ID A0A1R3IV22_9ROSI Unreviewed; 380 AA.
AC A0A1R3IV22;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Guanine nucleotide-binding protein alpha subunit {ECO:0000256|RuleBase:RU368109};
DE Short=GP-alpha {ECO:0000256|RuleBase:RU368109};
GN ORFNames=COLO4_21154 {ECO:0000313|EMBL:OMO86439.1};
OS Corchorus olitorius.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=93759 {ECO:0000313|EMBL:OMO86439.1, ECO:0000313|Proteomes:UP000187203};
RN [1] {ECO:0000313|Proteomes:UP000187203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA Shommy N.S.;
RT "Corchorus olitorius genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO86439.1}.
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DR EMBL; AWUE01017570; OMO86439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3IV22; -.
DR STRING; 93759.A0A1R3IV22; -.
DR OrthoDB; 2897309at2759; -.
DR Proteomes; UP000187203; Unassembled WGS sequence.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000187203};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU368109}.
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-2"
SQ SEQUENCE 380 AA; 44588 MW; 5C9F61E553FACB50 CRC64;
MLCTVLENMG LLCSKNHHYT EADSEENAQA AEIERRIEQE TKAEKHIQKL LLLGIKLLFQ
TGFDEAELKS YISVIHANIY QTIKILYDGS KEFAQNDEDS SKYILSSENK IIGEKLSEIG
SRLDYPRLNK ELAHEIETLW KDSAIQETYA RGNELQVPDC TNYFMENLQR LSDANYIPTK
EDVLYARVRT TGVVEIQFSP VGENKKSGEV YRLFDVGGQR NERRKWIHLF EGVTAVIFCA
AISEYDQTLF EDEQKNRMME TRELFDWVLK QPCFEKTSFM LFLNKFDIFE KKVLKVPLNV
CEWFKDYQPV STGKQEIEHA YEFVKKKFEE LYFQSTAPDR VDRVFKIYRT TALDQKLVKK
TFKLVDETLR RRNLFEAGLL
//
