G3BP1_BOVIN
ID G3BP1_BOVIN Reviewed; 465 AA.
AC Q32LC7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ras GTPase-activating protein-binding protein 1;
DE Short=G3BP-1;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q13283};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q13283};
DE AltName: Full=ATP-dependent DNA/RNA helicase G3BP;
GN Name=G3BP1; Synonyms=G3BP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP- and magnesium-dependent helicase that plays an essential
CC role in innate immunity. Participates in the DNA-triggered cGAS/STING
CC pathway by promoting the DNA binding and activation of CGAS. Enhances
CC also DDX58-induced type I interferon production probably by helping
CC DDX58 at sensing pathogenic RNA. In addition, plays an essential role
CC in stress granule formation. Unwinds preferentially partial DNA and RNA
CC duplexes having a 17 bp annealed portion and either a hanging 3' tail
CC or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and
CC RNA/RNA substrates with comparable efficiency. Acts unidirectionally by
CC moving in the 5' to 3' direction along the bound single-stranded DNA.
CC Phosphorylation-dependent sequence-specific endoribonuclease in vitro.
CC Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA
CC preferentially at the 3'-UTR. {ECO:0000250|UniProtKB:Q13283}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q13283};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:Q13283};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q13283};
CC Note=Mg(2+) is required for helicase activity.
CC {ECO:0000250|UniProtKB:Q13283};
CC -!- SUBUNIT: Homodimer and oligomer (By similarity). Component of a TAU
CC mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP1 (By
CC similarity). Binds to the SH3 domain of Ras GTPase-activating protein
CC (RASA1) in proliferating cells (By similarity). No interaction in
CC quiescent cells (By similarity). Interacts (via NTF2-like domain) with
CC USP10. Interacts with RPTOR and SPAG5; this complex is increased by
CC oxidative stress. Interacts with ATXN2L. Interacts with STYXL1.
CC Interacts with CGAS (via N-terminus); this interaction promotes the
CC DNA-binding and activation of CGAS. Interacts (via C-terminus) with
CC DDX58. Interacts (via NTF2-like domain) with CAPRIN1. Interacts with
CC PABPC1 (By similarity). {ECO:0000250|UniProtKB:P97855,
CC ECO:0000250|UniProtKB:Q13283}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P97855}. Perikaryon
CC {ECO:0000250|UniProtKB:P97855}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q13283}. Nucleus {ECO:0000250|UniProtKB:Q13283}.
CC Note=Cytoplasmic in proliferating cells, can be recruited to the plasma
CC membrane in exponentially growing cells. Cytosolic and partially
CC nuclear in resting cells. Recruited to stress granules in response to
CC arsenite treatment. The unphosphorylated form is recruited to stress
CC granules. HRAS signaling contributes to this process by regulating G3BP
CC dephosphorylation. {ECO:0000250|UniProtKB:Q13283}.
CC -!- DOMAIN: The NTF2 domain mediates multimerization. {ECO:0000250}.
CC -!- PTM: Phosphorylated exclusively on serine residues. Hyperphosphorylated
CC in quiescent fibroblasts. Hypophosphorylation leads to a decrease in
CC endoribonuclease activity. RASA1-dependent phosphorylation of Ser-149
CC induces a conformational change that prevents self-association.
CC Dephosphorylation after HRAS activation is required for stress granule
CC assembly. Ser-149 phosphorylation induces partial nuclear localization
CC (By similarity). {ECO:0000250}.
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DR EMBL; BC109645; AAI09646.1; -; mRNA.
DR RefSeq; NP_001032700.1; NM_001037611.2.
DR AlphaFoldDB; Q32LC7; -.
DR SMR; Q32LC7; -.
DR STRING; 9913.ENSBTAP00000027067; -.
DR PaxDb; Q32LC7; -.
DR PeptideAtlas; Q32LC7; -.
DR PRIDE; Q32LC7; -.
DR Ensembl; ENSBTAT00000027067; ENSBTAP00000027067; ENSBTAG00000020309.
DR GeneID; 534214; -.
DR KEGG; bta:534214; -.
DR CTD; 10146; -.
DR VEuPathDB; HostDB:ENSBTAG00000020309; -.
DR VGNC; VGNC:29176; G3BP1.
DR eggNOG; KOG0116; Eukaryota.
DR GeneTree; ENSGT00390000011365; -.
DR HOGENOM; CLU_022209_0_2_1; -.
DR InParanoid; Q32LC7; -.
DR OMA; RCKGPQG; -.
DR OrthoDB; 1526879at2759; -.
DR TreeFam; TF325464; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000020309; Expressed in pharyngeal tonsil and 110 other tissues.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0033677; F:DNA/RNA helicase activity; IEA:Ensembl.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0062029; P:positive regulation of stress granule assembly; IEA:Ensembl.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IEA:Ensembl.
DR GO; GO:0034063; P:stress granule assembly; IEA:Ensembl.
DR CDD; cd00780; NTF2; 1.
DR CDD; cd12463; RRM_G3BP1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034375; G3BP1.
DR InterPro; IPR034374; G3BP1_RRM.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR039539; Ras_GTPase_bind_prot.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10693; PTHR10693; 1.
DR PANTHER; PTHR10693:SF21; PTHR10693:SF21; 1.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; DNA-binding; Endonuclease; Helicase;
KW Hydrolase; Immunity; Innate immunity; Isopeptide bond; Methylation;
KW Nuclease; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Transport; Ubl conjugation.
FT CHAIN 1..465
FT /note="Ras GTPase-activating protein-binding protein 1"
FT /id="PRO_0000271370"
FT DOMAIN 11..133
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 339..414
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 145..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..205
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 375
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 428
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 434
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 434
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 446
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97855"
FT MOD_RES 459
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 459
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 464
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
SQ SEQUENCE 465 AA; 52122 MW; DFD85B9BDD9F7307 CRC64;
MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY VHGGLDSNGK PADAVYGQKE
IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN NNQALRRFMQ TFVLAPEGSV
ANKFYVHNDI FRYQDEVFGG FITEPQEESE EEVEEPEERQ QTPEVVPDDS GTFYDQTVSN
DLEEHLEEPV AEPEPEPEPE PEQEPVSEVQ EEKSEPVLEE TAPEDVQKSS SPAPADIAQT
VQEDLRTFSW ASVTSKNLPP SGAVPVTGIP PHVVKVPASQ PRPESKPESQ IPLQRPQRDQ
RVREQRINVP PQRGPRPVRE AGEQGDVEPR RIVRHPDSHQ LFIGNLPHEV DKSELKDFFQ
NYGNVVELRI NSGGKLPNFG FVVFDDSEPV QKVLSNRPIM FRGEVRLNVE EKKTRAAREG
DRRDNRLRGP GGPRGGLGGG MRGPPRGGMV QKPGFGVGRS IAPRQ
