ID   GPA1_LOTJA              Reviewed;         384 AA.
AC   P49082;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit;
DE            Short=GP-alpha-1;
GN   Name=GPA1;
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7972508; DOI=10.1104/pp.105.4.1453;
RA   Poulsen C., Mai X.M., Borg S.;
RT   "A Lotus japonicus cDNA encoding an alpha subunit of a heterotrimeric G-
RT   protein.";
RL   Plant Physiol. 105:1453-1454(1994).
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; X77250; CAA54467.1; -; mRNA.
DR   PIR; S47132; S47132.
DR   AlphaFoldDB; P49082; -.
DR   SMR; P49082; -.
DR   PRIDE; P49082; -.
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_0000203619"
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;  44849 MW;  AD8C6BC8B2D4B0A5 CRC64;
     MGLLCSKNRR YNDADTEENT QTAEIERRIE LETKAEKHIQ KLLLLGAGES GKSTIFKQIK
     LLFQTGFDEA ELKSYQPVIH ANVYQTIKLL HDGAKELAQN DVDFSKYVIS DENKEIGEKL
     SEIGGRLDYP CLTKELALEI ENLWKDAAIQ ETYARGNELQ VPDCTHYFME NLHRLSDANY
     VPTKDDVLYA RVRTTGVVEI QFSPVGENKK SGEVYRLFDV GGQRNERRKW IHLFEGVSAV
     IFCAAISEYD QTLFEDENKN RMMETKELFE WVLKQPCFEK TSFMLFLNKF DIFEKKILKV
     PLNVCEWFKD YQPVSTGKQE IEHAYEFVKK KFEESYFQNT APDRVDRVFK IYRTTALDQK
     VVKKTFKLVD ETLRRRNLFE AGLL