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P10824 (GNAI1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein G(i) subunit alpha-1
Alternative name(s):
Adenylate cyclase-inhibiting G alpha protein
Gene names
Name:Gnai1
Synonyms:Gnai-1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Subunit structure

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with GPSM1. Interacts with RGS12. Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains); the interaction occurs in the centrosomes. Interacts (GDP-bound form) with RIC8A (via C-terminus). Interacts with DRD2 By similarity. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.9

Subcellular location

Nucleus. Cytoplasm. Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. 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. Ref.5 Ref.6 Ref.7

Sequence similarities

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMLipoprotein
Myristate
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from mutant phenotype PubMed 11923410. Source: RGD

adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of synaptic transmission

Inferred from mutant phenotype PubMed 11923410. Source: RGD

   Cellular_componentcentrosome

Inferred from direct assay Ref.6. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.6. Source: UniProtKB

extrinsic component of cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

heterotrimeric G-protein complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane

Inferred from direct assay PubMed 16741924. Source: RGD

membrane raft

Inferred from direct assay PubMed 17157995. Source: RGD

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.5Ref.6Ref.7. Source: UniProtKB

protein complex

Inferred from direct assay Ref.10. Source: RGD

   Molecular_functionG-protein beta/gamma-subunit complex binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

G-protein coupled serotonin receptor binding

Inferred from physical interaction PubMed 16772521. Source: RGD

GDP binding

Inferred from direct assay Ref.10. Source: RGD

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activating protein binding

Inferred from direct assay Ref.10. Source: RGD

GTPase activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.4Ref.5Ref.6Ref.7. Source: UniProtKB

signal transducer activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 354353Guanine nucleotide-binding protein G(i) subunit alpha-1
PRO_0000203673

Regions

Nucleotide binding40 – 478GTP By similarity
Nucleotide binding43 – 486GTP
Nucleotide binding175 – 1817GTP By similarity
Nucleotide binding175 – 1784GTP
Nucleotide binding200 – 2045GTP By similarity
Nucleotide binding269 – 2724GTP

Sites

Metal binding471Magnesium By similarity
Metal binding1811Magnesium By similarity
Binding site3261GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity

Experimental info

Mutagenesis1491N → I: Inhibits interaction with RGS14. Does not inhibit interaction with RIC8A. Ref.7
Mutagenesis2041Q → L: Does not inhibit interaction with GNAI1 in the centrosomes. Ref.6

Secondary structure

............................................................. 354
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10824 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 99E9D11B485C2DE3

FASTA35440,345
        10         20         30         40         50         60 
MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEAG 

        70         80         90        100        110        120 
YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDAAR ADDARQLFVL AGAAEEGFMT 

       130        140        150        160        170        180 
AELAGVIKRL WKDSGVQACF NRSREYQLND SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK 

       190        200        210        220        230        240 
TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM 

       250        260        270        280        290        300 
NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA 

       310        320        330        340        350 
AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF 

« Hide

References

[1]"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].
[2]"Genetic similarity between spontaneously hypertensive rats and Wistar-Kyoto rats in the coding regions of signal transduction proteins."
Jackson E.K., Zhu C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: SHR and Wistar Kyoto.
[3]"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.
[4]"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.
[5]"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: FUNCTION, INTERACTION WITH RGS14, SUBCELLULAR LOCATION.
[6]"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, INTERACTION WITH RGS14, MUTAGENESIS OF GLN-204.
[7]"Activation of the regulator of G protein signaling 14-Galphai1-GDP signaling complex is regulated by resistance to inhibitors of cholinesterase-8A."
Vellano C.P., Shu F.J., Ramineni S., Yates C.K., Tall G.G., Hepler J.R.
Biochemistry 50:752-762(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RGS14 AND RIC8A, MUTAGENESIS OF ASN-149, SUBCELLULAR LOCATION.
[8]"Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis."
Coleman D.E., Berghuis A.M., Lee E., Linder M.E., Gilman A.G., Sprang S.R.
Science 265:1405-1412(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[9]"The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2."
Wall M.A., Coleman D.E., Lee E., Iniguez-Lluhi J.A., Posner B.A., Gilman A.G., Sprang S.R.
Cell 83:1047-1058(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HETEROTRIMER IN COMPLEX WITH GDP, SUBUNIT.
[10]"Structure of RGS4 bound to AlF4-activated G(i alpha1): stabilization of the transition state for GTP hydrolysis."
Tesmer J.J.G., Berman D.M., Gilman A.G., Sprang S.R.
Cell 89:251-261(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RGS4 AND GDP.
[11]"Crystal structures of the G protein Gi alpha 1 complexed with GDP and Mg2+: a crystallographic titration experiment."
Coleman D.E., Sprang S.R.
Biochemistry 37:14376-14385(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GDP.
[12]"The A326S mutant of Gialpha1 as an approximation of the receptor-bound state."
Posner B.A., Mixon M.B., Wall M.A., Sprang S.R., Gilman A.G.
J. Biol. Chem. 273:21752-21758(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 32-346 IN COMPLEX WITH GDP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17527 mRNA. Translation: AAA40825.1.
DQ120469 mRNA. Translation: AAZ23808.1.
DQ120470 mRNA. Translation: AAZ23809.1.
PIRA35377.
RGRTI1. C27423.
RefSeqNP_037277.1. NM_013145.1.
UniGeneRn.11391.

3D structure databases

PDBe
RCSB-PDB
PDBj
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/D22-354[»]
1SVKX-ray2.00A2-354[»]
1SVSX-ray1.50A2-354[»]
2BCJX-ray3.06Q-[»]
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[»]
DisProtDP00035.
ProteinModelPortalP10824.
SMRP10824. Positions 5-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247715. 1 interaction.
DIPDIP-6073N.
IntActP10824. 2 interactions.
MINTMINT-1795581.

PTM databases

PhosphoSiteP10824.

2D gel databases

World-2DPAGE0004:P10824.

Proteomic databases

PaxDbP10824.
PRIDEP10824.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25686.
KEGGrno:25686.

Organism-specific databases

CTD2770.
RGD2713. Gnai1.

Phylogenomic databases

eggNOGNOG322962.
HOGENOMHOG000038730.
HOVERGENHBG063184.
InParanoidP10824.
KOK04630.
PhylomeDBP10824.

Enzyme and pathway databases

ReactomeREACT_212996. Signal Transduction.
SABIO-RKP10824.

Gene expression databases

GenevestigatorP10824.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10218. PTHR10218. 1 hit.
PfamPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP10824.
NextBio607673.
PROP10824.

Entry information

Entry nameGNAI1_RAT
AccessionPrimary (citable) accession number: P10824
Secondary accession number(s): Q45QN2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references