GNAI1_BOVIN
ID GNAI1_BOVIN Reviewed; 354 AA.
AC P63097; P04898; P11015; P31871; Q2KJC0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-1;
DE AltName: Full=Adenylate cyclase-inhibiting G alpha protein;
GN Name=GNAI1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2419165; DOI=10.1016/0014-5793(86)80347-7;
RA Nukada T., Tanabe T., Takahashi H., Noda M., Haga K., Haga T., Ichiyama A.,
RA Kangawa K., Hiranaga M., Matsuo H., Numa S.;
RT "Primary structure of the alpha-subunit of bovine adenylate cyclase-
RT inhibiting G-protein deduced from the cDNA sequence.";
RL FEBS Lett. 197:305-310(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-354.
RX PubMed=3094012; DOI=10.1073/pnas.83.20.7663;
RA Michel T., Winslow J.W., Smith J.A., Seidman J.G., Neer E.J.;
RT "Molecular cloning and characterization of cDNA encoding the GTP-binding
RT protein alpha i and identification of a related protein, alpha h.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7663-7667(1986).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as
CC transducers downstream of G protein-coupled receptors (GPCRs) in
CC numerous signaling cascades. The alpha chain contains the guanine
CC nucleotide binding site and alternates between an active, GTP-bound
CC state and an inactive, GDP-bound state. Signaling by an activated GPCR
CC promotes GDP release and GTP binding. The alpha subunit has a low
CC GTPase activity that converts bound GTP to GDP, thereby terminating the
CC signal. Both GDP release and GTP hydrolysis are modulated by numerous
CC regulatory proteins (By similarity). Signaling is mediated via effector
CC proteins, such as adenylate cyclase. Inhibits adenylate cyclase
CC activity, leading to decreased intracellular cAMP levels (By
CC similarity). The inactive GDP-bound form prevents the association of
CC RGS14 with centrosomes and is required for the translocation of RGS14
CC from the cytoplasm to the plasma membrane. Required for normal
CC cytokinesis during mitosis (By similarity). Required for cortical
CC dynein-dynactin complex recruitment during metaphase (By similarity).
CC {ECO:0000250|UniProtKB:P10824, ECO:0000250|UniProtKB:P63096}.
CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta
CC and gamma. The alpha chain contains the guanine nucleotide binding
CC site. Part of a spindle orientation complex at least composed of GNAI1,
CC GPSM2 and NUMA1. Identified in complex with the beta subunit GNB1 and
CC the gamma subunit GNG1. Identified in complex with the beta subunit
CC GNB1 and the gamma subunit GNG2. GTP binding causes dissociation of the
CC heterotrimer, liberating the individual subunits so that they can
CC interact with downstream effector proteins. Interacts (GDP-bound form)
CC with GPSM1; this inhibits guanine nucleotide exchange and GTP binding.
CC Interacts (GDP-bound form) with GPSM2 (via GoLoco domains); this
CC inhibits guanine nucleotide exchange. Interacts with RGS10; this
CC strongly enhances GTP hydrolysis. Interacts with RGS1 and RGS16; this
CC strongly enhances GTPase activity. Interacts with RGS4. Interacts with
CC RGS12. Interacts (via active GTP- or inactive GDP-bound forms) with
CC RGS14 (via RGS and GoLoco domains). Interacts with RGS3, RGS6, RGS7,
CC RGS8, RGS17, RGS18 and RGS20 (in vitro). Interacts (GDP-bound form)
CC with RIC8A (via C-terminus). Interacts (inactive GDP-bound form) with
CC NUCB1 (via GBA motif); the interaction leads to activation of GNAI1 (By
CC similarity). Interacts (inactive GDP-bound form) with CCDC88C/DAPLE
CC (via GBA motif); the interaction leads to activation of GNAI1 (By
CC similarity). Interacts (inactive GDP-bound form) with CCDC8A/GIV (via
CC GBA motif) (By similarity). {ECO:0000250|UniProtKB:P10824,
CC ECO:0000250|UniProtKB:P63096}.
CC -!- INTERACTION:
CC P63097; P62871: GNB1; NbExp=3; IntAct=EBI-8309073, EBI-357141;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10824}. Cytoplasm
CC {ECO:0000250|UniProtKB:P10824}. Cell membrane
CC {ECO:0000250|UniProtKB:P10824}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P10824}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P10824}.
CC Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P63096}. Membrane
CC {ECO:0000250|UniProtKB:P10824}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P10824}. Note=Localizes in the centrosomes of
CC interphase and mitotic cells, but not in centrosomes during
CC cytokinesis. Detected at the cleavage furrow or the midbody. Localized
CC at the plasma membrane throughout mitosis. Colocalizes with RIC8A and
CC RGS14 at the plasma membrane. {ECO:0000250|UniProtKB:P10824}.
CC -!- PTM: Myristoylation at Gly-2 is required for membrane anchoring before
CC palmitoylation. {ECO:0000250|UniProtKB:P10824}.
CC -!- PTM: Palmitoylation at Cys-3 varies with membrane lipid composition.
CC {ECO:0000250|UniProtKB:P10824}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; X03642; CAA27288.1; -; mRNA.
DR EMBL; BC105419; AAI05420.1; -; mRNA.
DR EMBL; M14207; AAA30561.1; -; mRNA.
DR PIR; A23631; RGBOI1.
DR RefSeq; NP_776749.1; NM_174324.2.
DR RefSeq; XP_015324318.1; XM_015468832.1.
DR PDB; 6K42; EM; 4.10 A; A=1-354.
DR PDB; 6NBF; EM; 3.00 A; A=61-184.
DR PDB; 6NBH; EM; 3.50 A; A=61-184.
DR PDB; 6NBI; EM; 4.00 A; A=61-184.
DR PDB; 7D68; EM; 3.00 A; A=61-184.
DR PDBsum; 6K42; -.
DR PDBsum; 6NBF; -.
DR PDBsum; 6NBH; -.
DR PDBsum; 6NBI; -.
DR PDBsum; 7D68; -.
DR AlphaFoldDB; P63097; -.
DR SMR; P63097; -.
DR BioGRID; 159104; 2.
DR DIP; DIP-41168N; -.
DR IntAct; P63097; 1.
DR MINT; P63097; -.
DR STRING; 9913.ENSBTAP00000003515; -.
DR SwissPalm; P63097; -.
DR PaxDb; P63097; -.
DR PRIDE; P63097; -.
DR Ensembl; ENSBTAT00000003515; ENSBTAP00000003515; ENSBTAG00000002714.
DR GeneID; 281790; -.
DR KEGG; bta:281790; -.
DR CTD; 2770; -.
DR VEuPathDB; HostDB:ENSBTAG00000002714; -.
DR VGNC; VGNC:29449; GNAI1.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000153567; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P63097; -.
DR OMA; LWVDRGV; -.
DR OrthoDB; 754573at2759; -.
DR TreeFam; TF300673; -.
DR Reactome; R-BTA-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-BTA-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000002714; Expressed in omental fat pad and 105 other tissues.
DR GO; GO:0099738; C:cell cortex region; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISS:UniProtKB.
DR GO; GO:0031821; F:G protein-coupled serotonin receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; ISS:UniProtKB.
DR GO; GO:0043949; P:regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; 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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell membrane; Cytoplasm;
KW Cytoskeleton; GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Mitosis; Myristate; Nucleotide-binding; Nucleus; Palmitate;
KW Reference proteome; Transducer; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63096"
FT CHAIN 2..354
FT /note="Guanine nucleotide-binding protein G(i) subunit
FT alpha-1"
FT /id="PRO_0000203669"
FT DOMAIN 32..354
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 35..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 173..181
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 196..205
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 265..272
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 324..329
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 43..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P10824"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P10824"
FT BINDING 150..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P10824"
FT BINDING 175..178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P10824"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P10824"
FT BINDING 200..204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P10824"
FT BINDING 269..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P10824"
FT BINDING 326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P10824"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P63096"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P10824"
FT CONFLICT 113
FT /note="A -> S (in Ref. 3; AAA30561)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="K -> N (in Ref. 3; AAA30561)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="D -> E (in Ref. 3; AAA30561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40361 MW; 9F88311B46E62DE3 CRC64;
MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEAG
YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDSAR ADDARQLFVL AGAAEEGFMT
AELAGVIKRL WKDSGVQACF NRSREYQLND SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK
TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM
NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA
AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF
