ECO:0000250|UniProtKB:P51149}.
uniprot
proteins
amino_acid_sequence
MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWCYSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPIKLDKNERAKASAESCSC
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
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. 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 (By similarity). Also plays a central role in growth-factor-mediated cell signaling, nutrient-transporter-mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism (By similarity). Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes (By similarity). Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and Mycobacteria (By similarity). Plays a role in the fusion of phagosomes with lysosomes (By similarity). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts (PubMed:16040606). Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA (PubMed:16306406). Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation (By similarity). Involved in the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-independent autophagic pathway. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). Required for vesicular trafficking and cell surface expression of ACE2 (By similarity). May play a role in PRPH neuronal intermediate filament assembly (By similarity). {ECO:0000250|UniProtKB:P51149, ECO:0000250|UniProtKB:P51150, ECO:0000269|PubMed:16040606, ECO:0000269|PubMed:16306406}.
uniprot
proteins
mass_dalton
23504
uniprot
proteins
post_translational_modification
PTM: Deubiquitination at Lys-191 and Lys-194 by USP32. {ECO:0000250|UniProtKB:P51149}.; PTM: Phosphorylated at Ser-72 by LRRK1; phosphorylation is dependent on protein kinase C (PKC) activation of LRRK1. {ECO:0000250|UniProtKB:P51149}.; PTM: Prenylated. Prenylation is required for association with cellular membranes. {ECO:0000250|UniProtKB:P51149}.
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
15186776
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15978772
uniprot
proteins
pubmed
16040606
uniprot
proteins
pubmed
16306406
uniprot
proteins
pubmed
18756270
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
3057452
uniprot
proteins
sequence_length
207
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:16040606}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:16040606}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome 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}. Endosome membrane {ECO:0000250|UniProtKB:P51149}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P51150}. Mitochondrion membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}. Note=Colocalizes with OSBPL1A at the late endosome. Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts. Recruited to phagosomes containing S.aureus or Mycobacterium. Lipid droplet localization is increased upon ADRB2 stimulation. Recruited to damaged mitochondria during mitophagy in a RIMOC1-dependent manner. {ECO:0000250|UniProtKB:P51149, ECO:0000250|UniProtKB:P51150}.
uniprot
proteins