P08752 (GNAI2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Adenylate cyclase-inhibiting G alpha protein

Gene names

Name:	Gnai2
Synonyms:	Gnai-2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	355 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. May play a role in cell division.
Subunit structure	G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with UNC5B. Interacts with GPSM1. Interacts with RGS12 and RGS14 By similarity.
Subcellular location	Cytoplasm By similarity. Cytoplasm › cytoskeleton › centrosome By similarity. Cell membrane By similarity. Note: Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody By similarity.
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
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transducer
PTM	Lipoprotein Myristate Palmitate
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled acetylcholine receptor signaling pathway Inferred from mutant phenotype PubMed 11299198. Source: MGI activation of MAPKK activity Inferred from electronic annotation. Source: Compara adenosine receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Inferred from mutant phenotype PubMed 8622915. Source: MGI cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from sequence or structural similarity. Source: UniProtKB cell proliferation Inferred from physical interaction PubMed 14712229. Source: MGI gamma-aminobutyric acid signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome intracellular protein kinase cascade Inferred from electronic annotation. Source: Compara negative regulation of synaptic transmission Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara regulation of calcium ion transport Inferred from electronic annotation. Source: Compara
Cellular_component	centrosome Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara heterotrimeric G-protein complex Inferred from Biological aspect of Ancestor. Source: RefGenome membrane raft Inferred from electronic annotation. Source: Compara midbody Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	G-protein beta/gamma-subunit complex binding Inferred from Biological aspect of Ancestor. Source: RefGenome G-protein coupled receptor binding Inferred from Biological aspect of Ancestor. Source: RefGenome GTP binding Inferred from sequence alignment Ref.1. Source: MGI GTPase activity Inferred from Biological aspect of Ancestor. Source: RefGenome 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 – 355	355	Guanine nucleotide-binding protein G(i) subunit alpha-2		PRO_0000203681
Regions
	Nucleotide binding	40 – 47	8	GTP By similarity
	Nucleotide binding	176 – 182	7	GTP By similarity
	Nucleotide binding	201 – 205	5	GTP By similarity
	Nucleotide binding	270 – 273	4	GTP By similarity
Sites
	Metal binding	47	1	Magnesium By similarity
	Metal binding	182	1	Magnesium By similarity
	Binding site	327	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
	Sequence conflict	82	1	M → I in AAB30632. Ref.4
	Sequence conflict	82	1	M → L in AAA37692. Ref.1
	Sequence conflict	87	1	A → R in AAA37692. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P08752 [UniParc]. Last modified July 27, 2011. Version 5. Checksum: 90AC64AFA713493E	FASTA	355	40,489
	10 20 30 40 50 60 MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG 70 80 90 100 110 120 YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPQR ADDARQLFAL SCAAEEQGML 130 140 150 160 170 180 PEDLSGVIRR LWADHGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV 190 200 210 220 230 240 KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE 250 260 270 280 290 300 MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT QSSLTICFPE YTGANKYDEA 310 320 330 340 350 ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Inhibitory and stimulatory G proteins of adenylate cyclase: cDNA and amino acid sequences of the alpha chains." Sullivan K.A., Liao Y.-C., Alborzi A., Beiderman B., Chang F.-H., Masters S.B., Levinson A.D., Bourne H.R. Proc. Natl. Acad. Sci. U.S.A. 83:6687-6691(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Inner ear and Placenta.
[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]. Strain: C57BL/6. Tissue: Brain.
[4]	"G protein Gi2 alpha in the cochlea: cloning and selective occurrence in receptor cells." Tachibana M., Asano T., Wilcox E., Yokotani N., Rivolta M.N., Fex J. Brain Res. Mol. Brain Res. 21:355-358(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-355.
[5]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 36-46; 55-67; 146-162; 182-193; 199-206; 250-258; 279-296 AND 319-331, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M13963 mRNA. Translation: AAA37692.1. AK157998 mRNA. Translation: BAE34308.1. AK159222 mRNA. Translation: BAE34909.1. AK167388 mRNA. Translation: BAE39478.1. BC065159 mRNA. Translation: AAH65159.1. S71213 mRNA. Translation: AAB30632.2.
IPI	IPI00228617.
PIR	RGMSI2. B25889.
RefSeq	NP_032164.2. NM_008138.4.
UniGene	Mm.196464.
3D structure databases
ProteinModelPortal	P08752.
SMR	P08752. Positions 5-354.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-605N.
IntAct	P08752. 5 interactions.
STRING	10090.ENSMUSP00000057543.
PTM databases
PhosphoSite	P08752.
Proteomic databases
PaxDb	P08752.
PRIDE	P08752.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000055704; ENSMUSP00000057543; ENSMUSG00000032562.
GeneID	14678.
KEGG	mmu:14678.
Organism-specific databases
CTD	2771.
MGI	MGI:95772. Gnai2.
Phylogenomic databases
eggNOG	NOG322962.
GeneTree	ENSGT00690000101958.
HOGENOM	HOG000038730.
HOVERGEN	HBG063184.
InParanoid	Q3TXK7.
KO	K04630.
OMA	VIRRLWS.
OrthoDB	EOG4WDDC1.
Gene expression databases
ArrayExpress	P08752.
Bgee	P08752.
Genevestigator	P08752.
GermOnline	ENSMUSG00000032562. Mus musculus.
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
ChiTaRS	GNAI2. mouse.
NextBio	286578.
SOURCE	Search...

Entry information

Entry name

GNAI2_MOUSE

Accession

Primary (citable) accession number: P08752
Secondary accession number(s): Q3TXK7, Q6P1C0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	July 27, 2011
Last modified:	April 3, 2013
This is version 129 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program