ID   GPA1_LUPLU              Reviewed;         384 AA.
AC   Q40224;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit;
DE            Short=GP-alpha-1;
GN   Name=GPA1;
OS   Lupinus luteus (European yellow lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3873;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seedling;
RA   Kutsnetsov V.V., Oelmueller R.;
RT   "Isolation of cDNAs encoding the subunit alpha of heterotrimeric G proteins
RT   from Lupinus luteus.";
RL   (er) Plant Gene Register PGR96-113(1996).
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; X99485; CAA67845.1; -; mRNA.
DR   AlphaFoldDB; Q40224; -.
DR   SMR; Q40224; -.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:InterPro.
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; 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_0000203620"
FT   DOMAIN          38..384
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
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;  44678 MW;  17B46936731C0663 CRC64;
     MGLLCSRNRR YNDADAEENA QAAEIERRIE LETKAEKHIQ KLLLLGAGES GKSTIFKQIK
     LLFQTGFDEA ELKSYLPVIH ANVFQTIKLL HDGSKELAQN DVDSSKYVIS DENKDIGEKL
     SEIGSKLDYP YLTTELAKEI ETLWEDAAIQ ETYARGNELQ VPGCAHYFME NLQRLSDANY
     VPTKEDVLYA RVRTTGVVEI QFSPVGENKR SGEVYRLFDV GGQRNERRKW IHLFEGVSAV
     IFCAAISEYD QTLFEDENKN RMTETKELFE WILKQPCFEK TSFMLFLNKF DIFEKKILKV
     PLNVCEWFKD YQPVSTGKQE IEHAYEFVKK KFEELYFQST APERVDRVFK VYRTTALDQK
     LIKKTFKLVD ESLRRRNLFE AGLL