Rab39
entrez
270160
canonical
uniprot
Q8BHD0
canonical
ensembl
ENSMUSG00000055069
resolver
ensp
ENSMUSP00000063804
resolver
enst
ENSMUST00000068449
resolver
genesymbol
Rab39
resolver
genesymbol
Rab39a
resolver
genesymbol_syn
Rab39
resolver
genesymbol_syn
Rab39A
resolver
uniprot
Q0PD15
resolver
uniprot_entry
Q0PD15_MOUSE
resolver
uniprot_entry
RB39A_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) including c9Orf72, which promote the exchange of bound GDP for free GTP (By similarity). Regulated by GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity (Probable). Inhibited by GDP dissociation inhibitors (GDIs) (Probable). {ECO:0000250|UniProtKB:Q14964, ECO:0000305}.
uniprot
proteins
amino_acid_sequence
METIWIYQFRLIVIGDSTVGKSCLLHRFTQGRFPGLHSPACDPTVGVDFFSRLLEIEPGKRIKLQLWDTAGQERFRSITRSYYRNSVGGFLVFDITNRRSFEHVKDWLEEAKMHVQPFQIVFLLVGHKCDLASQRQVSREEAERLSTDCGMKYIETSAKDATNVEESFTILTRDIYELIKKGEICIQDGWEGVKSGFVPNTVHSSEEAVKPRKECFC
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 (By similarity). RAB39A regulates autophagosome-lysosome fusion via recruitment of the HOPS endosomal tethering complex onto lysosomes; this process involves lysosomal RAB39A and autophagosomal RAB2A recruitment of HOPS subcomplexes VPS41-VPS16-VPS18-VPS33A and VPS39-VPS11, respectively, which assemble into a functional complex to mediate membrane tethering and SNAREs-driven membrane fusion (By similarity). Also negatively regulates lipopolysaccharide (LPS)-induced autophagosome formation in macrophages, possibly by implicating PI3K (By similarity). Promotes the delivery of MHC-I molecules from the ER to phagosomes and the generation of peptide-loaded MHC-I complexes in phagosomes, thus enhancing antigen cross-presentation by dendritic cells (PubMed:31821587). 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 (By similarity). May be involved in multiple neurite formation (PubMed:23624502). {ECO:0000250|UniProtKB:Q14964, ECO:0000269|PubMed:23624502, ECO:0000269|PubMed:31821587}.
uniprot
proteins
mass_dalton
24978
uniprot
proteins
post_translational_modification
PTM: Prenylated. Prenylation is required for association with cellular membranes. {ECO:0000250|UniProtKB:Q14964}.
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
23294242
uniprot
proteins
pubmed
23624502
uniprot
proteins
pubmed
31821587
uniprot
proteins
sequence_length
217
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:31821587}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:31821587}. Lysosome membrane {ECO:0000250|UniProtKB:Q14964}. Autolysosome membrane {ECO:0000250|UniProtKB:Q14964}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. Primarily localized on lysosomes under basal conditions (By similarity). Primarily localized on autophagosomes/autolysosomes under autophagy-induced conditions (By similarity). Colocalized with VPS39 and VPS41 on lysosomes or autolysosomes (By similarity). Colocalized with STX17 on autolysosomes in autophagy-induced conditions (By similarity). Localized (GTP-bound) to phagosomes in dendritic cells; shuttles vesicles from the ER-Golgi to the phagosome (PubMed:31821587). {ECO:0000250|UniProtKB:Q14964, ECO:0000269|PubMed:31821587}.
uniprot
proteins