Rab44
entrez
442827
canonical
uniprot
Q8CB87
canonical
ensembl
ENSMUSG00000064147
resolver
ensp
ENSMUSP00000085253
resolver
ensp
ENSMUSP00000156400
resolver
ensp
ENSMUSP00000271143
resolver
ensp
ENSMUSP00000337310
resolver
enst
ENSMUST00000233717
resolver
genesymbol
Rab44
resolver
uniprot
A0A2Y9CZI3
resolver
uniprot
B9EID0
resolver
uniprot_entry
RAB44_MOUSE
resolver
uniprot_sec
A0A2Y9CZI3
resolver
uniprot_sec
B9EID0
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:P62820}.
uniprot
proteins
amino_acid_sequence
MEKGKGVSRKGRKLASSRRRQAREPADGQDAPVAAEAESWPSDADAELQGFFQDCGAKERGFVTREDLAEARFSFLGGEEPQMIFDWVDVESRGHLSLEEFSSGLKNVFGSSPGTHRLRTKRSLPSQRESVTSTLPVPEEADAEEKEAFLALIGQMETGHSLSEQAEIWKLWRELRQEEPQLAGNLEGFLAKMSSRLQEAQADREALAWTLRKRDSDHLYKVRQLYEETEEQIRREKQQLQAQSDSRGMALSAHMQEALEAKEQEVQRLAEGQRELEAQLLHLSSTQQEANRENLQLREAERDLAGQLEEVRGQLQVTRGHLDTARTRGKVSWQIEEEPSVPRANKEAPDPQAVPTEEAPLPELFGNNDNWDQFLSSIEAHSHRTLRLCWSPPPSPSSTSAPQTPRIVRQISISKISALQFSQEPASDPDPGPRGSPEVPPGGAKDGKGVEDPKGQDEQDVSSKQPVDSPDSDARPKGSFLWSLPGALTAESGTVEAAFRDQLAFEAEPPPQGLSSSPQSPAGSRKQTQTPDLGDKSLWSGPDPAKQSLEREVMAEDLKLGLGSQGATALPEGATEPSLSLESVDQVGPERPVQDATHLARQESHAKGFQEAPGQVLSLDSLPTHLPQSLEEQLRPEEGNLGERGQQDPGSEASESHGLEARSMESPQQDDPLPNTSQPPAETEVPAPGQMSPPRGSPILGAGAGLAVGTPETTHTLLTLAESEAQPGPVSMPVQVESKSGAPQPTEPEAESRPEDPRTDLQEAERSSSPGDLTAGKPQADPDYLYHVVFLGDSNVGKTSFLHLLHHDAFATGLTATVGVDFRVKNLLVDNKTFALQLWDTAGQERYHSLTRQLLRKAEGVVLMYDVTSQESFTHVRYWLDCLQDAGVEGVAMVLLGNKMDCEEERQVPTEAGRRLAQELGVSFGECSAALGHNILEPMMNLARSLKMQEDRLKASLAEVTHPQSTKRAGCCH
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). Promotes mast cell degranulation upon IgE Fc receptor (FcERI)-mediated activation (PubMed:33641252). {ECO:0000250|UniProtKB:P62820, ECO:0000269|PubMed:33641252}.; FUNCTION: [Isoform 2]: In bone marrow macrophages, GTP-bound RAB44 negatively regulates osteoclastogenesis by controlling lysosomal Ca(2+) influx and affecting NFATC1 signaling (PubMed:28791425, PubMed:35743062). Interaction of GDP-bound RAB44 with coronin-1C/COROC1C in macrophage promotes membrane fusion and osteoclast generation (PubMed:35743062). {ECO:0000269|PubMed:28791425, ECO:0000269|PubMed:35743062}.
uniprot
proteins
mass_dalton
106328
uniprot
proteins
mutagenesis
MUTAGEN Q8CB87-2:551; /note="T->N: Constitutively inactive (GDP-bound) mutant. Increased interaction with CORO1C. Osteoclastogenesis induction."; /evidence="ECO:0000269|PubMed:35743062"; MUTAGEN Q8CB87-2:596; /note="Q->L: Constitutively active (GTP-bound) mutant. Loss of interaction with CORO1C. Osteoclastogenesis inhibition."; /evidence="ECO:0000269|PubMed:35743062"; MUTAGEN Q8CB87-2:723; /note="C->A: Decreased osteoclastogenesis inhibition. Decreased osteoclastogenesis inhibition; when associated with A-724."; /evidence="ECO:0000269|PubMed:28791425"; MUTAGEN Q8CB87-2:724; /note="C->A: Decreased osteoclastogenesis inhibition; when associated with A-723."; /evidence="ECO:0000269|PubMed:28791425"; MUTAGEN Q8CB87-3:750; /note="T->N: Constitutively inactive (GDP-bound) mutant. Decreased beta-hexosaminidase secretion upon FcERI-mediated activation, compared to WT. No change in beta-hexosaminidase secretion upon ionomycin/PMA simulation, compared to WT."; /evidence="ECO:0000269|PubMed:33641252"; MUTAGEN Q8CB87-3:795; /note="Q->L: Constitutively active (GTP-bound) mutant. No change in beta-hexosaminidase secretion upon FcERI-mediated activation, compared to WT. Decreased beta-hexosaminidase secretion upon ionomycin/PMA simulation, compared to WT."; /evidence="ECO:0000269|PubMed:33641252
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21750661
uniprot
proteins
pubmed
28791425
uniprot
proteins
pubmed
33641252
uniprot
proteins
pubmed
35743062
uniprot
proteins
sequence_length
973
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:33641252}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:33641252}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane {ECO:0000269|PubMed:33641252}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Localized mainly to lysosomes and the ER and partially to early endosomes in bone marrow mast cells. {ECO:0000269|PubMed:33641252}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:33641252}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:28791425}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:28791425}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:28791425}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Localized mainly to the ER (PubMed:33641252). Localized to the Golgi complex, late endosomes and lysosomes monocyte/macrophage-like cells (PubMed:28791425). {ECO:0000269|PubMed:28791425, ECO:0000269|PubMed:33641252}.; SUBCELLULAR LOCATION: [Isoform 3]: Lysosome membrane {ECO:0000269|PubMed:33641252}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Localized mainly to lysosomes. {ECO:0000269|PubMed:33641252}.
uniprot
proteins