Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-00406
Entry Name
UniProt Accession
Theoretical PI
5.96
Molecular Weight
44545.91
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein alpha-1 subunit
Protein Synonyms/Alias
GP-alpha-1;
Gene Name
GPA1
Gene Synonyms/Alias
At2g26300; T1D16.6;
Created Date
01-NOV-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGLLCSRSR
[2]
N-Myristoylation
5
Canonical
***MGLLCSRSRHHT
[1]
S-Palmitoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] Predicted from GPS-Lipid
[2] Boisson B, Giglione C, Meinnel T. Unexpected protein families including celldefense components feature in the N-myristoylome of a higher eukaryote. J BiolChem. 2003 Oct 31;278(44):43418-29. Epub 2003 Aug 11.[PMID:12912986]
Functional Description
Exhibits a fast rate of basal nucleotide exchange. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Together with GCR1, may regulate the cell cycle via a signaling cascade that uses phosphatidylinositol-specific phospholipase C (PI-PLC) as an effector and inositol 1,4,5- trisphosphate(IP(3)) as a second messenger. Promotes abscisic acid (ABA) responses in guard cells. But, together with GCR1 and GB1, acts as a negative regulator of ABA during seed germination and early seedling development. Involved in the blue light (BL) signaling. Together with GCR1 and ADT3, required for BL-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated seedlings. Modulates root architecture (e.g. lateral root formation). Negatively regulated by RGS1.
Sequence Annotation
Nucleotide-binding: 45 52 GTP.
Nucleotide-binding: 187 193 GTP.
Nucleotide-binding: 218 222 GTP.
Nucleotide-binding: 287 290 GTP.
Metal binding site: 52 52 Magnesium.
Metal binding site: 193 193 Magnesium.
Binding site: 355 355 GTP; via amide nitrogen.
Protein Length
383 AA.
Protein Sequence
(Canonical)
MGLLCSRSRH HTEDTDENTQ AAEIERRIEQ EAKAEKHIRK LLLLGAGESG KSTIFKQIKL  60
LFQTGFDEGE LKSYVPVIHA NVYQTIKLLH DGTKEFAQNE TDSAKYMLSS ESIAIGEKLS  120
EIGGRLDYPR LTKDIAEGIE TLWKDPAIQE TCARGNELQV PDCTKYLMEN LKRLSDINYI  180
PTKEDVLYAR VRTTGVVEIQ FSPVGENKKS GEVYRLFDVG GQRNERRKWI HLFEGVTAVI  240
FCAAISEYDQ TLFEDEQKNR MMETKELFDW VLKQPCFEKT SFMLFLNKFD IFEKKVLDVP  300
LNVCEWFRDY QPVSSGKQEI EHAYEFVKKK FEELYYQNTA PDRVDRVFKI YRTTALDQKL  360
VKKTFKLVDE TLRRRNLLEA GLL                                          383
MGLLCSRSRH HTEDTDENTQ AAEIERRIEQ EAKAEKHIRK LLLLGAGESG KSTIFKQIKL  60
LFQTGFDEGE LKSYVPVIHA NVYQTIKLLH DGTKEFAQNE TDSAKYMLSS ESIAIGEKLS  120
EIGGRLDYPR LTKDIAEGIE TLWKDPAIQE TCARGNELQV PDCTKYLMEN LKRLSDINYI  180
PTKEDVLYAR VRTTGVVEIQ FSPVGENKKS GEVYRLFDVG GQRNERRKWI HLFEGVTAVI  240
FCAAISEYDQ TLFEDEQKNR MMETKELFDW VLKQPCFEKT SFMLFLNKFD IFEKKVLDVP  300
LNVCEWFRDY QPVSSGKQEI EHAYEFVKKK FEELYYQNTA PDRVDRVFKI YRTTALDQKL  360
VKKTFKLVDE TLRRRNLLEA GLL                                          383
FASTA
(Canonical)
>LipidDB-3702-00406|P18064
MGLLCSRSRHHTEDTDENTQAAEIERRIEQEAKAEKHIRKLLLLGAGESGKSTIFKQIKL
LFQTGFDEGELKSYVPVIHANVYQTIKLLHDGTKEFAQNETDSAKYMLSSESIAIGEKLS
EIGGRLDYPRLTKDIAEGIETLWKDPAIQETCARGNELQVPDCTKYLMENLKRLSDINYI
PTKEDVLYARVRTTGVVEIQFSPVGENKKSGEVYRLFDVGGQRNERRKWIHLFEGVTAVI
FCAAISEYDQTLFEDEQKNRMMETKELFDWVLKQPCFEKTSFMLFLNKFDIFEKKVLDVP
LNVCEWFRDYQPVSSGKQEIEHAYEFVKKKFEELYYQNTAPDRVDRVFKIYRTTALDQKL
VKKTFKLVDETLRRRNLLEAGLL
MGLLCSRSRHHTEDTDENTQAAEIERRIEQEAKAEKHIRKLLLLGAGESGKSTIFKQIKL
LFQTGFDEGELKSYVPVIHANVYQTIKLLHDGTKEFAQNETDSAKYMLSSESIAIGEKLS
EIGGRLDYPRLTKDIAEGIETLWKDPAIQETCARGNELQVPDCTKYLMENLKRLSDINYI
PTKEDVLYARVRTTGVVEIQFSPVGENKKSGEVYRLFDVGGQRNERRKWIHLFEGVTAVI
FCAAISEYDQTLFEDEQKNRMMETKELFDWVLKQPCFEKTSFMLFLNKFDIFEKKVLDVP
LNVCEWFRDYQPVSSGKQEIEHAYEFVKKKFEELYYQNTAPDRVDRVFKIYRTTALDQKL
VKKTFKLVDETLRRRNLLEAGLL
Gene Ontology
GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR
GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:RefGenome
GO:0005834; C:heterotrimeric G-protein complex; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0009506; C:plasmodesma; IDA:TAIR
GO:0016247; F:channel regulator activity; IMP:TAIR
GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome
GO:0001664; F:G-protein coupled receptor binding; IBA:RefGenome
GO:0005525; F:GTP binding; IDA:UniProtKB
GO:0003924; F:GTPase activity; IDA:TAIR
GO:0051020; F:GTPase binding; IPI:TAIR
GO:0005095; F:GTPase inhibitor activity; IDA:TAIR
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004871; F:signal transducer activity; IBA:RefGenome
GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB
GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:RefGenome
GO:0009785; P:blue light signaling pathway; IMP:UniProtKB
GO:0008219; P:cell death; IMP:TAIR
GO:0071215; P:cellular response to abscisic acid stimulus; IEP:UniProtKB
GO:0001789; P:G-protein coupled receptor signaling pathway, coupled to S1P second messenger; IMP:TAIR
GO:0009740; P:gibberellic acid mediated signaling pathway; IMP:TAIR
GO:0009094; P:L-phenylalanine biosynthetic process; IMP:TAIR
GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB
GO:0043086; P:negative regulation of catalytic activity; IDA:GOC
GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR
GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR
GO:0042127; P:regulation of cell proliferation; IMP:TAIR
GO:0010119; P:regulation of stomatal movement; IMP:TAIR
GO:0009749; P:response to glucose; IGI:TAIR
GO:0010244; P:response to low fluence blue light stimulus by blue low-fluence system; IMP:TAIR
GO:0009845; P:seed germination; IEP:UniProtKB
GO:0010027; P:thylakoid membrane organization; IMP:TAIR
GO:0006571; P:tyrosine biosynthetic process; IMP:TAIR
Interpro
InterPro; IPR001019; Gprotein_alpha_su
InterPro; IPR011025; GproteinA_insert
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR002976; Plant_Gprotein_alpha
Pfam
Pfam; PF00503; G-alpha;
SMART
SMART; SM00275; G_alpha;
PROSITE
PRINTS
PRINTS; PR00318; GPROTEINA;
PRINTS; PR01242; GPROTEINAPLT;