P35288
uniprot
P35288
canonical
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP (Probable). Regulated by GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity (Probable). Inhibited by GDP dissociation inhibitors (GDIs) (Probable). {ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MLEEDMEVAIKMVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIQVNDEDVRLMLWDTAGQEEFDAITKAYYRGAQACVLVFSTTDRESFEAISSWREKVVAEVGDIPTALVQNKIDLLDDSCIKNEEAEGLAKRLKLRFYRTSVKEDLNVSEVFKYLAEKHLQKLKQQITEDPEQTHSSSNKIGVFNASVGSHLGQNSSSLNGGDVINLRPNKQRTKRTRNPFSSCSVP
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Rab23 are the cause of the open brain phenotype. Mice suffer from exencephaly and severe malformations of the spinal cord and the dorsal root ganglia, leading to complete embryonic lethality. In addition, mice display poorly developed eyes and polydactyly. {ECO:0000269|PubMed:7720556}.
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 set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). In conjunction with IFT57 and KIF17, it drives the localization of specific G protein-coupled receptors, such as the dopamime receptor DRD1, to primary cilia (By similarity). Has a critical role in the formation and elongation of neuronal primary cilia, thereby impacting the activation of sonic hedgehog (Shh) signaling (PubMed:40825043). Additionally, it is involved in the down-regulation of Shh signaling by cooperating with SUFU to prevent the nuclear import of GLI1 transcription factor, thus suppressing its transcriptional activity (PubMed:11449277, PubMed:16364285). Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes (By similarity). {ECO:0000250|UniProtKB:Q9ULC3, ECO:0000269|PubMed:11071781, ECO:0000269|PubMed:11449277, ECO:0000269|PubMed:16364285, ECO:0000269|PubMed:18218620, ECO:0000269|PubMed:40825043, ECO:0000269|PubMed:7720556}.
uniprot
proteins
mass_dalton
26678
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
11071781
uniprot
proteins
pubmed
11449277
uniprot
proteins
pubmed
14617350
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1555775
uniprot
proteins
pubmed
16034420
uniprot
proteins
pubmed
16364285
uniprot
proteins
pubmed
16463280
uniprot
proteins
pubmed
18218620
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
40825043
uniprot
proteins
pubmed
7720556
uniprot
proteins
pubmed
8125302
uniprot
proteins
sequence_length
237
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14617350}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:14617350}. Cytoplasm {ECO:0000269|PubMed:14617350}. Endosome membrane {ECO:0000269|PubMed:14617350}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9ULC3}. Cytoplasmic vesicle, phagosome {ECO:0000305}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250|UniProtKB:Q9ULC3}.
uniprot
proteins