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Protein

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

Gene

Gnai1

Organism
Rattus norvegicus (Rat)
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 (PubMed:19703466, PubMed:24596087, PubMed:25037222). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:21158412). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:21158412). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (PubMed:19703466). 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 (PubMed:16870394).Curated5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi47MagnesiumCombined sources2 Publications1
Metal bindingi181MagnesiumCombined sources3 Publications1
Binding sitei326GTP; via amide nitrogenCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi43 – 48GTPCombined sources6
Nucleotide bindingi150 – 151GTPCombined sources2
Nucleotide bindingi175 – 178GTPCombined sources4
Nucleotide bindingi200 – 204GTPCombined sources5
Nucleotide bindingi269 – 272GTPCombined sources4

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • G-protein beta/gamma-subunit complex binding Source: GO_Central
  • G-protein coupled receptor binding Source: UniProtKB
  • G-protein coupled serotonin receptor binding Source: RGD
  • GTPase activating protein binding Source: RGD
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • signal transducer activity Source: GO_Central

GO - Biological processi

  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: GO_Central
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB
  • cellular response to forskolin Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • negative regulation of synaptic transmission Source: RGD
  • regulation of cAMP-mediated signaling Source: UniProtKB
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-RNO-112043. PLC beta mediated events.
R-RNO-170670. Adenylate cyclase inhibitory pathway.
R-RNO-202040. G-protein activation.
R-RNO-392170. ADP signalling through P2Y purinoceptor 12.
R-RNO-400042. Adrenaline,noradrenaline inhibits insulin secretion.
R-RNO-418594. G alpha (i) signalling events.
R-RNO-418597. G alpha (z) signalling events.
R-RNO-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
SABIO-RKP10824.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi2713. Gnai1.

Subcellular locationi

  • Nucleus
  • Cytoplasm 1 Publication
  • Cell membrane 2 Publications; Peripheral membrane protein 2 Publications; Cytoplasmic side Curated
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
  • 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 (PubMed:21158412).By similarity1 Publication

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • heterotrimeric G-protein complex Source: RGD
  • lysosomal membrane Source: Ensembl
  • membrane Source: RGD
  • membrane raft Source: RGD
  • midbody Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi43E → A: Mildly impairs receptor binding; mildly decreases basal and receptor-stimulated GDP exchange. 1 Publication1
Mutagenesisi149N → I: Inhibits interaction with RGS14. Does not inhibit interaction with RIC8A. 1 Publication1
Mutagenesisi189F → Y: Increases basal GDP exchange rate; no effect on receptor-stimulated GDP exchange. 1 Publication1
Mutagenesisi191F → Y: No effect on basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange. 1 Publication1
Mutagenesisi204Q → L: Expected to have lost GTPase activity; inhibits the forskolin-mediated increase of cellular cAMP levels. Does not inhibit interaction with RGS14 at centrosomes. 2 Publications1
Mutagenesisi329T → A: Increases basal GDP exchange rate and inhibits the forskolin-mediated increase of cellular cAMP levels. 1 Publication1
Mutagenesisi332V → A: Increases basal GDP exchange rate. 1 Publication1
Mutagenesisi336F → A or C: Increases basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange. 1 Publication1
Mutagenesisi336F → Y: Strongly increases basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange. 1 Publication1
Mutagenesisi345K → L: Mildly impairs receptor binding; mildly decreases basal and receptor-stimulated GDP exchange. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002036732 – 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

PRIDEiP10824.

2D gel databases

World-2DPAGE0004:P10824.

PTM databases

iPTMnetiP10824.
PhosphoSitePlusiP10824.
SwissPalmiP10824.

Interactioni

Subunit structurei

Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (PubMed:8521505, PubMed:24596087, PubMed:25037222). Identified in complex with the beta subunit GNB1 and the gamma subunit GNG1 (PubMed:24596087). Identified in complex with the beta subunit GNB1 and the gamma subunit GNG2 (PubMed:8521505). GTP binding causes dissociation of the heterotrimer, liberating the individual subunits so that they can interact with downstream effector proteins. Interacts (GDP-bound form) with GPSM1; this inhibits guanine nucleotide exchange and GTP binding (PubMed:11121039). Interacts (GDP-bound form) with GPSM2 (via GoLoco domains); this inhibits guanine nucleotide exchange (By similarity). Interacts with RGS10; this strongly enhances GTP hydrolysis. Interacts with RGS1 and RGS16 (By similarity). Interacts with RGS4 (PubMed:9108480). Interacts with RGS12 (PubMed:11387333). Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains) (PubMed:11387333, PubMed:16870394, PubMed:17635935, PubMed:21158412). Interacts with RGS3, RGS6, RGS7, RGS8, RGS17, RGS18 and RGS20 (in vitro) (By similarity). Interacts (GDP-bound form) with RIC8A (via C-terminus) (PubMed:21158412).By similarity8 Publications

GO - Molecular functioni

  • G-protein beta/gamma-subunit complex binding Source: GO_Central
  • G-protein coupled receptor binding Source: UniProtKB
  • G-protein coupled serotonin receptor binding Source: RGD
  • GTPase activating protein binding Source: RGD

Protein-protein interaction databases

BioGridi247715. 1 interactor.
DIPiDIP-6073N.
IntActiP10824. 2 interactors.
MINTiMINT-1795581.

Structurei

Secondary structure

1354
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 31Combined sources24
Beta strandi33 – 39Combined sources7
Helixi46 – 57Combined sources12
Helixi63 – 68Combined sources6
Helixi70 – 91Combined sources22
Helixi100 – 110Combined sources11
Helixi111 – 116Combined sources6
Helixi121 – 132Combined sources12
Helixi134 – 140Combined sources7
Helixi141 – 145Combined sources5
Helixi152 – 156Combined sources5
Helixi159 – 162Combined sources4
Beta strandi164 – 166Combined sources3
Helixi171 – 175Combined sources5
Beta strandi183 – 191Combined sources9
Beta strandi194 – 201Combined sources8
Helixi205 – 214Combined sources10
Beta strandi219 – 226Combined sources8
Helixi227 – 231Combined sources5
Beta strandi237 – 241Combined sources5
Helixi242 – 254Combined sources13
Helixi257 – 259Combined sources3
Beta strandi262 – 269Combined sources8
Helixi271 – 278Combined sources8
Helixi283 – 285Combined sources3
Helixi296 – 308Combined sources13
Turni314 – 316Combined sources3
Beta strandi319 – 323Combined sources5
Helixi329 – 346Combined sources18
Helixi348 – 350Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AGRX-ray2.80A/D2-354[»]
1AS0X-ray2.00A2-354[»]
1AS2X-ray2.80A2-354[»]
1AS3X-ray2.40A2-354[»]
1BH2X-ray2.10A32-346[»]
1BOFX-ray2.20A2-354[»]
1CIPX-ray1.50A2-354[»]
1GDDX-ray2.20A2-354[»]
1GFIX-ray2.20A2-354[»]
1GG2X-ray2.40A2-354[»]
1GIAX-ray2.00A2-354[»]
1GILX-ray2.30A2-354[»]
1GITX-ray2.60A2-354[»]
1GP2X-ray2.30A2-354[»]
1SHZX-ray2.85A/D22-48[»]
A/D185-353[»]
1SVKX-ray2.00A2-354[»]
1SVSX-ray1.50A2-354[»]
2BCJX-ray3.06Q1-28[»]
2ZJYX-ray2.80A1-354[»]
2ZJZX-ray2.60A/B1-354[»]
3AH8X-ray2.90A2-28[»]
3D7MX-ray2.90A1-354[»]
3FFAX-ray2.30A1-348[»]
3FFBX-ray2.57A1-354[»]
3V00X-ray2.90A/B/C220-298[»]
4N0DX-ray1.55A1-354[»]
4N0EX-ray2.10A1-354[»]
4PAMX-ray2.10A1-354[»]
4PANX-ray2.40A1-354[»]
4PAOX-ray2.00A1-354[»]
4PAQX-ray2.00A1-354[»]
5KDLX-ray2.67A/B1-354[»]
5KDOX-ray1.90A1-354[»]
DisProtiDP00035.
ProteinModelPortaliP10824.
SMRiP10824.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10824.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP10824.
KOiK04630.
OMAiSARAXYL.
OrthoDBiEOG091G0VUT.
PhylomeDBiP10824.

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.

P10824-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEAG YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDAAR
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):40,345
Last modified:January 23, 2007 - v3
Checksum:i99E9D11B485C2DE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17527 mRNA. Translation: AAA40825.1.
DQ120469 mRNA. Translation: AAZ23808.1.
DQ120470 mRNA. Translation: AAZ23809.1.
PIRiA35377.
C27423. RGRTI1.
RefSeqiNP_037277.1. NM_013145.1.
UniGeneiRn.11391.

Genome annotation databases

EnsembliENSRNOT00000091004; ENSRNOP00000074036; ENSRNOG00000057096.
GeneIDi25686.
KEGGirno:25686.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17527 mRNA. Translation: AAA40825.1.
DQ120469 mRNA. Translation: AAZ23808.1.
DQ120470 mRNA. Translation: AAZ23809.1.
PIRiA35377.
C27423. RGRTI1.
RefSeqiNP_037277.1. NM_013145.1.
UniGeneiRn.11391.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AGRX-ray2.80A/D2-354[»]
1AS0X-ray2.00A2-354[»]
1AS2X-ray2.80A2-354[»]
1AS3X-ray2.40A2-354[»]
1BH2X-ray2.10A32-346[»]
1BOFX-ray2.20A2-354[»]
1CIPX-ray1.50A2-354[»]
1GDDX-ray2.20A2-354[»]
1GFIX-ray2.20A2-354[»]
1GG2X-ray2.40A2-354[»]
1GIAX-ray2.00A2-354[»]
1GILX-ray2.30A2-354[»]
1GITX-ray2.60A2-354[»]
1GP2X-ray2.30A2-354[»]
1SHZX-ray2.85A/D22-48[»]
A/D185-353[»]
1SVKX-ray2.00A2-354[»]
1SVSX-ray1.50A2-354[»]
2BCJX-ray3.06Q1-28[»]
2ZJYX-ray2.80A1-354[»]
2ZJZX-ray2.60A/B1-354[»]
3AH8X-ray2.90A2-28[»]
3D7MX-ray2.90A1-354[»]
3FFAX-ray2.30A1-348[»]
3FFBX-ray2.57A1-354[»]
3V00X-ray2.90A/B/C220-298[»]
4N0DX-ray1.55A1-354[»]
4N0EX-ray2.10A1-354[»]
4PAMX-ray2.10A1-354[»]
4PANX-ray2.40A1-354[»]
4PAOX-ray2.00A1-354[»]
4PAQX-ray2.00A1-354[»]
5KDLX-ray2.67A/B1-354[»]
5KDOX-ray1.90A1-354[»]
DisProtiDP00035.
ProteinModelPortaliP10824.
SMRiP10824.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247715. 1 interactor.
DIPiDIP-6073N.
IntActiP10824. 2 interactors.
MINTiMINT-1795581.

PTM databases

iPTMnetiP10824.
PhosphoSitePlusiP10824.
SwissPalmiP10824.

2D gel databases

World-2DPAGE0004:P10824.

Proteomic databases

PRIDEiP10824.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000091004; ENSRNOP00000074036; ENSRNOG00000057096.
GeneIDi25686.
KEGGirno:25686.

Organism-specific databases

CTDi2770.
RGDi2713. Gnai1.

Phylogenomic databases

GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP10824.
KOiK04630.
OMAiSARAXYL.
OrthoDBiEOG091G0VUT.
PhylomeDBiP10824.

Enzyme and pathway databases

ReactomeiR-RNO-112043. PLC beta mediated events.
R-RNO-170670. Adenylate cyclase inhibitory pathway.
R-RNO-202040. G-protein activation.
R-RNO-392170. ADP signalling through P2Y purinoceptor 12.
R-RNO-400042. Adrenaline,noradrenaline inhibits insulin secretion.
R-RNO-418594. G alpha (i) signalling events.
R-RNO-418597. G alpha (z) signalling events.
R-RNO-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
SABIO-RKP10824.

Miscellaneous databases

EvolutionaryTraceiP10824.
PROiP10824.

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_RAT
AccessioniPrimary (citable) accession number: P10824
Secondary accession number(s): Q45QN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 170 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.