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Entry version 189 (02 Jun 2021)
Sequence version 3 (23 Jan 2007)
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Protein

Guanine nucleotide-binding protein G(i) subunit alpha-3

Gene

Gnai3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:2159473).

Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels. Stimulates the activity of receptor-regulated K+ channels. The active GTP-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.

By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi47MagnesiumBy similarity1
Metal bindingi181MagnesiumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei326GTP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi43 – 48GTPBy similarity6
Nucleotide bindingi150 – 151GTPBy similarity2
Nucleotide bindingi175 – 181GTPBy similarity7
Nucleotide bindingi200 – 204GTPBy similarity5
Nucleotide bindingi269 – 272GTPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransducer
Biological processCell cycle, Cell division
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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-418594, G alpha (i) signalling events
R-RNO-9009391, Extra-nuclear estrogen signaling

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P08753

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(i) subunit alpha-3
Alternative name(s):
G(i) alpha-3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Gnai3
Synonyms:Gnai-3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Rat genome database

More...
RGDi
2714, Gnai3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi203G → A: Reduces cell migration by 50% and increases mitosis six-fold. 1 Publication1
Mutagenesisi204Q → L: No effect on promotion of cell migration or GTP-binding activity. Increases sensitivity to activation by CCDC88A. 2 Publications1
Mutagenesisi208R → A: Dramatically decreases binding to CCDC88A. 1 Publication1
Mutagenesisi211W → A: Abolishes binding to NUCB1. Dramatically decreases binding to CCDC88A. Does not affect GTP-binding activity but increases the basal exchange rate. 3 Publications1
Mutagenesisi215F → A: Abolishes binding to NUCB1. Dramatically decreases binding to CCDC88A. Does not affect GTP-binding activity but increases the basal exchange rate. 3 Publications1
Mutagenesisi248K → E: Abolishes binding to NUCB1. 1 Publication1
Mutagenesisi248K → M: Dramatically decreases interaction with NUCB1. 1 Publication1
Mutagenesisi258W → F: No effect on interaction with NUCB1. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002036942 – 354Guanine nucleotide-binding protein G(i) subunit alpha-3Add BLAST353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycineBy similarity1
Lipidationi3S-palmitoyl cysteineBy similarity1

Keywords - PTMi

Lipoprotein, Myristate, Palmitate

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P08753

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P08753

PRoteomics IDEntifications database

More...
PRIDEi
P08753

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P08753

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P08753

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P08753

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000019465, Expressed in duodenum and 20 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P08753, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha subunit contains the guanine nucleotide binding site (PubMed:2159473). GTP binding causes dissociation of the heterotrimer, liberating the individual subunits so that they can interact with downstream effector proteins.

Forms a complex with CCDC88A/GIV and EGFR which leads to enhanced EGFR signaling and triggering of cell migration; ligand stimulation is required for recruitment of GNAI3 to the complex (PubMed:20462955).

Interacts (inactive GDP-bound form) with CCDC88A/GIV (via GBA motif); the interaction leads to activation of GNAI3 (PubMed:19211784).

Interacts (inactive GDP-bound form) with CCDC88C/DAPLE (via GBA motif); the interaction leads to activation of GNAI3 (By similarity).

Interacts (inactive GDP-bound form) with NUCB1 (via GBA motif) and NUCB2 (via GBA motif); the interaction leads to activation of GNAI3 (PubMed:21653697).

Interacts (inactive GDP-bound form) with PLCD4 (via GBA motif); the interaction leads to activation of GNAI3 (By similarity).

Interacts with INSR; the interaction is probably mediated by CCDC88A/GIV (PubMed:25187647).

Interacts with GPSM1 (PubMed:11121039).

Interacts (GDP-bound form) with GPSM2 (via GoLoco domains). Does not interact with RGS2.

Interacts with RGS8 and RGS10; this strongly enhances the intrinsic GTPase activity (By similarity).

Interacts with RGS12 (PubMed:11387333).

Interacts with RGS16; this strongly enhances the intrinsic GTPase activity (By similarity).

Interacts (via active GTP- or inactive GDP-bound form) with RGS14 (PubMed:11387333, PubMed:16870394).

By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
247672, 2 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P08753

Database of interacting proteins

More...
DIPi
DIP-608N

Protein interaction database and analysis system

More...
IntActi
P08753, 3 interactors

Molecular INTeraction database

More...
MINTi
P08753

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000026710

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1354
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P08753

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P08753

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini32 – 354G-alphaPROSITE-ProRule annotationAdd BLAST323

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni35 – 48G1 motifPROSITE-ProRule annotationAdd BLAST14
Regioni173 – 181G2 motifPROSITE-ProRule annotation9
Regioni196 – 205G3 motifPROSITE-ProRule annotation10
Regioni265 – 272G4 motifPROSITE-ProRule annotation8
Regioni324 – 329G5 motifPROSITE-ProRule annotation6

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0082, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153567

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_014184_6_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P08753

Identification of Orthologs from Complete Genome Data

More...
OMAi
PEYSGGH

Database of Orthologous Groups

More...
OrthoDBi
754573at2759

TreeFam database of animal gene trees

More...
TreeFami
TF300673

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00066, G-alpha, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.400.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001408, Gprotein_alpha_I
IPR001019, Gprotein_alpha_su
IPR011025, GproteinA_insert
IPR027417, P-loop_NTPase

The PANTHER Classification System

More...
PANTHERi
PTHR10218, PTHR10218, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00503, G-alpha, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00318, GPROTEINA
PR00441, GPROTEINAI

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00275, G_alpha, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47895, SSF47895, 1 hit
SSF52540, SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51882, G_ALPHA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P08753-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEDG YSEDECKQYK VVVYSNTIQS IIAIIRAMGR LKIDFGEAAR
110 120 130 140 150
ADDARQLFVL AGSAEEGVMT SELAGVIKRL WRDGGVQACF SRSREYQLND
160 170 180 190 200
SASYYLNDLD RISQTNYIPT QQDVLRTRVK TTGIVETHFT FKELYFKMFD
210 220 230 240 250
VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM NRMHESMKLF
260 270 280 290 300
DSICNNKWFT DTSIILFLNK KDLFEEKIKR SPLTICYPEY TGSNTYEEAA
310 320 330 340 350
AYIQCQFEDL NRRKDTKEVY THFTCATDTK NVQFVFDAVT DVIIKNNLKE

CGLY
Length:354
Mass (Da):40,522
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA65D63CE5A32C777
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J03219 mRNA Translation: AAA41224.1
M20713 mRNA Translation: AAA40823.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E27423, RGRTI3

NCBI Reference Sequences

More...
RefSeqi
NP_037238.1, NM_013106.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000026710; ENSRNOP00000026710; ENSRNOG00000019465

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25643

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25643

UCSC genome browser

More...
UCSCi
RGD:2714, rat

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03219 mRNA Translation: AAA41224.1
M20713 mRNA Translation: AAA40823.1
PIRiE27423, RGRTI3
RefSeqiNP_037238.1, NM_013106.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6MHEX-ray2.20A26-354[»]
6MHFX-ray2.00A26-354[»]
BMRBiP08753
SMRiP08753
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi247672, 2 interactors
CORUMiP08753
DIPiDIP-608N
IntActiP08753, 3 interactors
MINTiP08753
STRINGi10116.ENSRNOP00000026710

PTM databases

iPTMnetiP08753
PhosphoSitePlusiP08753
SwissPalmiP08753

Proteomic databases

jPOSTiP08753
PaxDbiP08753
PRIDEiP08753

Genome annotation databases

EnsembliENSRNOT00000026710; ENSRNOP00000026710; ENSRNOG00000019465
GeneIDi25643
KEGGirno:25643
UCSCiRGD:2714, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2773
RGDi2714, Gnai3

Phylogenomic databases

eggNOGiKOG0082, Eukaryota
GeneTreeiENSGT00940000153567
HOGENOMiCLU_014184_6_0_1
InParanoidiP08753
OMAiPEYSGGH
OrthoDBi754573at2759
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-418594, G alpha (i) signalling events
R-RNO-9009391, Extra-nuclear estrogen signaling
SABIO-RKiP08753

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P08753

Gene expression databases

BgeeiENSRNOG00000019465, Expressed in duodenum and 20 other tissues
GenevisibleiP08753, RN

Family and domain databases

CDDicd00066, G-alpha, 1 hit
Gene3Di1.10.400.10, 1 hit
InterProiView protein in InterPro
IPR001408, Gprotein_alpha_I
IPR001019, Gprotein_alpha_su
IPR011025, GproteinA_insert
IPR027417, P-loop_NTPase
PANTHERiPTHR10218, PTHR10218, 1 hit
PfamiView protein in Pfam
PF00503, G-alpha, 1 hit
PRINTSiPR00318, GPROTEINA
PR00441, GPROTEINAI
SMARTiView protein in SMART
SM00275, G_alpha, 1 hit
SUPFAMiSSF47895, SSF47895, 1 hit
SSF52540, SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51882, G_ALPHA, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGNAI3_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08753
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 189 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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