GNAI3
entrez
2773
canonical
uniprot
P08754
canonical
ensembl
ENSG00000065135
resolver
ensp
ENSP00000358867
resolver
ensp
ENSP00000549799
resolver
ensp
ENSP00000549802
resolver
ensp
ENSP00000590702
resolver
enst
ENST00000369851
resolver
enst
ENST00000879740
resolver
enst
ENST00000879743
resolver
enst
ENST00000920643
resolver
genesymbol
GNAI3
resolver
hgnc
HGNC:4387
resolver
uniprot
P17539
resolver
uniprot
Q5TZX1
resolver
uniprot_entry
GNAI3_HUMAN
resolver
uniprot_sec
P17539
resolver
uniprot_sec
Q5TZX1
resolver
amino_acid_sequence
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTPELAGVIKRLWRDGGVQACFSRSREYQLNDSASYYLNDLDRISQSNYIPTQQDVLRTRVKTTGIVETHFTFKDLYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTETSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKECGLY
uniprot
proteins
disease_involvement
DISEASE: Auriculocondylar syndrome 1 (ARCND1) [MIM:602483]: An autosomal dominant form of auriculocondylar syndrome, a craniofacial malformation syndrome characterized by variable mandibular anomalies, including mild to severe micrognathia, temporomandibular joint ankylosis, cleft palate, and a characteristic ear malformation that consists of separation of the lobule from the external ear, giving the appearance of a question mark (question-mark ear). Other frequently described features include prominent cheeks, cupped and posteriorly rotated ears, preauricular tags, and microstomia. Glossoptosis, masticatory abnormalities, orthodontic problems, and malocclusion occur in a majority of affected subjects. {ECO:0000269|PubMed:22560091, ECO:0000269|PubMed:23315542, ECO:0000269|PubMed:34789173, ECO:0000269|PubMed:35170830}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (By similarity). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:18434541, PubMed:19478087, PubMed:8774883). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (PubMed:19478087). Stimulates the activity of receptor-regulated K(+) channels (PubMed:2535845). The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division (PubMed:17635935). The active GTP-bound form activates the calcium permeant TRPC5 ion channels (PubMed:37137991). {ECO:0000250|UniProtKB:P08753, ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:2535845, ECO:0000269|PubMed:37137991, ECO:0000269|PubMed:8774883}.
uniprot
proteins
mass_dalton
40532
uniprot
proteins
mutagenesis
MUTAGEN 35; /note="K->A: Decreased affinity for PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 36; /note="L->A: Increased affinity for PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 37; /note="L->A: No effect on binding to PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 39; /note="L->A: Decreased affinity for PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 42; /note="G->R: Decreased affinity for PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 184; /note="I->A: No effect on binding to PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 211; /note="W->A: Decreased affinity for CCDC88C and PLCD4."; /evidence="ECO:0000269|PubMed:26126266, ECO:0000269|PubMed:30194280"; MUTAGEN 215; /note="F->A: Decreased affinity for CCDC88C and PLCD4."; /evidence="ECO:0000269|PubMed:26126266, ECO:0000269|PubMed:30194280"; MUTAGEN 218; /note="V->A: No effect on binding to PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 248; /note="K->M: No effect on binding to CCDC88C."; /evidence="ECO:0000269|PubMed:26126266"; MUTAGEN 249; /note="L->H: Decreased affinity for PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 249; /note="L->V: No effect on binding to PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 252; /note="S->A: Increased affinity for PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 252; /note="S->D: Decreased affinity for PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 256; /note="N->A: Decreased affinity for PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 256; /note="N->E: Decreased affinity for PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 257; /note="K->A: No effect on binding to PLCD4."; /evidence="ECO:0000269|PubMed:30194280"; MUTAGEN 258; /note="W->F: Increased affinity for PLCD4. No effect on binding to CCDC88C."; /evidence="ECO:0000269|PubMed:26126266, ECO:0000269|PubMed:30194280"; MUTAGEN 259; /note="F->A: No effect on binding to PLCD4."; /evidence="ECO:0000269|PubMed:30194280
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Deamidated at Gln-204 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA. {ECO:0000269|PubMed:24141704}.
uniprot
proteins
protein_family
G(i/o/t/z) subfamily
uniprot
proteins
protein_family
G-alpha family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16870394
uniprot
proteins
pubmed
17635935
uniprot
proteins
pubmed
18434541
uniprot
proteins
pubmed
19211784
uniprot
proteins
pubmed
19478087
uniprot
proteins
pubmed
20462955
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22560091
uniprot
proteins
pubmed
22952234
uniprot
proteins
pubmed
23315542
uniprot
proteins
pubmed
24141704
uniprot
proteins
pubmed
2440724
uniprot
proteins
pubmed
2452165
uniprot
proteins
pubmed
25187647
uniprot
proteins
pubmed
25255805
uniprot
proteins
pubmed
2535845
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26126266
uniprot
proteins
pubmed
27864364
uniprot
proteins
pubmed
2834384
uniprot
proteins
pubmed
30194280
uniprot
proteins
pubmed
3109953
uniprot
proteins
pubmed
3120178
uniprot
proteins
pubmed
3132707
uniprot
proteins
pubmed
34789173
uniprot
proteins
pubmed
35170830
uniprot
proteins
pubmed
37137991
uniprot
proteins
pubmed
8774883
uniprot
proteins
sequence_length
354
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17635935}. Cell membrane {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:27864364}; Lipid-anchor {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody. {ECO:0000269|PubMed:17635935}.
uniprot
proteins