Ric8a
entrez
293614
canonical
uniprot
Q80ZG1
canonical
ensembl
ENSRNOG00000013256
resolver
ensp
ENSRNOP00000018470
resolver
enst
ENSRNOT00000018470
resolver
genesymbol
Ric8a
resolver
uniprot
B1H241
resolver
uniprot
F7F506
resolver
uniprot_entry
F7F506_RAT
resolver
uniprot_entry
RIC8A_RAT
resolver
uniprot_sec
B1H241
resolver
amino_acid_sequence
MEPRAVADALETGEEDAVTEALRSFNREHSQSFTFDDAQQEDRKRLAKLLVSVLEQGLSPKHRVTWLQTIRILSRDRSCLDSFASRQSLHALACYADIAISEEPIPQPPDMDVLLESLKCLCNLVLSSPTAQMLAAEARLVVRLAERVGLYRKRSYPHEVQFFDLRLLFLLTALRTDVRQQLFQELHGVRLLTDALELTLGVAPKENPLVILPAQETERAMEILKVLFNITYDSVKREVDEEDAALYRYLGTLLRHCVMADAAGDRTEEFHGHTVNLLGNLPLKCLDVLLALELHEGSLEFMGVNMDVINALLAFLEKRLHQTHRLKECVAPVLSVLTECARMHRPARKFLKAQVLPPLRDVRTRPEVGDLLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLAARGLMAGGRPEGQYSEDEDTDTEEYREAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAMKLVNMFDKLSRHRLIQPMGMSPRGHLTSLQDAMCETMEGQLSSDPDSDPD
uniprot
proteins
function
FUNCTION: Chaperone that specifically binds and folds nascent G alpha proteins prior to G protein heterotrimer formation, promoting their stability and activity: folds GNAI1, GNAO1, GNA13 and GNAQ (PubMed:29844055, PubMed:32103024, PubMed:32126208). Does not fold G(s) G-alpha proteins GNAS nor GNAL (PubMed:29844055). Also acts as a guanine nucleotide exchange factor (GEF) for G alpha proteins by stimulating exchange of bound GDP for free GTP (PubMed:12509430, PubMed:16275912, PubMed:29844055, PubMed:31155309, PubMed:32103024). Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein (GNAI1), possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex (PubMed:12509430, PubMed:16275912). Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation (By similarity). {ECO:0000250|UniProtKB:Q9NPQ8, ECO:0000269|PubMed:12509430, ECO:0000269|PubMed:16275912, ECO:0000269|PubMed:29844055, ECO:0000269|PubMed:31155309, ECO:0000269|PubMed:32103024, ECO:0000269|PubMed:32126208}.
uniprot
proteins
mass_dalton
59827
uniprot
proteins
mutagenesis
MUTAGEN 71; /note="R->E: Abolished ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 123; /note="N->A: Abolished ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 163; /note="F->A: Does not affect ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 174; /note="L->W: Does not affect ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 225; /note="K->A: Does not affect ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 228; /note="F->W: Does not affect ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 273; /note="Missing: Reduced ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 365..367; /note="RPE->APA: Does not affect ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 381; /note="T->A: Does not affect ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 383; /note="L->E: Reduced ability to promote guanine exchange of G-alpha proteins."; /evidence="ECO:0000269|PubMed:32103024"; MUTAGEN 389; /note="R->A: Does not greatly affect ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 412; /note="Y->A: Does not affect ability to promote guanine exchange of G-alpha proteins."; /evidence="ECO:0000269|PubMed:32103024"; MUTAGEN 415; /note="A->W: Strongly reduced ability to promote guanine exchange of G-alpha proteins."; /evidence="ECO:0000269|PubMed:32103024"; MUTAGEN 416; /note="A->W: Does not greatly affect ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 420; /note="Missing: Abolished ability to fold GNAQ."; /evidence="ECO:0000269|PubMed:32126208"; MUTAGEN 435; /note="S->A: Decreased ability to fold G-alpha proteins."; /evidence="ECO:0000269|PubMed:29844055, ECO:0000269|PubMed:31155309, ECO:0000269|PubMed:32103024"; MUTAGEN 435; /note="S->D: Mimics phosphorylation; partial ability to fold G-alpha proteins."; /evidence="ECO:0000269|PubMed:29844055"; MUTAGEN 440; /note="T->A: Decreased ability to fold G-alpha proteins."; /evidence="ECO:0000269|PubMed:29844055, ECO:0000269|PubMed:31155309, ECO:0000269|PubMed:32103024"; MUTAGEN 440; /note="T->D: Mimics phosphorylation; partial ability to fold G-alpha proteins."; /evidence="ECO:0000269|PubMed:29844055"; MUTAGEN 478; /note="E->A,K: Reduced ability to promote guanine exchange of G-alpha proteins."; /evidence="ECO:0000269|PubMed:32103024"; MUTAGEN 482; /note="L->D: Reduced ability to promote guanine exchange of G-alpha proteins."; /evidence="ECO:0000269|PubMed:32103024
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-435 and Thr-440 by CK2, stabilizing its interface with G alpha proteins. {ECO:0000269|PubMed:29844055, ECO:0000269|PubMed:32103024, ECO:0000269|PubMed:32126208}.
uniprot
proteins
protein_family
Synembryn family
uniprot
proteins
pubmed
12509430
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
16275912
uniprot
proteins
pubmed
21158412
uniprot
proteins
pubmed
29844055
uniprot
proteins
pubmed
31155309
uniprot
proteins
pubmed
32103024
uniprot
proteins
pubmed
32126208
uniprot
proteins
sequence_length
530
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:21158412}. Cytoplasm {ECO:0000269|PubMed:21158412}.
uniprot
proteins