GPA2_SOYBN
ID GPA2_SOYBN Reviewed; 385 AA.
AC P93163;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Guanine nucleotide-binding protein alpha-2 subunit;
DE Short=GP-alpha-2;
GN Name=GPA2; Synonyms=GA2;
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. Corsoy;
RX PubMed=9002626; DOI=10.1007/bf00041411;
RA Gotor C., Lam E., Cejudo F.J., Romero L.C.;
RT "Isolation and analysis of the soybean SGA2 gene (cDNA), encoding a new
RT member of the plant G-protein family of signal transducers.";
RL Plant Mol. Biol. 32:1227-1234(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 (70-190) is required for self-activation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; X95582; CAA64834.1; -; mRNA.
DR RefSeq; NP_001236873.1; NM_001249944.1.
DR AlphaFoldDB; P93163; -.
DR SMR; P93163; -.
DR STRING; 3847.GLYMA17G34450.1; -.
DR PRIDE; P93163; -.
DR GeneID; 547977; -.
DR KEGG; gmx:547977; -.
DR eggNOG; KOG0082; Eukaryota.
DR InParanoid; P93163; -.
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-2 subunit"
FT /id="PRO_0000203627"
FT DOMAIN 39..385
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 42..55
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 187..195
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 216..225
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 285..292
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 47..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 189..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 220..224
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 289..292
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; 45096 MW; 7721B1E307067075 CRC64;
MGLLCSRNRR YNDADAEENA QTAEIERRIE VRNERAEKHI QKLLLLGAGE SGKSTIFKQI
KLLFQTGFDE AELKSYLPVI HANVYQTIKL LHDGSKEFAQ NDVDSSKYVI SNENKEIGEK
LLEIGGRLDY PYLSKELAQE IENLWKDPAI QETYARGSEL QIPDCTDYFM ENLQRLSDAN
YVPTKEDVLY ARVRTTGVVE IQFSPVGENK KSDEVYRLFD VGGQRNERRK WIHLFEGVSA
VIFCAAISEY DQTLFEDENR NRMMETKELF EWILKQPCFE KTSFMLFLNK FDIFEKKILK
VPLNVCEWFK DYQPVSTGKQ EIEHAYEFVK KKFEESYFQS TAPDRVDRVF KIYRTTALDQ
KVVKKTFKLV DETLRRRNLL EAGLL
