RAB7A
entrez
7879
canonical
uniprot
P51149
canonical
ensembl
ENSG00000075785
resolver
ensp
ENSP00000265062
resolver
ensp
ENSP00000501618
resolver
ensp
ENSP00000502000
resolver
ensp
ENSP00000502088
resolver
ensp
ENSP00000502486
resolver
ensp
ENSP00000571075
resolver
ensp
ENSP00000571076
resolver
ensp
ENSP00000571077
resolver
ensp
ENSP00000571078
resolver
ensp
ENSP00000571080
resolver
ensp
ENSP00000571081
resolver
ensp
ENSP00000571082
resolver
ensp
ENSP00000571083
resolver
ensp
ENSP00000571084
resolver
ensp
ENSP00000571085
resolver
ensp
ENSP00000571086
resolver
ensp
ENSP00000571087
resolver
ensp
ENSP00000571088
resolver
ensp
ENSP00000601750
resolver
ensp
ENSP00000601752
resolver
ensp
ENSP00000601753
resolver
ensp
ENSP00000601754
resolver
ensp
ENSP00000601755
resolver
ensp
ENSP00000636900
resolver
ensp
ENSP00000636901
resolver
ensp
ENSP00000636902
resolver
ensp
ENSP00000636903
resolver
ensp
ENSP00000636904
resolver
ensp
ENSP00000636905
resolver
ensp
ENSP00000636906
resolver
enst
ENST00000265062
resolver
enst
ENST00000674589
resolver
enst
ENST00000675342
resolver
enst
ENST00000675497
resolver
enst
ENST00000676214
resolver
enst
ENST00000901016
resolver
enst
ENST00000901017
resolver
enst
ENST00000901018
resolver
enst
ENST00000901019
resolver
enst
ENST00000901021
resolver
enst
ENST00000901022
resolver
enst
ENST00000901023
resolver
enst
ENST00000901024
resolver
enst
ENST00000901025
resolver
enst
ENST00000901026
resolver
enst
ENST00000901027
resolver
enst
ENST00000901028
resolver
enst
ENST00000901029
resolver
enst
ENST00000931691
resolver
enst
ENST00000931693
resolver
enst
ENST00000931694
resolver
enst
ENST00000931695
resolver
enst
ENST00000931696
resolver
enst
ENST00000966841
resolver
enst
ENST00000966842
resolver
enst
ENST00000966843
resolver
enst
ENST00000966844
resolver
enst
ENST00000966845
resolver
enst
ENST00000966846
resolver
enst
ENST00000966847
resolver
genesymbol
RAB7A
resolver
genesymbol_syn
RAB7
resolver
hgnc
HGNC:9788
resolver
uniprot
A0A158RFU6
resolver
uniprot
A8K3V6
resolver
uniprot
Q9NWJ0
resolver
uniprot
Q9UPB0
resolver
uniprot_entry
A0A158RFU6_HUMAN
resolver
uniprot_entry
RAB7A_HUMAN
resolver
uniprot_sec
A8K3V6
resolver
uniprot_sec
Q9NWJ0
resolver
uniprot_sec
Q9UPB0
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:0000305}.
uniprot
proteins
amino_acid_sequence
MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWCYSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPIKLDKNDRAKASAESCSC
uniprot
proteins
disease_involvement
DISEASE: Charcot-Marie-Tooth disease, axonal, type 2B (CMT2B) [MIM:600882]: A dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. {ECO:0000269|PubMed:12545426, ECO:0000269|PubMed:15455439, ECO:0000269|PubMed:17060578, ECO:0000269|PubMed:20028791, ECO:0000269|PubMed:21151572, ECO:0000269|PubMed:23179371}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (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). {ECO:0000250|UniProtKB:P51150, ECO:0000269|PubMed:11179213, ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:14617358, ECO:0000269|PubMed:20028791, ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:33147445, ECO:0000269|PubMed:38538795}.
uniprot
proteins
mass_dalton
23490
uniprot
proteins
mutagenesis
MUTAGEN 8; /note="L->A: Abolishes interaction with RILP and reduces its localization to late endosomal/lysosomal compartments."; /evidence="ECO:0000269|PubMed:15933719"; MUTAGEN 10; /note="K->A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments."; /evidence="ECO:0000269|PubMed:15933719"; MUTAGEN 22; /note="T->N: Abolishes localization on late endosomes, lysosomes and phagosomes and reduces phagosomal fusions. Abolishes association of RILP with the phagosomes. No loss of interaction with CLN5. No loss of interaction with PRPH. Reduced interaction with VPS13A. Inhibits SARS-CoV-2 infection."; /evidence="ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:23179371, ECO:0000269|PubMed:30709847, ECO:0000269|PubMed:34159616"; MUTAGEN 67; /note="Q->L: Does not abolish localization on late endosomes, lysosomes and phagosomes and does not reduce phagosomal fusions. No loss of interaction with CLN5 and VPS13A. Increases interaction with PRPH. Inhibits SARS-CoV-2 infection."; /evidence="ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:23179371, ECO:0000269|PubMed:30709847, ECO:0000269|PubMed:34159616"; MUTAGEN 180; /note="V->A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments."; /evidence="ECO:0000269|PubMed:15933719"; MUTAGEN 182; /note="L->A: Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments; when associated with A-183."; /evidence="ECO:0000269|PubMed:15933719"; MUTAGEN 183; /note="Y->A: Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments; when associated with A-182."; /evidence="ECO:0000269|PubMed:15933719
uniprot
proteins
post_translational_modification
PTM: Deubiquitination at Lys-191 and Lys-194 by USP32. {ECO:0000269|PubMed:36476874}.; PTM: Phosphorylated at Ser-72 by LRRK1; phosphorylation is dependent on protein kinase C (PKC) activation of LRRK1. {ECO:0000269|PubMed:36040231}.; PTM: Prenylated. Prenylation is required for association with cellular membranes. {ECO:0000269|PubMed:37821429}.
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
11179213
uniprot
proteins
pubmed
12545426
uniprot
proteins
pubmed
12643545
uniprot
proteins
pubmed
12944476
uniprot
proteins
pubmed
14617358
uniprot
proteins
pubmed
14668488
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14998988
uniprot
proteins
pubmed
15455439
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15933719
uniprot
proteins
pubmed
16176980
uniprot
proteins
pubmed
16925951
uniprot
proteins
pubmed
17060578
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19392663
uniprot
proteins
pubmed
20028791
uniprot
proteins
pubmed
20048159
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20100911
uniprot
proteins
pubmed
20851765
uniprot
proteins
pubmed
21151572
uniprot
proteins
pubmed
21255211
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22261744
uniprot
proteins
pubmed
22431521
uniprot
proteins
pubmed
22660413
uniprot
proteins
pubmed
23179371
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26416964
uniprot
proteins
pubmed
28325809
uniprot
proteins
pubmed
30709847
uniprot
proteins
pubmed
31636202
uniprot
proteins
pubmed
33147445
uniprot
proteins
pubmed
34159616
uniprot
proteins
pubmed
34432599
uniprot
proteins
pubmed
34552186
uniprot
proteins
pubmed
36040231
uniprot
proteins
pubmed
36476874
uniprot
proteins
pubmed
37821429
uniprot
proteins
pubmed
37857821
uniprot
proteins
pubmed
38538795
uniprot
proteins
pubmed
40839735
uniprot
proteins
pubmed
8954989
uniprot
proteins
pubmed
9126495
uniprot
proteins
sequence_length
207
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:21255211}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:14617358, ECO:0000269|PubMed:16176980, ECO:0000269|PubMed:20028791, ECO:0000269|PubMed:28325809, ECO:0000269|PubMed:31636202}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:20028791, ECO:0000269|PubMed:31636202, ECO:0000269|PubMed:38538795}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome membrane {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:20028791}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lipid droplet {ECO:0000250|UniProtKB:P51150}. Endosome membrane {ECO:0000269|PubMed:22431521}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P51150}. Mitochondrion membrane {ECO:0000305|PubMed:34432599}; Peripheral membrane protein {ECO:0000305}. Note=Colocalizes with OSBPL1A at the late endosome (PubMed:16176980). 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 (PubMed:21255211). Lipid droplet localization is increased upon ADRB2 stimulation (By similarity). Recruited to damaged mitochondria during mitophagy in a RIMOC1-dependent manner (PubMed:34432599). {ECO:0000250|UniProtKB:P51150, ECO:0000269|PubMed:16176980, ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:34432599}.
uniprot
proteins