| Tag |
Content |
LipidDB ID |
LipidDB-3702-00567 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
4.79 |
Molecular Weight |
11139.4 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
Guanine nucleotide-binding protein subunit gamma 2 |
Protein Synonyms/Alias |
Ggamma-subunit 2; Heterotrimeric G protein gamma-subunit 2; AtAGG2; |
Gene Name |
GG2 |
Gene Synonyms/Alias |
AGG2; At3g22942; F5N5; |
Created Date |
31-OCT-2012 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
95 | Canonical | GPKEAKRCGCSIL** | [1][2] | S-Palmitoylation | 97 | Canonical | KEAKRCGCSIL**** | [2] | S-Farnesylation |
|
Organism |
Arabidopsis thaliana (Mouse-ear cress) |
NCBI Taxa ID |
3702 |
Reference |
[1] Adjobo-Hermans MJ, Goedhart J, Gadella TW Jr. Plant G protein heterotrimersrequire dual lipidation motifs of Galpha and Ggamma and do not dissociate uponactivation. J Cell Sci. 2006 Dec 15;119(Pt 24):5087-97.[ PMID:17158913]
[2] Zeng Q, Wang X, Running MP. Dual lipid modification of ArabidopsisGgamma-subunits is required for efficient plasma membrane targeting. PlantPhysiol. 2007 Mar;143(3):1119-31. Epub 2007 Jan 12.[ PMID:17220359]
|
Functional Description |
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Involved in the abscisic acid (ABA) and ethylene signaling pathways. Regulates basipetal transport of auxin (IAA) in roots and hypocotyls, and thus modulates root architecture (e.g. lateral root formation). The heterotrimeric G- protein controls defense responses to necrotrophic and vascular fungi probably by modulating cell wall-related genes expression; involved in resistance to Plectosphaerella cucumerina. |
Sequence Annotation |
Domain: 21 100 G protein gamma.
Region: 90 96 Regulates lipidation and cell membranesubcellular localization.
Modified residue: 97 97 Cysteine methyl ester.
|
Protein Length |
100 AA. |
Protein Sequence
(Canonical) |
MEAGSSNSSG QLSGRVVDTR GKHRIQAELK RLEQEARFLE EELEQLEKMD NASASCKEFL 60
DSVDSKPDPL LPETTGPVNA TWDQWFEGPK EAKRCGCSIL 100
MEAGSSNSSG QLSGRVVDTR GKHRIQAELK RLEQEARFLE EELEQLEKMD NASASCKEFL 60
DSVDSKPDPL LPETTGPVNA TWDQWFEGPK EAKRCGCSIL 100
|
FASTA
(Canonical) |
>LipidDB-3702-00567|Q93V47
MEAGSSNSSGQLSGRVVDTRGKHRIQAELKRLEQEARFLEEELEQLEKMDNASASCKEFL
DSVDSKPDPLLPETTGPVNATWDQWFEGPKEAKRCGCSIL
MEAGSSNSSGQLSGRVVDTRGKHRIQAELKRLEQEARFLEEELEQLEKMDNASASCKEFL
DSVDSKPDPLLPETTGPVNATWDQWFEGPKEAKRCGCSIL
|
Gene Ontology |
GO:0005834; C:heterotrimeric G-protein complex; IDA:UniProtKB GO:0005886; C:plasma membrane; IDA:UniProtKB GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW GO:0010540; P:basipetal auxin transport; IMP:TAIR GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:InterPro GO:0048527; P:lateral root development; IMP:TAIR GO:0018345; P:protein palmitoylation; IMP:UniProtKB GO:0018342; P:protein prenylation; IMP:UniProtKB GO:0009845; P:seed germination; IMP:TAIR |
Interpro |
InterPro; IPR015898; G-protein_gamma-like_dom |
Pfam |
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SMART |
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PROSITE |
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PRINTS |
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