LipidDB ID

LipidDB-9606-00480

Entry Name

UniProt Accession

P63096; A8KA88; B4E2V1; C9J3A4; P04898; P11015; P31871; Q5U074; Q8TAN5; Q9UGA4;

Theoretical PI

5.69

Molecular Weight

40361.08

Genbank Protein ID

AAM12619.1; AAC09361.1; CAB43212.2; AAV38580.1; BAF85642.1; BAG65263.1; EAW77011.1; AAH26326.1; AAA35893.1; AAA35893.1; AAA35893.1; AAA52581.1;

Genbank Nucleotide ID

AF493905; AF055013; AL049933; BT019775; AK292953; AK304442; AC004159; AC080066; CH471091; BC026326; M20596; M20594; M20595; M17219;

Protein Name

Guanine nucleotide-binding protein G(i) subunit alpha-1

Protein Synonyms/Alias

Adenylate cyclase-inhibiting G alpha protein;

Gene Name

GNAI1

Gene Synonyms/Alias

Created Date

13-AUG-1987

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Degtyarev MY, Spiegel AM, Jones TL. Palmitoylation of a G protein alpha isubunit requires membrane localization not myristoylation. J Biol Chem. 1994 Dec 9;269(49):30898-903.[PMID:7983022]
[2] Suzuki T, Moriya K, Nagatoshi K, Ota Y, Ezure T, Ando E, Tsunasawa S, UtsumiT. Strategy for comprehensive identification of human N-myristoylated proteinsusing an insect cell-free protein synthesis system. Proteomics. 2010May;10(9):1780-93. doi: 10.1002/pmic.200900783.[PMID:20213681]

Functional Description

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.

Sequence Annotation

Nucleotide-binding: 40 47 GTP.
Nucleotide-binding: 175 181 GTP.
Nucleotide-binding: 200 204 GTP.
Nucleotide-binding: 269 272 GTP.
Metal binding site: 47 47 Magnesium.
Metal binding site: 181 181 Magnesium.
Binding site: 326 326 GTP; via amide nitrogen.
Modified residue: 178 178 ADP-ribosylarginine; by cholera toxin.
Modified residue: 351 351 ADP-ribosylcysteine; by pertussis toxin.

Protein Length

354 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005813; C:centrosome; IDA:UniProtKB
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome
GO:0005765; C:lysosomal membrane; IDA:UniProtKB
GO:0030496; C:midbody; IDA:UniProtKB
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome
GO:0031821; F:G-protein coupled serotonin receptor binding; IBA:RefGenome
GO:0005525; F:GTP binding; ISS:BHF-UCL
GO:0003924; F:GTPase activity; IBA:RefGenome
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004871; F:signal transducer activity; IBA:RefGenome
GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; TAS:Reactome
GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:RefGenome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0007049; P:cell cycle; IEA:UniProtKB-KW
GO:0051301; P:cell division; IMP:UniProtKB
GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:BHF-UCL
GO:0030168; P:platelet activation; TAS:Reactome
GO:0043434; P:response to peptide hormone; ISS:BHF-UCL
GO:0007268; P:synaptic transmission; TAS:Reactome

Interpro

InterPro; IPR001408; Gprotein_alpha_I
InterPro; IPR001019; Gprotein_alpha_su
InterPro; IPR011025; GproteinA_insert
InterPro; IPR027417; P-loop_NTPase

Pfam

Pfam; PF00503; G-alpha;

SMART

SMART; SM00275; G_alpha;

PROSITE

PRINTS

PRINTS; PR00318; GPROTEINA;
PRINTS; PR00441; GPROTEINAI;