G3BP1_PONAB
ID G3BP1_PONAB Reviewed; 466 AA.
AC Q5RB87; Q5RBE0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 122.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR858711; CAH90920.1; -; mRNA.
DR EMBL; CR858766; CAH90973.1; -; mRNA.
DR RefSeq; NP_001125562.1; NM_001132090.1.
DR RefSeq; XP_009239479.1; XM_009241204.1.
DR RefSeq; XP_009239480.1; XM_009241205.1.
DR RefSeq; XP_009239481.1; XM_009241206.1.
DR AlphaFoldDB; Q5RB87; -.
DR SMR; Q5RB87; -.
DR STRING; 9601.ENSPPYP00000017869; -.
DR Ensembl; ENSPPYT00000018585; ENSPPYP00000017869; ENSPPYG00000015968.
DR GeneID; 100172476; -.
DR KEGG; pon:100172476; -.
DR CTD; 10146; -.
DR eggNOG; KOG0116; Eukaryota.
DR GeneTree; ENSGT00390000011365; -.
DR HOGENOM; CLU_022209_0_2_1; -.
DR InParanoid; Q5RB87; -.
DR OMA; RCKGPQG; -.
DR OrthoDB; 1526879at2759; -.
DR TreeFam; TF325464; -.
DR Proteomes; UP000001595; Chromosome 5.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
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..466
FT /note="Ras GTPase-activating protein-binding protein 1"
FT /id="PRO_0000271371"
FT DOMAIN 11..133
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 340..415
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 144..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..430
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 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 376
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 429
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 435
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 435
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 447
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97855"
FT MOD_RES 460
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 460
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 465
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT CROSSLNK 376
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT CONFLICT 319
FT /note="I -> V (in Ref. 1; CAH90920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 52192 MW; FF9429D1BA9E3673 CRC64;
MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY VHGGLDSNGK PADAVYGQKE
IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN NNQALRRFMQ TFVLAPEGSV
ANKFYVHNDI FRYQDEVFGG FVTEPQEESE EEVEEPEERQ QTPEVVPDDS GTFYDQAVVS
NDMEEHLEEP VAEPEPDPEP EPEQEPVSEI QEEKPEPVLE ETVPEDAQKS SSPAPADIAQ
TVQEDLRTFS WASVTSKNLP PSGAVPVTGI PPHVVKVPAS QPRPESKPES QIPPQRPQRD
QRVREQRINI PPQRGPRPIR EAGEQGDIEP RRMVRHPDSH QLFIGNLPHE VDKSELKDFF
QSYGNVVELR INSGGKLPNF GFVVFDDSEP VQKVLSNRPI MFRGEVRLNV EEKKTRAARE
GDRRDNRLRG PGGPRGGLGG GMRGPPRGGM VQKPGFGVGR GLAPRQ
