GNAI3_CRIGR
ID GNAI3_CRIGR Reviewed; 63 AA.
AC Q60397;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-3;
DE AltName: Full=G(i) alpha-3;
DE Flags: Fragment;
GN Name=GNAI3;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7698751; DOI=10.1006/geno.1994.1618;
RA Baron B., Fernandez M.A., Toledo F., le Roscouet D., Mayau V., Martin N.,
RA Buttin G., Debatisse M.;
RT "The highly conserved Chinese hamster GNAI3 gene maps less than 60 kb from
RT the AMPD2 gene and lacks the intronic U6 snRNA present in its human
RT counterpart.";
RL Genomics 24:288-294(1994).
CC -!- FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G
CC proteins) function as transducers downstream of G protein-coupled
CC receptors (GPCRs) in numerous signaling cascades. The alpha chain
CC contains the guanine nucleotide binding site and alternates between an
CC active, GTP-bound state and an inactive, GDP-bound state. Signaling by
CC an activated GPCR promotes GDP release and GTP binding. The alpha
CC subunit has a low GTPase activity that converts bound GTP to GDP,
CC thereby terminating the signal. Both GDP release and GTP hydrolysis are
CC modulated by numerous regulatory proteins. Signaling is mediated via
CC effector proteins, such as adenylate cyclase. Inhibits adenylate
CC cyclase activity, leading to decreased intracellular cAMP levels.
CC Stimulates the activity of receptor-regulated K(+) channels. The active
CC GTP-bound form prevents the association of RGS14 with centrosomes and
CC is required for the translocation of RGS14 from the cytoplasm to the
CC plasma membrane. May play a role in cell division.
CC {ECO:0000250|UniProtKB:P08754}.
CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta
CC and gamma. The alpha subunit contains the guanine nucleotide binding
CC site. GTP binding causes dissociation of the heterotrimer, liberating
CC the individual subunits so that they can interact with downstream
CC effector proteins. Forms a complex with CCDC88A/GIV and EGFR which
CC leads to enhanced EGFR signaling and triggering of cell migration;
CC ligand stimulation is required for recruitment of GNAI3 to the complex
CC (By similarity). Interacts (inactive GDP-bound form) with CCDC88A/GIV
CC (via GBA motif); the interaction leads to activation of GNAI3 (By
CC similarity). Interacts (inactive GDP-bound form) with CCDC88C/DAPLE
CC (via GBA motif); the interaction leads to activation of GNAI3 (By
CC similarity). Interacts (inactive GDP-bound form) with NUCB1 (via GBA
CC motif) and NUCB2 (via GBA motif); the interaction leads to activation
CC of GNAI3 (By similarity). Interacts (inactive GDP-bound form) with
CC PLCD4 (via GBA motif); the interaction leads to activation of GNAI3 (By
CC similarity). Interacts with INSR; the interaction is probably mediated
CC by CCDC88A/GIV (By similarity). Interacts with GPSM1. Interacts (GDP-
CC bound form) with GPSM2 (via GoLoco domains). Does not interact with
CC RGS2. Interacts with RGS8 and RGS10; this strongly enhances the
CC intrinsic GTPase activity. Interacts with RGS12. Interacts with RGS16;
CC this strongly enhances the intrinsic GTPase activity. Interacts (via
CC active GTP- or inactive GDP-bound form) with RGS14.
CC {ECO:0000250|UniProtKB:P08753, ECO:0000250|UniProtKB:P08754,
CC ECO:0000250|UniProtKB:Q9DC51}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08754}. Cell
CC membrane {ECO:0000250|UniProtKB:P08754}; Lipid-anchor {ECO:0000305}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P08754}. Note=Localizes in the centrosomes of
CC interphase and mitotic cells. Detected at the cleavage furrow and/or
CC the midbody. {ECO:0000250|UniProtKB:P08754}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; X79282; CAA55869.1; -; Genomic_DNA.
DR PIR; I48071; I48071.
DR AlphaFoldDB; Q60397; -.
DR SMR; Q60397; -.
DR STRING; 10029.NP_001230987.1; -.
DR eggNOG; KOG0082; Eukaryota.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001408; Gprotein_alpha_I.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR PRINTS; PR00441; GPROTEINAI.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell membrane; Cytoplasm; Cytoskeleton;
KW GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Transducer.
FT CHAIN <1..63
FT /note="Guanine nucleotide-binding protein G(i) subunit
FT alpha-3"
FT /id="PRO_0000203691"
FT DOMAIN <1..63
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION <1..?1
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION <1..?1
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION <1..?1
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION <1..?1
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 33..38
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT NON_TER 1
SQ SEQUENCE 63 AA; 7288 MW; 32C3A203F194ADB9 CRC64;
GSNTYEEAAA YIQCQFEDLN RRKDTKEIYT HFTCATDTKN VQFVFDAVTD VIIKNNLKEC
GLY
