P10824 (GNAI1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › centrosome. 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 process	Cell cycle Cell division
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane Nucleus
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transducer
PTM	Lipoprotein Myristate Palmitate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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_component	centrosome Inferred from direct assay Ref.6. Source: UniProtKB cytoplasm Inferred from direct assay Ref.6. Source: UniProtKB heterotrimeric G-protein complex Inferred from Biological aspect of Ancestor. Source: RefGenome 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
Molecular_function	G-protein beta/gamma-subunit complex binding Inferred from Biological aspect of Ancestor. Source: RefGenome 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 signal transducer activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 354

354

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

PRO_0000203673

Regions

Nucleotide binding

40 – 47

8

GTP By similarity

Nucleotide binding

43 – 48

6

GTP

Nucleotide binding

175 – 181

7

GTP By similarity

Nucleotide binding

175 – 178

4

GTP

Nucleotide binding

200 – 204

5

GTP By similarity

Nucleotide binding

269 – 272

4

GTP

Sites

Metal binding

47

1

Magnesium By similarity

Metal binding

181

1

Magnesium By similarity

Binding site

326

1

GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation

2

1

N-myristoyl glycine By similarity

Lipidation

3

1

S-palmitoyl cysteine By similarity

Experimental info

Mutagenesis

149

1

N → I: Inhibits interaction with RGS14. Does not inhibit interaction with RIC8A. Ref.7

Mutagenesis

204

1

Q → L: Does not inhibit interaction with GNAI1 in the centrosomes. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

354

Helix Strand Turn

Details...

Helix

11 – 16

6

Helix

20 – 23

4

Helix

27 – 29

3

Beta strand

33 – 39

7

Helix

46 – 57

12

Helix

63 – 68

6

Helix

70 – 91

22

Helix

100 – 110

11

Helix

111 – 116

6

Helix

121 – 132

12

Helix

134 – 140

7

Helix

141 – 145

5

Helix

152 – 156

5

Helix

159 – 162

4

Beta strand

164 – 166

3

Helix

171 – 175

5

Beta strand

183 – 191

9

Beta strand

194 – 201

8

Helix

205 – 214

10

Beta strand

219 – 226

8

Helix

227 – 231

5

Beta strand

237 – 241

5

Helix

242 – 254

13

Helix

257 – 259

3

Beta strand

262 – 269

8

Helix

271 – 278

8

Helix

283 – 285

3

Helix

296 – 308

13

Turn

314 – 316

3

Beta strand

319 – 323

5

Helix

329 – 346

18

Helix

348 – 350

3

Sequences

	Sequence		Length	Mass (Da)
	P10824 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 99E9D11B485C2DE3	FASTA	354	40,345
	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

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.

IPI

IPI00231733.

PIR

A35377.
RGRTI1. C27423.

RefSeq

NP_037277.1. NM_013145.1.

UniGene

Rn.11391.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AGR	X-ray	2.80	A/D	2-354	[»]
1AS0	X-ray	2.00	A	2-353	[»]
1AS2	X-ray	2.80	A	2-353	[»]
1AS3	X-ray	2.40	A	2-353	[»]
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	2-353	[»]
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	2-353	[»]
1GP2	X-ray	2.30	A	2-354	[»]
1SHZ	X-ray	2.85	A/D	22-354	[»]
1SVK	X-ray	2.00	A	2-353	[»]
1SVS	X-ray	1.50	A	2-353	[»]
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	1-354	[»]
3FFB	X-ray	2.57	A	1-354	[»]
3V00	X-ray	2.90	A/B/C	25-354	[»]

DisProt

DP00035.

ProteinModelPortal

P10824.

SMR

P10824. Positions 5-353.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6073N.

IntAct

P10824. 1 interaction.

PTM databases

PhosphoSite

P10824.

2D gel databases

World-2DPAGE

0004:P10824.

Proteomic databases

PaxDb

P10824.

PRIDE

P10824.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

25686.

KEGG

rno:25686.

Organism-specific databases

CTD

2770.

RGD

2713. Gnai1.

Phylogenomic databases

eggNOG

NOG322962.

HOGENOM

HOG000038730.

HOVERGEN

HBG063184.

InParanoid

P10824.

KO

K04630.

OrthoDB

EOG4WDDC1.

Enzyme and pathway databases

Reactome

REACT_111984. Signal Transduction.

SABIO-RK

P10824.

Gene expression databases

ArrayExpress

P10824.

Genevestigator

P10824.

GermOnline

ENSRNOG00000019465. Rattus norvegicus.

Family and domain databases

Gene3D

1.10.400.10. 1 hit.

InterPro

IPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
[Graphical view]

PANTHER

PTHR10218. PTHR10218. 1 hit.

Pfam

PF00503. G-alpha. 1 hit.
[Graphical view]

PRINTS

PR00318. GPROTEINA.
PR00441. GPROTEINAI.

SMART

SM00275. G_alpha. 1 hit.
[Graphical view]

SUPFAM

SSF47895. Transducn_insert. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P10824.

NextBio

607673.

Entry information

Entry name

GNAI1_RAT

Accession

Primary (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:	May 1, 2013
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program