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Protein

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

Gene

Gnai1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (By similarity). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (By similarity). 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. Required for normal cytokinesis during mitosis (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi47MagnesiumBy similarity1
Metal bindingi181MagnesiumBy similarity1
Binding sitei326GTP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi43 – 48GTPBy similarity6
Nucleotide bindingi150 – 151GTPBy similarity2
Nucleotide bindingi175 – 178GTPBy similarity4
Nucleotide bindingi200 – 204GTPBy similarity5
Nucleotide bindingi269 – 272GTPBy similarity4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-112043. PLC beta mediated events.
R-MMU-170670. Adenylate cyclase inhibitory pathway.
R-MMU-202040. G-protein activation.
R-MMU-392170. ADP signalling through P2Y purinoceptor 12.
R-MMU-400042. Adrenaline,noradrenaline inhibits insulin secretion.
R-MMU-418594. G alpha (i) signalling events.
R-MMU-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(i) subunit alpha-1
Alternative name(s):
Adenylate cyclase-inhibiting G alpha protein
Gene namesi
Name:Gnai1
Synonyms:Gnai-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:95771. Gnai1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  • Membrane By similarity; Lipid-anchor By similarity

  • Note: Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody (By similarity). Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00004084772 – 354Guanine nucleotide-binding protein G(i) subunit alpha-1Add BLAST353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Lipidationi3S-palmitoyl cysteineBy similarity1

Keywords - PTMi

Lipoprotein, Myristate, Palmitate

Proteomic databases

MaxQBiB2RSH2.
PaxDbiB2RSH2.
PeptideAtlasiB2RSH2.
PRIDEiB2RSH2.

PTM databases

iPTMnetiB2RSH2.
PhosphoSitePlusiB2RSH2.
SwissPalmiB2RSH2.

Expressioni

Gene expression databases

BgeeiENSMUSG00000057614.
GenevisibleiB2RSH2. MM.

Interactioni

Subunit structurei

Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Identified in complex with the beta subunit GNB1 and the gamma subunit GNG1. Identified in complex with the beta subunit GNB1 and the gamma subunit GNG2. GTP binding causes dissociation of the heterotrimer, liberating the individual subunits so that they can interact with downstream effector proteins (By similarity). Interacts (GDP-bound form) with GPSM1; this inhibits guanine nucleotide exchange and GTP binding (By similarity). Interacts (GDP-bound form) with GPSM2 (via GoLoco domains); this inhibits guanine nucleotide exchange. Interacts with RGS10; this strongly enhances GTP hydrolysis. Interacts with RGS1 and RGS16; this strongly enhances GTPase activity. Interacts with RGS4. Interacts with RGS12. Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains). Interacts with RGS3, RGS6, RGS7, RGS8, RGS17, RGS18 and RGS20 (in vitro) (By similarity). Interacts (GDP-bound form) with RIC8A (via C-terminus) (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199966. 1 interactor.
IntActiB2RSH2. 1 interactor.
STRINGi10090.ENSMUSP00000074259.

Structurei

3D structure databases

ProteinModelPortaliB2RSH2.
SMRiB2RSH2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-alpha family. G(i/o/t/z) subfamily.Curated

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiB2RSH2.
KOiK04630.
OMAiSARAXYL.
OrthoDBiEOG091G0VUT.
PhylomeDBiB2RSH2.
TreeFamiTF300673.

Family and domain databases

CDDicd00066. G-alpha. 1 hit.
Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B2RSH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEAG YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDSAR
110 120 130 140 150
ADDARQLFVL AGAAEEGFMT AELAGVIKRL WKDSGVQACF NRSREYQLND
160 170 180 190 200
SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK TTGIVETHFT FKDLHFKMFD
210 220 230 240 250
VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM NRMHESMKLF
260 270 280 290 300
DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA
310 320 330 340 350
AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD

CGLF
Length:354
Mass (Da):40,361
Last modified:July 1, 2008 - v1
Checksum:i9F88311B46E62DE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC138862 mRNA. Translation: AAI38863.1.
BC138865 mRNA. Translation: AAI38866.1.
CCDSiCCDS39018.1.
RefSeqiNP_034435.1. NM_010305.1.
UniGeneiMm.254629.

Genome annotation databases

EnsembliENSMUST00000074694; ENSMUSP00000074259; ENSMUSG00000057614.
GeneIDi14677.
KEGGimmu:14677.
UCSCiuc008wns.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC138862 mRNA. Translation: AAI38863.1.
BC138865 mRNA. Translation: AAI38866.1.
CCDSiCCDS39018.1.
RefSeqiNP_034435.1. NM_010305.1.
UniGeneiMm.254629.

3D structure databases

ProteinModelPortaliB2RSH2.
SMRiB2RSH2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199966. 1 interactor.
IntActiB2RSH2. 1 interactor.
STRINGi10090.ENSMUSP00000074259.

PTM databases

iPTMnetiB2RSH2.
PhosphoSitePlusiB2RSH2.
SwissPalmiB2RSH2.

Proteomic databases

MaxQBiB2RSH2.
PaxDbiB2RSH2.
PeptideAtlasiB2RSH2.
PRIDEiB2RSH2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000074694; ENSMUSP00000074259; ENSMUSG00000057614.
GeneIDi14677.
KEGGimmu:14677.
UCSCiuc008wns.1. mouse.

Organism-specific databases

CTDi2770.
MGIiMGI:95771. Gnai1.

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiB2RSH2.
KOiK04630.
OMAiSARAXYL.
OrthoDBiEOG091G0VUT.
PhylomeDBiB2RSH2.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiR-MMU-112043. PLC beta mediated events.
R-MMU-170670. Adenylate cyclase inhibitory pathway.
R-MMU-202040. G-protein activation.
R-MMU-392170. ADP signalling through P2Y purinoceptor 12.
R-MMU-400042. Adrenaline,noradrenaline inhibits insulin secretion.
R-MMU-418594. G alpha (i) signalling events.
R-MMU-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

PROiB2RSH2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000057614.
GenevisibleiB2RSH2. MM.

Family and domain databases

CDDicd00066. G-alpha. 1 hit.
Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiGNAI1_MOUSE
AccessioniPrimary (citable) accession number: B2RSH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: July 1, 2008
Last modified: November 30, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.