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P10824

- GNAI1_RAT

UniProt

P10824 - GNAI1_RAT

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Protein

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

Gene

Gnai1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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. 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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471MagnesiumBy similarity
Metal bindingi181 – 1811MagnesiumBy similarity
Binding sitei326 – 3261GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 478GTPBy similarity
Nucleotide bindingi43 – 486GTP
Nucleotide bindingi175 – 1817GTPBy similarity
Nucleotide bindingi175 – 1784GTP
Nucleotide bindingi200 – 2045GTPBy similarity
Nucleotide bindingi269 – 2724GTP

GO - Molecular functioni

  1. GDP binding Source: RGD
  2. G-protein beta/gamma-subunit complex binding Source: RefGenome
  3. G-protein coupled serotonin receptor binding Source: RGD
  4. GTPase activating protein binding Source: RGD
  5. GTPase activity Source: RefGenome
  6. GTP binding Source: UniProtKB-KW
  7. metal ion binding Source: UniProtKB-KW
  8. signal transducer activity Source: RefGenome

GO - Biological processi

  1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: RefGenome
  2. cell cycle Source: UniProtKB-KW
  3. cell division Source: UniProtKB
  4. G-protein coupled receptor signaling pathway Source: RGD
  5. negative regulation of synaptic transmission 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

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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2713. Gnai1.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. heterotrimeric G-protein complex Source: RefGenome
  4. membrane Source: RGD
  5. membrane raft Source: RGD
  6. midbody Source: UniProtKB
  7. nucleus Source: UniProtKB-KW
  8. plasma membrane Source: UniProtKB
  9. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi149 – 1491N → I: Inhibits interaction with RGS14. Does not inhibit interaction with RIC8A. 1 Publication
Mutagenesisi204 – 2041Q → L: Does not inhibit interaction with GNAI1 in the centrosomes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 354353Guanine nucleotide-binding protein G(i) subunit alpha-1PRO_0000203673Add
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

PaxDbiP10824.
PRIDEiP10824.

2D gel databases

World-2DPAGE0004:P10824.

PTM databases

PhosphoSiteiP10824.

Expressioni

Gene expression databases

GenevestigatoriP10824.

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 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).By similarity

Protein-protein interaction databases

BioGridi247715. 1 interaction.
DIPiDIP-6073N.
IntActiP10824. 2 interactions.
MINTiMINT-1795581.

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 167
Helixi20 – 234
Helixi27 – 293
Beta strandi33 – 397
Helixi46 – 5712
Helixi63 – 686
Helixi70 – 9122
Helixi100 – 11011
Helixi111 – 1166
Helixi121 – 13212
Helixi134 – 1407
Helixi141 – 1455
Helixi152 – 1565
Helixi159 – 1624
Beta strandi164 – 1663
Helixi171 – 1755
Beta strandi183 – 1919
Beta strandi194 – 2018
Helixi205 – 21410
Beta strandi219 – 2268
Helixi227 – 2315
Beta strandi237 – 2415
Helixi242 – 25413
Helixi257 – 2593
Beta strandi262 – 2698
Helixi271 – 2788
Helixi283 – 2853
Helixi296 – 30813
Turni314 – 3163
Beta strandi319 – 3235
Helixi329 – 34618
Helixi348 – 3503

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4PAMX-ray2.10A1-354[»]
4PANX-ray2.40A1-354[»]
4PAOX-ray2.00A1-354[»]
4PAQX-ray2.00A1-354[»]
DisProtiDP00035.
ProteinModelPortaliP10824.
SMRiP10824. Positions 5-353.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10824.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG322962.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP10824.
KOiK04630.
PhylomeDBiP10824.

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.

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:
EMBL
GenBank
DDBJ
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

GeneIDi25686.
KEGGirno:25686.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M17527 mRNA. Translation: AAA40825.1 .
DQ120469 mRNA. Translation: AAZ23808.1 .
DQ120470 mRNA. Translation: AAZ23809.1 .
PIRi A35377.
C27423. RGRTI1.
RefSeqi NP_037277.1. NM_013145.1.
UniGenei Rn.11391.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AGR X-ray 2.80 A/D 2-354 [» ]
1AS0 X-ray 2.00 A 2-354 [» ]
1AS2 X-ray 2.80 A 2-354 [» ]
1AS3 X-ray 2.40 A 2-354 [» ]
1BH2 X-ray 2.10 A 32-346 [» ]
1BOF X-ray 2.20 A 2-354 [» ]
1CIP X-ray 1.50 A 2-354 [» ]
1GDD X-ray 2.20 A 2-354 [» ]
1GFI X-ray 2.20 A 2-354 [» ]
1GG2 X-ray 2.40 A 2-354 [» ]
1GIA X-ray 2.00 A 2-354 [» ]
1GIL X-ray 2.30 A 2-354 [» ]
1GIT X-ray 2.60 A 2-354 [» ]
1GP2 X-ray 2.30 A 2-354 [» ]
1SHZ X-ray 2.85 A/D 22-354 [» ]
1SVK X-ray 2.00 A 2-354 [» ]
1SVS X-ray 1.50 A 2-354 [» ]
2BCJ X-ray 3.06 Q - [» ]
2ZJY X-ray 2.80 A 1-354 [» ]
2ZJZ X-ray 2.60 A/B 1-354 [» ]
3AH8 X-ray 2.90 A 2-28 [» ]
3D7M X-ray 2.90 A 1-354 [» ]
3FFA X-ray 2.30 A 1-348 [» ]
3FFB X-ray 2.57 A 1-354 [» ]
3V00 X-ray 2.90 A/B/C 220-298 [» ]
4N0D X-ray 1.55 A 1-354 [» ]
4N0E X-ray 2.10 A 1-354 [» ]
4PAM X-ray 2.10 A 1-354 [» ]
4PAN X-ray 2.40 A 1-354 [» ]
4PAO X-ray 2.00 A 1-354 [» ]
4PAQ X-ray 2.00 A 1-354 [» ]
DisProti DP00035.
ProteinModelPortali P10824.
SMRi P10824. Positions 5-353.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247715. 1 interaction.
DIPi DIP-6073N.
IntActi P10824. 2 interactions.
MINTi MINT-1795581.

PTM databases

PhosphoSitei P10824.

2D gel databases

World-2DPAGE 0004:P10824.

Proteomic databases

PaxDbi P10824.
PRIDEi P10824.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25686.
KEGGi rno:25686.

Organism-specific databases

CTDi 2770.
RGDi 2713. Gnai1.

Phylogenomic databases

eggNOGi NOG322962.
HOGENOMi HOG000038730.
HOVERGENi HBG063184.
InParanoidi P10824.
KOi K04630.
PhylomeDBi P10824.

Enzyme and pathway databases

SABIO-RK P10824.

Miscellaneous databases

EvolutionaryTracei P10824.
NextBioi 607673.
PROi P10824.

Gene expression databases

Genevestigatori P10824.

Family and domain databases

Gene3Di 1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR10218. PTHR10218. 1 hit.
Pfami PF00503. G-alpha. 1 hit.
[Graphical view ]
PRINTSi PR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTi SM00275. G_alpha. 1 hit.
[Graphical view ]
SUPFAMi SSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNeti Search...

Publicationsi

  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.

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: October 29, 2014
This is version 148 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

External Data

Dasty 3