IDH3G
entrez
3421
canonical
uniprot
P51553
canonical
ensembl
ENSG00000067829
resolver
ensp
ENSP00000217901
resolver
ensp
ENSP00000359110
resolver
genesymbol
IDH3G
resolver
hgnc
HGNC:5386
resolver
uniprot
E9PDD5
resolver
uniprot
O15384
resolver
uniprot
Q9BUU5
resolver
uniprot_entry
IDH3G_HUMAN
resolver
uniprot_entry
O15384_HUMAN
resolver
uniprot_sec
E9PDD5
resolver
uniprot_sec
Q9BUU5
resolver
activity_regulation
ACTIVITY REGULATION: The heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits can be allosterically activated by citrate (CIT) or/and ADP, and the two activators can act independently or synergistically. The heterodimer composed of IDH3A and IDH3B subunits cannot be allosterically regulated and the allosteric regulation of the heterotetramer is through the IDH3G subunit and not the IDH3B subunit. The IDH3G subunit contains the allosteric site which consists of a CIT-binding site and an ADP-binding site, and the binding of CIT and ADP causes conformational changes at the allosteric site which are transmitted to the active site in the catalytic subunit (IDH3A) through a cascade of conformational changes at the heterodimer interface, leading to stabilization of the isocitrate-binding at the active site and thus activation of the enzyme. ATP can activate the heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits at low concentrations but inhibits their activities at high concentrations, whereas ATP exhibits only inhibitory effect on the heterodimer composed of IDH3A and IDH3B subunits. {ECO:0000269|PubMed:28098230, ECO:0000269|PubMed:28139779}.
uniprot
proteins
amino_acid_sequence
MALKVATVAGSAAKAVLGPALLCRPWEVLGAHEVPSRNIFSEQTIPPSAKYGGRHTVTMIPGDGIGPELMLHVKSVFRHACVPVDFEEVHVSSNADEEDIRNAIMAIRRNRVALKGNIETNHNLPPSHKSRNNILRTSLDLYANVIHCKSLPGVVTRHKDIDILIVRENTEGEYSSLEHESVAGVVESLKIITKAKSLRIAEYAFKLAQESGRKKVTAVHKANIMKLGDGLFLQCCREVAARYPQITFENMIVDNTTMQLVSRPQQFDVMVMPNLYGNIVNNVCAGLVGGPGLVAGANYGHVYAVFETATRNTGKSIANKNIANPTATLLASCMMLDHLKLHSYATSIRKAVLASMDNENMHTPDIGGQGTTSEAIQDVIRHIRVINGRAVEA
uniprot
proteins
disease_involvement
DISEASE: Retinitis pigmentosa 99 (RP99) [MIM:301148]: An X-linked recessive form of retinitis pigmentosa, a retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. {ECO:0000269|PubMed:40119724}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers. {ECO:0000269|PubMed:28139779}.
uniprot
proteins
mass_dalton
42794
uniprot
proteins
mutagenesis
MUTAGEN 117; /note="N->A: No effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 120; /note="T->A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 130; /note="S->A: No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 133; /note="N->A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 136; /note="R->A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 167; /note="R->A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 173; /note="E->A: No effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 174; /note="Y->F: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 190; /note="K->A: Complete loss of the activation of the heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP."; /evidence="ECO:0000269|PubMed:28098230, ECO:0000269|PubMed:28139779"; MUTAGEN 229; /note="D->A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 276; /note="Y->F: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 311; /note="R->A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 312; /note="N->A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 313; /note="T->A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 315; /note="K->A: No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP."; /evidence="ECO:0000269|PubMed:28098230"; MUTAGEN 324; /note="N->A: Complete loss of the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP."; /evidence="ECO:0000269|PubMed:28098230
uniprot
proteins
protein_family
Isocitrate and isopropylmalate dehydrogenases family
uniprot
proteins
pubmed
10601238
uniprot
proteins
pubmed
11256614
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28098230
uniprot
proteins
pubmed
28139779
uniprot
proteins
pubmed
40119724
uniprot
proteins
pubmed
9286695
uniprot
proteins
sequence_length
393
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11256614, ECO:0000269|PubMed:40119724}. Photoreceptor inner segment {ECO:0000269|PubMed:40119724}.
uniprot
proteins