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Protein

Guanine nucleotide-binding protein G(i) subunit alpha-2

Gene

Gnai2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. May play a role in cell division.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi47MagnesiumBy similarity1
Metal bindingi182MagnesiumBy similarity1
Binding sitei327GTP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi40 – 47GTPBy similarity8
Nucleotide bindingi176 – 182GTPBy similarity7
Nucleotide bindingi201 – 205GTPBy similarity5
Nucleotide bindingi270 – 273GTPBy similarity4

GO - Molecular functioni

GO - Biological processi

  • activation of MAPKK activity Source: RGD
  • adenosine receptor signaling pathway Source: RGD
  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: RGD
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB
  • cell proliferation Source: RGD
  • gamma-aminobutyric acid signaling pathway Source: RGD
  • G-protein coupled acetylcholine receptor signaling pathway Source: RGD
  • G-protein coupled receptor signaling pathway Source: RGD
  • intracellular signal transduction Source: RGD
  • negative regulation of synaptic transmission Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • regulation of calcium ion transport Source: RGD

Keywordsi

Molecular functionTransducer
Biological processCell cycle, Cell division
LigandGTP-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-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
SABIO-RKiP04897.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(i) subunit alpha-2
Alternative name(s):
Adenylate cyclase-inhibiting G alpha protein
Gene namesi
Name:Gnai2
Synonyms:Gnai-2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi620243. Gnai2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi82M → I: Increases sensitivity to RGS14 GTPase activity; when associated with I-85; R-86; R-90; K-92; G-96; A-98; A-99; A-111; G-112; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with I-85 and A-111. 1 Publication1
Mutagenesisi85V → I: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; R-86; R-90; K-92; G-96; A-98; A-99; A-111; G-112; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with I-82 and A-111. 1 Publication1
Mutagenesisi86K → R: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-90; K-92; G-96; A-98; A-99; A-111; G-112; T-121 and A-122. 1 Publication1
Mutagenesisi90N → R: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; K-92; G-96; A-98; A-99; A-111; G-112; T-121 and A-122. 1 Publication1
Mutagenesisi92Q → K: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; G-96; A-98; A-99; A-111; G-112; T-121 and A-122. 1 Publication1
Mutagenesisi96A → G: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; A-98; A-99; A-111; G-112; T-121 and A-122. 1 Publication1
Mutagenesisi98P → A: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-99; A-111; G-112; T-121 and A-122. 1 Publication1
Mutagenesisi99Q → A: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-111; G-112; T-121 and A-122. 1 Publication1
Mutagenesisi111S → A: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-99; G-112; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with G-112; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with I-82 and A-85. 1 Publication1
Mutagenesisi112C → G: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-99; A-111; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with G-111; T-121 and A-122. 1 Publication1
Mutagenesisi117Missing : Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-99; A-111; G-112; T-121 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with G-111; G-112; T-121 and A-122. 1
Mutagenesisi121P → T: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-99; A-111; G-112 and A-122. Does not increase sensitivity to RGS14 GTPase activity; when associated with G-111; G-112 and A-122. 1 Publication1
Mutagenesisi122E → A: Increases sensitivity to RGS14 GTPase activity; when associated with I-82; I-85; R-86; R-90; K-92; G-96; A-98; A-99; A-111; G-112 and T-121. Does not increase sensitivity to RGS14 GTPase activity; when associated with G-111; G-112 and T-121. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002036822 – 355Guanine nucleotide-binding protein G(i) subunit alpha-2Add BLAST354

Amino acid modifications

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

Keywords - PTMi

Lipoprotein, Myristate, Palmitate

Proteomic databases

PaxDbiP04897.
PRIDEiP04897.

PTM databases

iPTMnetiP04897.
PhosphoSitePlusiP04897.
SwissPalmiP04897.

Expressioni

Gene expression databases

BgeeiENSRNOG00000016592.
ExpressionAtlasiP04897. baseline and differential.
GenevisibleiP04897. RN.

Interactioni

Subunit structurei

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with UNC5B (By similarity). Interacts with GPSM1. Interacts with RGS12 and RGS14.By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi249564. 2 interactors.
CORUMiP04897.
DIPiDIP-607N.
IntActiP04897. 2 interactors.
STRINGi10116.ENSRNOP00000022550.

Structurei

3D structure databases

ProteinModelPortaliP04897.
SMRiP04897.
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.
InParanoidiP04897.
KOiK04630.
OMAiEQGIMPD.
OrthoDBiEOG091G0VUT.
PhylomeDBiP04897.
TreeFamiTF300673.

Family and domain databases

CDDicd00066. G-alpha. 1 hit.
Gene3Di1.10.400.10. 1 hit.
InterProiView protein in InterPro
IPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiView protein in Pfam
PF00503. G-alpha. 1 hit.
PRINTSiPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTiView protein in SMART
SM00275. G_alpha. 1 hit.
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P04897-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEDG YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPQR
110 120 130 140 150
ADDARQLFAL SCAAEEQGML PEDLSGVIRR LWADHGVQAC FGRSREYQLN
160 170 180 190 200
DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV KTTGIVETHF TFKDLHFKMF
210 220 230 240 250
DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE MNRMHESMKL
260 270 280 290 300
FDSICNNKWF TDTSIILFLN KKDLFEEKIT QSPLTICFPE YTGANKYDEA
310 320 330 340 350
ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK

DCGLF
Length:355
Mass (Da):40,499
Last modified:January 23, 2007 - v3
Checksum:i9360ABAC6BDC493E
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti166 – 167SD → PN in tryptic peptides. 2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12672 mRNA. Translation: AAA41260.1.
M17528 mRNA. Translation: AAA40824.1.
BC078806 mRNA. Translation: AAH78806.1.
PIRiD27423. RGRTI2.
RefSeqiNP_112297.1. NM_031035.3.
XP_006243920.1. XM_006243858.1.
UniGeneiRn.3036.

Genome annotation databases

EnsembliENSRNOT00000022550; ENSRNOP00000022550; ENSRNOG00000016592.
GeneIDi81664.
KEGGirno:81664.
UCSCiRGD:620243. rat.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiGNAI2_RAT
AccessioniPrimary (citable) accession number: P04897
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 164 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome