GPA1_SOLLC
ID GPA1_SOLLC Reviewed; 384 AA.
AC P26981;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit;
DE Short=GP-alpha-1;
GN Name=GPA1; Synonyms=GA1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. VF36; TISSUE=Pistil;
RX PubMed=1748292; DOI=10.1016/0378-1119(91)90318-6;
RA Ma H., Yanofsky M.F., Huang H.;
RT "Isolation and sequence analysis of TGA1 cDNAs encoding a tomato G protein
RT alpha subunit.";
RL Gene 107:189-195(1991).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- DOMAIN: The helical domain (69-189) is required for self-activation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; M74419; AAA34167.1; -; mRNA.
DR PIR; JH0514; RGTOOA.
DR RefSeq; NP_001292984.1; NM_001306055.1.
DR AlphaFoldDB; P26981; -.
DR SMR; P26981; -.
DR STRING; 4081.Solyc08g061220.2.1; -.
DR PaxDb; P26981; -.
DR PRIDE; P26981; -.
DR GeneID; 543985; -.
DR KEGG; sly:543985; -.
DR eggNOG; KOG0082; Eukaryota.
DR InParanoid; P26981; -.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P26981; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:EnsemblPlants.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016247; F:channel regulator activity; IEA:EnsemblPlants.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0051020; F:GTPase binding; IEA:EnsemblPlants.
DR GO; GO:0005095; F:GTPase inhibitor activity; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009785; P:blue light signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0008219; P:cell death; IEA:EnsemblPlants.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:EnsemblPlants.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:EnsemblPlants.
DR GO; GO:0090333; P:regulation of stomatal closure; IEA:EnsemblPlants.
DR GO; GO:0009749; P:response to glucose; IEA:EnsemblPlants.
DR GO; GO:0010244; P:response to low fluence blue light stimulus by blue low-fluence system; IEA:EnsemblPlants.
DR GO; GO:0019236; P:response to pheromone; IEA:EnsemblPlants.
DR GO; GO:0009845; P:seed germination; IEA:EnsemblPlants.
DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0010027; P:thylakoid membrane organization; IEA:EnsemblPlants.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:EnsemblPlants.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002976; Plant_Gprotein_alpha.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR PANTHER; PTHR10218:SF333; PTHR10218:SF333; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR01242; GPROTEINAPLT.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..384
FT /note="Guanine nucleotide-binding protein alpha-1 subunit"
FT /id="PRO_0000203621"
FT DOMAIN 38..384
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..54
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 186..194
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 215..224
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 284..291
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 354..359
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 46..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 188..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 219..223
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 288..291
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 44903 MW; 5C95ED74EFC01A0A CRC64;
MGSLCSRNKH YSQADDEENT QTAEIERRIE QETKAEKHIQ KLLLLGAGDS GKSTIFKQIK
LLFQTGFDEE ELKNYIPVIH ANVYQTTKIL HDGSKELAQN ELEASKYLLS AENKEIGEKL
SEIGGRLDYP HLTKDLVQDI EALWKDPAIQ ETLLRGNELQ VPDCAHYFME NLERFSDVHY
IPTKEDVLFA RIRTTGVVEI QFSPVGENKK SGEVYRLFDV GGQRNERRKW IHLFEGVTAV
IFCAAISEYD QTLFEDERKN RMMETKELFE WVLKQPCFEK TSFMLFLNKF DIFEQKVPKV
PLNACEWFKD YQSVSTGKQE IEHAYEFVKK KFEESYFQCT APDRVDRVFK IYRTTALDQK
LVKKTFKLVD ETLRRRNLFE AGLL
