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Entry version 223 (29 Sep 2021)
Sequence version 3 (23 Jan 2007)
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Protein

Guanine nucleotide-binding protein alpha-1 subunit

Gene

GPA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

Alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) that mediates mating pheromone signal transduction. Binding of alpha-factor or a-factor to its cognate transmembrane receptor STE2 and STE3, respectively, allows the receptor to serve as a guanine nucleotide exchange factor (GEF) on GPA1. The exchange of GDP for GTP on the G protein alpha subunit alters its interaction with the G protein beta subunit STE4, leading to dissociation of the G protein beta-gamma dimer STE4-STE18. The dissociated subunits activate downstream effectors to activate the mating response pathway and induce changes necessary to produce mating-competent cells. STE4-STE18 activate the downstream pheromone signaling MAP kinase cascade leading to expression of mating-specific genes, inducing cell cycle arrest in G1, promoting polarized cell growth to form mating projections (shmoos), and establishing the changes in plasma membrane, cell wall and nuclear envelope to permit cell-cell fusion (plasmogamy) and fusion of the two haploid nuclei (karyogamy). GPA1 transmits a signal that requires direct binding to the effector enzyme PI3K located at the endosome, promoting increased PI3 production. The intrinsic GTPase activity of GPA1 determines the duration of signaling, and is dramatically accelerated by the RGS protein SST2. In unstimulated cells, GDP-bound GPA1 sequesters the G protein beta-gamma subunit STE4-STE18, preventing it from activating the downstream effectors. Also down-regulates the signal by inhibiting the pheromone-induced accumulation of FUS3 in the nucleus.

20 Publications

Miscellaneous

Present with 9920 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the G protein coupled receptors (GPCRs) STE2 and STE3, which serve as guanine nucleotide-exchange factors (GEFs), and inactivated by SST2, probably acting as a GTPase-activating protein (GAP).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi55MagnesiumBy similarity1
Metal bindingi300MagnesiumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei444GTP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi48 – 55GTPBy similarity8
Nucleotide bindingi294 – 300GTPBy similarity7
Nucleotide bindingi319 – 323GTPBy similarity5
Nucleotide bindingi388 – 391GTPBy 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 processPheromone response
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-112043, PLC beta mediated events
R-SCE-202040, G-protein activation
R-SCE-399997, Acetylcholine regulates insulin secretion
R-SCE-416476, G alpha (q) signalling events
R-SCE-416482, G alpha (12/13) signalling events
R-SCE-418592, ADP signalling through P2Y purinoceptor 1
R-SCE-434316, Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion
R-SCE-9013148, CDC42 GTPase cycle

<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_and_taxonomy_section">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 alpha-1 subunit
Alternative name(s):
GP1-alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:GPA1
Synonyms:CDC70, DAC1, SCG1
Ordered Locus Names:YHR005C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 VIII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000001047, GPA1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YHR005C

<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, Endosome, 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_and_biotech_section">'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>Mutagenesisi2G → A: Abolishes both palmitoylation and N-myristoylation. 3 Publications1
Mutagenesisi3C → A: Abolishes palmitoylation but not N-myristoylation. 2 Publications1
Mutagenesisi15D → V: Slightly reduces ligand-dependent pheromone signaling. 1 Publication1
Mutagenesisi17F → L: Leads to a hypersensitive signaling phenotype resulting in greatly enhanced signal at low alpha-factor concentrations. 1 Publication1
Mutagenesisi18L → P or Q: Reduces ligand-dependent pheromone signaling. 1 Publication1
Mutagenesisi21 – 22KR → EE: Impairs interaction with FUS3. 1 Publication2
Mutagenesisi50G → D: Confers insensitivity to pheromone. 4 Publications1
Mutagenesisi50G → V: Has increased GTP occupancy and moderately reduces hydrolysis of GTP, resulting in a constitutively active form that down-regulates the pheromone response and causes hyperadaptation to pheromone. 4 Publications1
Mutagenesisi54K → E or I: Prevents GDP to GTP exchange; suppressor of L-323. 2 Publications1
Mutagenesisi165K → R: Substantial decrease in ubiquitination. 1 Publication1
Mutagenesisi297R → H: Slows hydrolysis of GTP. 1
Mutagenesisi302G → S in GPA1(SST); weakens interaction to SST2 and blocks its negative regulatory effect. 1 Publication1
Mutagenesisi321G → T: Causes a specific mating defect in alpha cells. 1 Publication1
Mutagenesisi322G → A, E or R: Confers insensitivity to pheromone. 3 Publications1
Mutagenesisi323Q → L: Prevents hydrolysis of GTP; eliminates the interaction with STE4 and constitutively activates the pheromone response pathway. 1 Publication1
Mutagenesisi327R → S: Suppressor of L-323; does not prevent GTP binding to GPA1. 1 Publication1
Mutagenesisi345A → T: Suppressor of a STE2-L236H mutant. 1 Publication1
Mutagenesisi353Missing : Suppressor of L-323. 1 Publication1
Mutagenesisi355E → K: Confers insensitivity to pheromone. 1 Publication1
Mutagenesisi364E → K: Enhances the rate of GDP for GTP exchange and slows hydrolysis of GTP, resulting in a constitutively active form that down-regulates the pheromone response independently of the pheromone receptor. 3 Publications1
Mutagenesisi388N → D: Forms a nondissociable complex with the pheromone receptor in response to receptor activation, resulting in reduced pheromone responsiveness. 4 Publications1
Mutagenesisi388N → K: Causes constitutive activation of the pheromone response pathway. 4 Publications1
Mutagenesisi391D → A: Causes constitutive activation of the pheromone response pathway. 1 Publication1
Mutagenesisi467K → P: Impairs pheromone signaling in a and alpha cells. 1 Publication1
Mutagenesisi468K → P: Impairs pheromone signaling specifically in a cells. 1 Publication1
Mutagenesisi470G → D: Confers insensitivity to pheromone. 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_processing_section">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 methionineiRemoved
<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_00002036162 – 472Guanine nucleotide-binding protein alpha-1 subunitAdd BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 glycine3 Publications1
Lipidationi3S-palmitoyl cysteine2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-myristoylation by NMT1 is pheromone-stimulated and required for palmitoylation of Cys-3. This lipid modification anchors the protein to membranes. Depalmitoylated by YLR118C/APT1.5 Publications
Monoubiquitination targets the protein for degradation to the vacuole, and polyubiquitination tags the protein for degradation by the proteasome. This may be an additional signaling regulation mechanism.1 Publication

Keywords - PTMi

Isopeptide bond, Lipoprotein, Myristate, Palmitate, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P08539

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

More...
PaxDbi
P08539

PRoteomics IDEntifications database

More...
PRIDEi
P08539

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P08539

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P08539

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. In its GDP-bound form, binds to the G protein beta-gamma dimer STE4-STE18. Directly interacts with the beta subunit STE4. Probably forms preactivation complexes with unligated receptors STE2 and STE3.

Interacts with FUS3. Pheromone-induced activation of GPA1 increases its association with FUS3.

Interacts with SCP160. SCP160 binds specifically to the GTP-bound form of GPA1.

Interacts with the phoshpatidylinositol 3-kinase (PI3K) subunits VPS15 and VPS34 at the endosome. The GTP-bound form of GPA1 binds directly and selectively to the catalytic subunit VPS34, while the GDP-bound form binds to VPS15, which appears to function as an alternative G protein beta subunit for GPA1.

Interacts with regulators of G protein signaling (RGS) proteins MDM1, RAX1, RGS2 and SST2, but SST2 alone binds preferentially to the transition state conformation of GPA1, indicating that it acts as a GAP for this G protein.

7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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

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GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
36430, 57 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1646, G protein heterotrimer

Database of interacting proteins

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DIPi
DIP-15N

Protein interaction database and analysis system

More...
IntActi
P08539, 17 interactors

STRING: functional protein association networks

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STRINGi
4932.YHR005C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P08539, protein

<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

1472
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P08539

Database of comparative protein structure models

More...
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_and_domains_section">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>Domaini40 – 472G-alphaPROSITE-ProRule annotationAdd BLAST433

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>Regioni43 – 56G1 motifPROSITE-ProRule annotationAdd BLAST14
Regioni127 – 235Insert; not present in other G-proteinsAdd BLAST109
Regioni162 – 199DisorderedSequence analysisAdd BLAST38
Regioni292 – 300G2 motifPROSITE-ProRule annotation9
Regioni315 – 324G3 motifPROSITE-ProRule annotation10
Regioni384 – 391G4 motifPROSITE-ProRule annotation8
Regioni442 – 447G5 motifPROSITE-ProRule annotation6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi175 – 191Basic and acidic residuesSequence analysisAdd BLAST17

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains an 'insertion' sequence of 109 residues which is not present in other G-protein alpha chains.

<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(q) subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0082, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000168787

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_014184_2_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P08539

Identification of Orthologs from Complete Genome Data

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OMAi
QVIWADA

Family and domain databases

Conserved Domains Database

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CDDi
cd00066, G-alpha, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.400.10, 2 hits
3.40.50.300, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002975, Fungi_Gprotein_alpha
IPR001019, Gprotein_alpha_su
IPR011025, GproteinA_insert
IPR027417, P-loop_NTPase

The PANTHER Classification System

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PANTHERi
PTHR10218, PTHR10218, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00318, GPROTEINA
PR01241, GPROTEINAFNG

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00275, G_alpha, 1 hit

Superfamily database of structural and functional annotation

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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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P08539-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGCTVSTQTI GDESDPFLQN KRANDVIEQS LQLEKQRDKN EIKLLLLGAG
60 70 80 90 100
ESGKSTVLKQ LKLLHQGGFS HQERLQYAQV IWADAIQSMK ILIIQARKLG
110 120 130 140 150
IQLDCDDPIN NKDLFACKRI LLKAKALDYI NASVAGGSDF LNDYVLKYSE
160 170 180 190 200
RYETRRRVQS TGRAKAAFDE DGNISNVKSD TDRDAETVTQ NEDADRNNSS
210 220 230 240 250
RINLQDICKD LNQEGDDQMF VRKTSREIQG QNRRNLIHED IAKAIKQLWN
260 270 280 290 300
NDKGIKQCFA RSNEFQLEGS AAYYFDNIEK FASPNYVCTD EDILKGRIKT
310 320 330 340 350
TGITETEFNI GSSKFKVLDA GGQRSERKKW IHCFEGITAV LFVLAMSEYD
360 370 380 390 400
QMLFEDERVN RMHESIMLFD TLLNSKWFKD TPFILFLNKI DLFEEKVKSM
410 420 430 440 450
PIRKYFPDYQ GRVGDAEAGL KYFEKIFLSL NKTNKPIYVK RTCATDTQTM
460 470
KFVLSAVTDL IIQQNLKKIG II
Length:472
Mass (Da):54,076
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:i2E87C546E133D6E5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti82W → R in AAA18403 (PubMed:3113738).Curated1
Sequence conflicti194A → V in AAA18403 (PubMed:3113738).Curated1
Sequence conflicti226R → K in AAA18403 (PubMed:3113738).Curated1
Sequence conflicti246K → R in AAA18403 (PubMed:3113738).Curated1
Sequence conflicti469I → S in AAA18403 (PubMed:3113738).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M15867 Genomic DNA Translation: AAA34650.1
M17414 Unassigned DNA Translation: AAA18403.1
U10555 Genomic DNA Translation: AAB68432.1
AY692963 Genomic DNA Translation: AAT92982.1
BK006934 Genomic DNA Translation: DAA06692.1

Protein sequence database of the Protein Information Resource

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PIRi
A25906

NCBI Reference Sequences

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RefSeqi
NP_011868.1, NM_001179135.1

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YHR005C_mRNA; YHR005C; YHR005C

Database of genes from NCBI RefSeq genomes

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GeneIDi
856394

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
sce:YHR005C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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
M15867 Genomic DNA Translation: AAA34650.1
M17414 Unassigned DNA Translation: AAA18403.1
U10555 Genomic DNA Translation: AAB68432.1
AY692963 Genomic DNA Translation: AAT92982.1
BK006934 Genomic DNA Translation: DAA06692.1
PIRiA25906
RefSeqiNP_011868.1, NM_001179135.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SCGmodel-A1-472[»]
7AD3electron microscopy3.50E/H300-472[»]
SMRiP08539
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi36430, 57 interactors
ComplexPortaliCPX-1646, G protein heterotrimer
DIPiDIP-15N
IntActiP08539, 17 interactors
STRINGi4932.YHR005C

PTM databases

iPTMnetiP08539
SwissPalmiP08539

Proteomic databases

MaxQBiP08539
PaxDbiP08539
PRIDEiP08539

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
856394

Genome annotation databases

EnsemblFungiiYHR005C_mRNA; YHR005C; YHR005C
GeneIDi856394
KEGGisce:YHR005C

Organism-specific databases

SGDiS000001047, GPA1
VEuPathDBiFungiDB:YHR005C

Phylogenomic databases

eggNOGiKOG0082, Eukaryota
GeneTreeiENSGT00940000168787
HOGENOMiCLU_014184_2_0_1
InParanoidiP08539
OMAiQVIWADA

Enzyme and pathway databases

ReactomeiR-SCE-112043, PLC beta mediated events
R-SCE-202040, G-protein activation
R-SCE-399997, Acetylcholine regulates insulin secretion
R-SCE-416476, G alpha (q) signalling events
R-SCE-416482, G alpha (12/13) signalling events
R-SCE-418592, ADP signalling through P2Y purinoceptor 1
R-SCE-434316, Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion
R-SCE-9013148, CDC42 GTPase cycle

Miscellaneous databases

Protein Ontology

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PROi
PR:P08539
RNActiP08539, protein

Family and domain databases

CDDicd00066, G-alpha, 1 hit
Gene3Di1.10.400.10, 2 hits
3.40.50.300, 2 hits
InterProiView protein in InterPro
IPR002975, Fungi_Gprotein_alpha
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
PR01241, GPROTEINAFNG
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
Search...

<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 nameiGPA1_YEAST
<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: P08539
Secondary accession number(s): D3DKU8
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 223 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 programFungal 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, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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