GNAI2_CANLF
ID GNAI2_CANLF Reviewed; 355 AA.
AC P38400;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-2;
DE AltName: Full=Adenylate cyclase-inhibiting G alpha protein;
GN Name=GNAI2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2477170; DOI=10.1161/01.res.65.4.1136;
RA Holmer S.R., Stevens S., Homcy C.J.;
RT "Tissue- and species-specific expression of inhibitory guanine nucleotide-
RT binding proteins. Cloning of a full-length complementary DNA from canine
RT heart.";
RL Circ. Res. 65:1136-1140(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Boudreaux M.K.;
RT "Guanine nucleotide-binding regulatory protein, alpha inhibitory subunit
RT mRNA.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. The G(i) proteins are involved in hormonal regulation of
CC adenylate cyclase: they inhibit the cyclase in response to beta-
CC adrenergic stimuli. May play a role in cell division (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site. In this
CC context, interacts with GNB2 (By similarity). Interacts with UNC5B (By
CC similarity). Interacts with GPSM1 (By similarity). Interacts with RGS12
CC and RGS14 (By similarity). Interacts (inactive GDP-bound form) with
CC NUCB1 (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) (By similarity). Interacts (inactive GDP-bound form)
CC with CCDC8A/GIV (via GBA motif) (By similarity). Interacts with CXCR1
CC and CXCR2 (By similarity). {ECO:0000250|UniProtKB:P04897,
CC ECO:0000250|UniProtKB:P04899}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P04899}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P04899}. Note=Localizes in the centrosomes of
CC interphase and mitotic cells. Detected at the cleavage furrow and/or
CC the midbody (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; AY563036; AAS67003.1; -; mRNA.
DR PIR; A61031; A61031.
DR RefSeq; NP_001003364.1; NM_001003364.1.
DR AlphaFoldDB; P38400; -.
DR SMR; P38400; -.
DR STRING; 9612.ENSCAFP00000033576; -.
DR PaxDb; P38400; -.
DR PRIDE; P38400; -.
DR Ensembl; ENSCAFT00030022602; ENSCAFP00030019719; ENSCAFG00030012013.
DR Ensembl; ENSCAFT00040029611; ENSCAFP00040025722; ENSCAFG00040016016.
DR Ensembl; ENSCAFT00845039975; ENSCAFP00845031303; ENSCAFG00845022609.
DR GeneID; 442957; -.
DR KEGG; cfa:442957; -.
DR CTD; 2771; -.
DR VEuPathDB; HostDB:ENSCAFG00845022609; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000155125; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P38400; -.
DR OMA; XYLNDER; -.
DR OrthoDB; 754573at2759; -.
DR TreeFam; TF300673; -.
DR Reactome; R-CFA-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-CFA-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-CFA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-CFA-418594; G alpha (i) signalling events.
DR Reactome; R-CFA-9009391; Extra-nuclear estrogen signaling.
DR Proteomes; UP000002254; Chromosome 20.
DR Bgee; ENSCAFG00000010740; Expressed in granulocyte and 46 other tissues.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
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; Myristate;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P04899"
FT CHAIN 2..355
FT /note="Guanine nucleotide-binding protein G(i) subunit
FT alpha-2"
FT /id="PRO_0000203677"
FT DOMAIN 32..355
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 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 325..330
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P04899"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 355 AA; 40546 MW; 43ABC59C505208C0 CRC64;
MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG
YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFDDPSR ADDARQLFAL SCTAEEQGVL
PEDLSCVIRR LWADNGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV
KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE
MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT HSPLTICFPE YTGANKYEEA
ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF
