GNAI3_XENLA
ID GNAI3_XENLA Reviewed; 345 AA.
AC P27045;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=2116977; DOI=10.1016/0014-5793(90)80964-k;
RA Olate J., Martinez S., Purcell P., Jorquera H., Codina J., Birnbaumer L.,
RA Allende J.E.;
RT "Molecular cloning and sequence determination of four different cDNA
RT species coding for alpha-subunits of G proteins from Xenopus laevis
RT oocytes.";
RL FEBS Lett. 268:27-31(1990).
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. May play a
CC role in cell division. {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 (By similarity). {ECO:0000250|UniProtKB:P08754}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08754}. Cell
CC membrane {ECO:0000250|UniProtKB:P08754}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P08754}. Membrane
CC {ECO:0000250|UniProtKB:P08754}; Lipid-anchor
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; X56090; CAA39570.1; -; mRNA.
DR PIR; S11046; RGXLI3.
DR AlphaFoldDB; P27045; -.
DR SMR; P27045; -.
DR Proteomes; UP000186698; Genome assembly.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001408; Gprotein_alpha_I.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell membrane; Cytoplasm; Cytoskeleton;
KW GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transducer.
FT CHAIN <1..345
FT /note="Guanine nucleotide-binding protein G(i) subunit
FT alpha-3"
FT /id="PRO_0000203695"
FT DOMAIN 23..345
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 26..39
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 164..172
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 187..196
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 256..263
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 315..320
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 34..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 141..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 166..172
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 191..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 260..263
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 317
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT NON_TER 1
SQ SEQUENCE 345 AA; 39648 MW; 74E070802EABA352 CRC64;
REAAERSKMI DRNLREDGEK ASKEVKLLLL GAGESGKSTI VKQMKIIHED GYSEEECRQY
KVVVYSNTIQ SIIAIIRAMG RLRIDFGDVA RADDARQLFV LASSAEEGVM SPELAGVIQR
LWEDSGVQAC FSRSREYQLN DSASYYLSDI ERIAQGSYIP TQQDVLRTRV KTTGIVETHF
TFKDLYFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSD YDLLLAEDEE MNRMHESMKL
FDSICNNKWF IDTSIILFLN KKDLFEEKIS RSPLTICYPE YSGSNTYEEA AAYIQCQFED
LNRRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKSNLM ECGLY
