ID B1PS51_SCODU Unreviewed; 383 AA.
AC B1PS51;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Guanine nucleotide-binding protein alpha subunit {ECO:0000256|RuleBase:RU368109};
DE Short=GP-alpha {ECO:0000256|RuleBase:RU368109};
OS Scoparia dulcis (Sweet broom) (Capraria dulcis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plantaginaceae; Gratioleae; Scoparia.
OX NCBI_TaxID=107240 {ECO:0000313|EMBL:ACA62792.1};
RN [1] {ECO:0000313|EMBL:ACA62792.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18981590; DOI=10.1248/bpb.31.2150;
RA Shite M., Yamamura Y., Hayashi T., Kurosaki F.;
RT "Cloning and characterization of Sdga gene encoding alpha-subunit of
RT heterotrimeric guanosine 5'-triphosphate-binding protein complex in
RT Scoparia dulcis.";
RL Biol. Pharm. Bull. 31:2150-2153(2008).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. {ECO:0000256|RuleBase:RU368109}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC {ECO:0000256|RuleBase:RU368109}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU368109}.
CC -!- DOMAIN: The helical domain is required for self-activation.
CC {ECO:0000256|RuleBase:RU368109}.
CC -!- SIMILARITY: Belongs to the G-alpha family.
CC {ECO:0000256|ARBA:ARBA00005804, ECO:0000256|RuleBase:RU368109}.
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DR EMBL; EU489474; ACA62792.1; -; mRNA.
DR AlphaFoldDB; B1PS51; -.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:UniProtKB-UniRule.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:UniProtKB-UniRule.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10218:SF302; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-8 SUBUNIT-RELATED; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR01242; GPROTEINAPLT.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 2: Evidence at transcript level;
KW Cell membrane {ECO:0000256|RuleBase:RU368109};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU368109};
KW Lipoprotein {ECO:0000256|RuleBase:RU368109};
KW Magnesium {ECO:0000256|PIRSR:PIRSR602976-2, ECO:0000256|RuleBase:RU368109};
KW Membrane {ECO:0000256|RuleBase:RU368109};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602976-2,
KW ECO:0000256|RuleBase:RU368109}; Myristate {ECO:0000256|RuleBase:RU368109};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU368109};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|RuleBase:RU368109};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU368109}.
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-2"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-2"
SQ SEQUENCE 383 AA; 44808 MW; 5DBE2F87E9ADF849 CRC64;
MGLLCSRQRH SQAYSEENEQ TAEIERRIEQ ETKAEKHIQK LLLLGAGDSG KSTIFKQIKL
LFQSGFDEAE LKGYIPVIHA NVYQTIKILH DGSKELAQTD ADSSKFVISD QNKEIGARFS
EIGSMLEYPR LTRDLARDIE TLWRDSAIQE TYSRGNELQV PDCAHYFMEN LQRFSDEDYV
PTKEDVLYAR VRTTGVVEIQ FSPVGENKKS GEVYRLFDVG GQRNERRKWI HLFDGVTAVI
FCAAISEYDQ TLFEDDNRNR MMETKELFEW VLKQPCFEKT SFMLFLNKFD LFEKKVLNVP
LNVCSWFKEY QPVSMGKQEV EHAYEFVKKK FEELYFQSTN PDCVDRVFKI YRTTALDQKL
VKKTFKLVDE TLRRRNLFEA GLL
//
