ID   GPA1_SOLTU              Reviewed;         384 AA.
AC   P93564;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit;
DE            Short=GP-alpha-1;
GN   Name=GPA1;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RA   Provart N.J., Ma H., Willmitzer L., Mueller-Roeber B.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
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; X87836; CAA61105.1; -; mRNA.
DR   AlphaFoldDB; P93564; -.
DR   SMR; P93564; -.
DR   STRING; 4113.PGSC0003DMT400033822; -.
DR   EnsemblPlants; RHC08H1G1124.2.1; RHC08H1G1124.2.1; RHC08H1G1124.2.
DR   Gramene; RHC08H1G1124.2.1; RHC08H1G1124.2.1; RHC08H1G1124.2.
DR   eggNOG; KOG0082; Eukaryota.
DR   InParanoid; P93564; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P93564; baseline.
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:0000250"
FT   CHAIN           2..384
FT                   /note="Guanine nucleotide-binding protein alpha-1 subunit"
FT                   /id="PRO_0000203625"
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;  44922 MW;  101AAD19E546DAD9 CRC64;
     MGSLCSRNKH YSQADDEENT QTAEIERRIE QETKADKHIQ KLLLLGAGDS GKSTIFKQIK
     LLFQTGFDEA ELKNYIPVIH ANVYQTIKIL HDGSKELAQN ELEASKYLLS AENKEIGEKL
     SEIGGRLDYP RLTKDLVQDI EALWKDPAIQ ETLLRGNELQ VPDCAHYFME NLERFSDIHY
     IPTKEDVLFA RIRTTGVVEI QFSPVGENKK SGEVYRLFDV GGQRNERRKW IHLFEGVTAV
     IFCAAISEYD QTLFEDERKN RMMETKELFE WVLKQPCFEK TSFMLFLNKF DIFEQKVLKV
     PLNTCEWFKD YQSVSTGKQE IEHAYEFVKK KFEESYFQCT APDRVDRVFK IYRTTALDQK
     LVKKTFKLVD ETLRRRNLFE AGLL