GPA1_SOYBN
ID GPA1_SOYBN Reviewed; 385 AA.
AC P49084;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit;
DE Short=GP-alpha-1;
GN Name=GPA1; Synonyms=GA1;
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Williams;
RX PubMed=7630957; DOI=10.1104/pp.108.3.1315;
RA Kim W.Y., Cheong N.E., Lee D.C., Je D.Y., Bahk J.D., Cho M.J., Lee S.Y.;
RT "Cloning and sequencing analysis of a full-length cDNA encoding a G protein
RT alpha subunit, SGA1, from soybean.";
RL Plant Physiol. 108:1315-1316(1995).
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; L27418; AAA99517.1; -; mRNA.
DR PIR; T07159; T07159.
DR RefSeq; NP_001238184.1; NM_001251255.1.
DR AlphaFoldDB; P49084; -.
DR SMR; P49084; -.
DR STRING; 3847.GLYMA04G05960.1; -.
DR PRIDE; P49084; -.
DR GeneID; 547804; -.
DR KEGG; gmx:547804; -.
DR eggNOG; KOG0082; Eukaryota.
DR InParanoid; P49084; -.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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..385
FT /note="Guanine nucleotide-binding protein alpha-1 subunit"
FT /id="PRO_0000203626"
FT DOMAIN 38..385
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 355..360
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 357
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 385 AA; 44919 MW; 655478036330FFAA CRC64;
MGLVCSRSRR FREAHAEENA QDAEIERRIE LETKAEKHIQ KLLLLGAGES GRSTIFKQIK
LLFQTGFNEA ELKSYIPVVH ANVYQTIKVL QDGSKELAQN DFDSSKYVIS NENQDIGQKL
SEIGGTLVYP RLTKELAQEI ETMWEDAAIQ ETYARGNELQ VPDCAHYFME NLERLSDANY
VPTKEDFLYA RVRTTGVVEI QFSPVGENKR SGEVYRLFDV GGQRNERRKW IHLFEGVTAV
IFCSAISEYD QTLYEDENKN RMMETKELFE WVLRQPCFEK TSFMLFLNKF DIFEKKVLNV
PLNVCEWFKH DYQPVSTEKQ EIEHAYEFVK KKFEELYFQS TAPDCVDRVF KIYQATAPDQ
KLVKKTFKLG DETLRRRNPL EAGLL
