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Protein

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

Gene

Gnai2

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) 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471MagnesiumBy similarity
Metal bindingi182 – 1821MagnesiumBy similarity
Binding sitei327 – 3271GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 478GTPBy similarity
Nucleotide bindingi176 – 1827GTPBy similarity
Nucleotide bindingi201 – 2055GTPBy similarity
Nucleotide bindingi270 – 2734GTPBy similarity

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: GO_Central
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB
  • cell proliferation Source: Ensembl
  • gamma-aminobutyric acid signaling pathway Source: RGD
  • G-protein coupled acetylcholine receptor signaling pathway Source: Ensembl
  • 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
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.
SABIO-RKP04897.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi620243. Gnai2.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
  • Membrane By similarity; Lipid-anchor By similarity

  • Note: Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody (By similarity).By similarity

GO - Cellular componenti

  • cell body Source: Ensembl
  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: RGD
  • dendrite Source: Ensembl
  • extracellular exosome Source: Ensembl
  • heterotrimeric G-protein complex Source: GO_Central
  • membrane Source: RGD
  • membrane raft Source: RGD
  • midbody Source: UniProtKB
  • nucleoplasm Source: Ensembl
  • nucleus Source: RGD
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi82 – 821M → 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 Publication
Mutagenesisi85 – 851V → 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 Publication
Mutagenesisi86 – 861K → 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 Publication
Mutagenesisi90 – 901N → 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 Publication
Mutagenesisi92 – 921Q → 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 Publication
Mutagenesisi96 – 961A → 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 Publication
Mutagenesisi98 – 981P → 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 Publication
Mutagenesisi99 – 991Q → 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 Publication
Mutagenesisi111 – 1111S → 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 Publication
Mutagenesisi112 – 1121C → 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 Publication
Mutagenesisi117 – 1171Missing : 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.
Mutagenesisi121 – 1211P → 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 Publication
Mutagenesisi122 – 1221E → 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 355354Guanine nucleotide-binding protein G(i) subunit alpha-2PRO_0000203682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Lipidationi3 – 31S-palmitoyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate

Proteomic databases

PaxDbiP04897.
PRIDEiP04897.

PTM databases

iPTMnetiP04897.
PhosphoSiteiP04897.
SwissPalmiP04897.

Expressioni

Gene expression databases

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 interactions.
DIPiDIP-607N.
IntActiP04897. 1 interaction.
MINTiMINT-1795638.
STRINGi10116.ENSRNOP00000022550.

Structurei

3D structure databases

ProteinModelPortaliP04897.
SMRiP04897. Positions 5-354.
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.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP04897.
KOiK04630.
OMAiYSGANKY.
OrthoDBiEOG72C50B.
PhylomeDBiP04897.
TreeFamiTF300673.

Family and domain databases

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti166 – 1672SD → PN in tryptic peptides.

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

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP04897.
SMRiP04897. Positions 5-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249564. 2 interactions.
DIPiDIP-607N.
IntActiP04897. 1 interaction.
MINTiMINT-1795638.
STRINGi10116.ENSRNOP00000022550.

PTM databases

iPTMnetiP04897.
PhosphoSiteiP04897.
SwissPalmiP04897.

Proteomic databases

PaxDbiP04897.
PRIDEiP04897.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2771.
RGDi620243. Gnai2.

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP04897.
KOiK04630.
OMAiYSGANKY.
OrthoDBiEOG72C50B.
PhylomeDBiP04897.
TreeFamiTF300673.

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.
SABIO-RKP04897.

Miscellaneous databases

PROiP04897.

Gene expression databases

ExpressionAtlasiP04897. baseline and differential.
GenevisibleiP04897. RN.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence determination of cDNAs for alpha subunits of the guanine nucleotide-binding proteins Gs, Gi, and Go from rat brain."
    Itoh H., Kozasa T., Nagata S., Nakamura S., Katada T., Ui M., Iwai S., Ohtsuka E., Kawasaki H., Suzuki K., Kaziro Y.
    Proc. Natl. Acad. Sci. U.S.A. 83:3776-3780(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning of five GTP-binding protein cDNA species from rat olfactory neuroepithelium."
    Jones D.T., Reed R.R.
    J. Biol. Chem. 262:14241-14249(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. "Purification and characterization of Go alpha and three types of Gi alpha after expression in Escherichia coli."
    Linder M.E., Ewald D.A., Miller R.J., Gilman A.G.
    J. Biol. Chem. 265:8243-8251(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 12-126.
  5. "Activator of G protein signaling 3 is a guanine dissociation inhibitor for Galpha i subunits."
    de Vries L., Fischer T., Tronchere H., Brothers G.M., Strockbine B., Siderovski D.P., Farquhar M.G.
    Proc. Natl. Acad. Sci. U.S.A. 97:14364-14369(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPSM1.
  6. "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor activity."
    Kimple R.J., De Vries L., Tronchere H., Behe C.I., Morris R.A., Gist Farquhar M., Siderovski D.P.
    J. Biol. Chem. 276:29275-29281(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RGS12 AND RGS14.
  7. "Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR domain of RGS14 influence its dynamic subcellular localization."
    Shu F.J., Ramineni S., Amyot W., Hepler J.R.
    Cell. Signal. 19:163-176(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "The RGS14 GoLoco domain discriminates among Galphai isoforms."
    Mittal V., Linder M.E.
    J. Biol. Chem. 279:46772-46778(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF MET-82; VAL-85; LYS-86; ASN-90; GLN-92; ALA-96; PRO-98; GLN-99; SER-111; CYS-112; PRO-121 AND GLU-122.
  9. "Localization of Gi alpha proteins in the centrosomes and at the midbody: implication for their role in cell division."
    Cho H., Kehrl J.H.
    J. Cell Biol. 178:245-255(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiGNAI2_RAT
AccessioniPrimary (citable) accession number: P04897
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 152 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.