Q01514
uniprot
Q01514
canonical
amino_acid_sequence
MASEIHMSEPMCLIENTEAQLVINQEALRILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKRTGFSLGSTVQSHTKGIWMWCVPHPKKAGQTLVLLDTEGLEDVEKGDNQNDCWIFALAVLLSSTFIYNSIGTINQQAMDQLHYVTELTDLIKSKSSPDQSDVDNSANFVGFFPIFVWTLRDFSLDLEFDGESITPDEYLETSLALRKGTDENTKKFNMPRLCIRKFFPKRKCFIFDRPGDRKQLSKLEWIQEDQLNKEFVEQVAEFTSYIFSYSGVKTLSGGITVNGPRLKSLVQTYVSAICSGELPCMENAVLTLAQIENSAAVQKAITYYEEQMNQKIHMPTETLQELLDLHRTCEREAIEVFMKNSFKDVDQKFQEELGAQLEAKRDAFVKKNMDMSSAHCSDLLEGLFAHLEEEVKQGTFYKPGGYYLFLQRKQELEKKYIQTPGKGLQAEVMLRKYFESKEDLADTLLKMDQSLTEKEKQIEMERIKAEAAEAANRALAEMQKKHEMLMEQKEQSYQEHMKQLTEKMEQERKELMAEQQRIISLKLQEQERLLKQGFQNESLQLRQEIEKIKNMPPPRSCTIL
uniprot
proteins
ec_number
3.6.1.-
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens (PubMed:18025219, PubMed:21551061, PubMed:24715728, PubMed:24739961). Hydrolyzes GTP to GMP in two consecutive cleavage reactions: GTP is first hydrolyzed to GDP and then to GMP in a processive manner (By similarity). Following infection, recruited to the pathogen-containing vacuoles or vacuole-escaped bacteria and promotes both inflammasome assembly and autophagy (PubMed:21551061, PubMed:24715728, PubMed:24739961). Acts as a positive regulator of inflammasome assembly by facilitating the detection of inflammasome ligands from pathogens (PubMed:24715728, PubMed:24739961). Involved in the lysis of pathogen-containing vacuoles, releasing pathogens into the cytosol (PubMed:24715728, PubMed:24739961). Following pathogen release in the cytosol, forms a protein coat in a GTPase-dependent manner that encapsulates pathogens and promotes the detection of ligands by pattern recognition receptors (By similarity). Plays a key role in inflammasome assembly in response to infection by Gram-negative bacteria: following pathogen release in the cytosol, forms a protein coat that encapsulates Gram-negative bacteria and directly binds to lipopolysaccharide (LPS), disrupting the O-antigen barrier and unmasking lipid A that is that detected by the non-canonical inflammasome effector CASP4/CASP11 (PubMed:24715728, PubMed:24739961). Also promotes recruitment of proteins that mediate bacterial cytolysis, leading to release double-stranded DNA (dsDNA) that activates the AIM2 inflammasome (PubMed:24715728, PubMed:24739961). Involved in autophagy by regulating bacteriolytic peptide generation via its interaction with ubiquitin-binding protein SQSTM1, which delivers monoubiquitinated proteins to autolysosomes for the generation of bacteriolytic peptides (PubMed:21551061). Confers protection to several pathogens, including the bacterial pathogens L.monocytogenes and M.bovis BCG as well as the protozoan pathogen T.gondii (PubMed:18025219, PubMed:21551061). Exhibits antiviral activity against influenza virus (By similarity). {ECO:0000250|UniProtKB:P32455, ECO:0000269|PubMed:18025219, ECO:0000269|PubMed:21551061, ECO:0000269|PubMed:24715728, ECO:0000269|PubMed:24739961}.
uniprot
proteins
mass_dalton
67712
uniprot
proteins
mutagenesis
MUTAGEN 48; /note="R->P: Loss of localization to cytoplasmic vesicle."; /evidence="ECO:0000269|PubMed:21551061"; MUTAGEN 52; /note="S->N: Loss of catalytic activity and localization to cytoplasmic vesicle."; /evidence="ECO:0000269|PubMed:21551061
uniprot
proteins
post_translational_modification
PTM: Isoprenylation of mouse GBP1 is incomplete (PubMed:10888661). It persistently exists in the cell as a mixture of C20-modified and (more predominantly) unmodified form (PubMed:10888661). Isoprenylation is required for proper subcellular location (By similarity). {ECO:0000250|UniProtKB:P32455, ECO:0000269|PubMed:10888661}.; PTM: Phosphorylated at Ser-156 by PIM1 in absence of infection, inhibits GBP1: phosphorylation promotes interaction with 14-3-3 protein sigma (SFN), leading to GBP1 retention in the cytosol. Dephosphorylated in response to infection, liberating GBP1. {ECO:0000250|UniProtKB:P32455}.
uniprot
proteins
protein_family
GB1 subfamily
uniprot
proteins
protein_family
GB1/RHD3 GTPase family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
10888661
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1715024
uniprot
proteins
pubmed
1753106
uniprot
proteins
pubmed
18025219
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21551061
uniprot
proteins
pubmed
24715728
uniprot
proteins
pubmed
24739961
uniprot
proteins
sequence_length
589
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18025219, ECO:0000269|PubMed:21551061}; Lipid-anchor {ECO:0000250|UniProtKB:P32455}; Cytoplasmic side {ECO:0000250|UniProtKB:P32455}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P32455}; Lipid-anchor {ECO:0000250|UniProtKB:P32455}; Cytoplasmic side {ECO:0000250|UniProtKB:P32455}. Cell membrane {ECO:0000250|UniProtKB:P32455}; Lipid-anchor {ECO:0000250|UniProtKB:P32455}; Cytoplasmic side {ECO:0000250|UniProtKB:P32455}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P32455}. Secreted {ECO:0000250|UniProtKB:P32455}. Note=Localizes to pathogen-containing vacuoles or to the cell surface of bacteria that escaped vacuoles. Secreted from endothelial cells in the cerebrospinal fluid, upon bacterial challenge and independently of IFNG induction. Golgi membrane localization requires isoprenylation and the presence of another IFNG-induced factor. Sequestered in the cytosol following phosphorylation by PIM1 and subsequent interaction with 14-3-3 protein sigma (SFN). {ECO:0000250|UniProtKB:P32455}.
uniprot
proteins