ID GPA10_DICDI Reviewed; 349 AA.
AC Q55EP5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 107.
DE RecName: Full=Guanine nucleotide-binding protein-like alpha-10 subunit;
GN Name=gpaJ; Synonyms=gpa10; ORFNames=DDB_G0268802;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
CC -!- CAUTION: Although this protein belongs to the G-alpha family, its
CC Walker A GTP-binding motif is defective and therefore both its GTP-
CC binding activity and function are dubious. {ECO:0000305}.
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DR EMBL; AAFI02000004; EAL72990.1; -; Genomic_DNA.
DR RefSeq; XP_646975.1; XM_641883.1.
DR AlphaFoldDB; Q55EP5; -.
DR SMR; Q55EP5; -.
DR STRING; 44689.Q55EP5; -.
DR PaxDb; 44689-DDB0230129; -.
DR EnsemblProtists; EAL72990; EAL72990; DDB_G0268802.
DR GeneID; 8616667; -.
DR KEGG; ddi:DDB_G0268802; -.
DR dictyBase; DDB_G0268802; gpaJ.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q55EP5; -.
DR PhylomeDB; Q55EP5; -.
DR Reactome; R-DDI-112043; PLC beta mediated events.
DR Reactome; R-DDI-170660; Adenylate cyclase activating pathway.
DR Reactome; R-DDI-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-DDI-202040; G-protein activation.
DR Reactome; R-DDI-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-DDI-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-DDI-416476; G alpha (q) signalling events.
DR Reactome; R-DDI-416482; G alpha (12/13) signalling events.
DR Reactome; R-DDI-418594; G alpha (i) signalling events.
DR Reactome; R-DDI-418597; G alpha (z) signalling events.
DR Reactome; R-DDI-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR PRO; PR:Q55EP5; -.
DR Proteomes; UP000002195; Chromosome 1.
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: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; 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 PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10218:SF324; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-6 SUBUNIT-RELATED; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
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 GTP-binding; Nucleotide-binding; Reference proteome; Transducer.
FT CHAIN 1..349
FT /note="Guanine nucleotide-binding protein-like alpha-10
FT subunit"
FT /id="PRO_0000327590"
FT DOMAIN 33..349
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 36..49
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 168..176
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 191..200
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 262..269
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 320..325
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 195..199
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 266..269
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 349 AA; 40929 MW; AE0AAD81ED9E9203 CRC64;
MSFLCSENSY QQQSKISIDI DKSLKNHKLK LEEEIRVLIY GQKKVGVTTL FKTFLLMGES
QITPEELMDN RNNVYKTIIN QLKKFIIISN NSKIELENNN NIQMSNLILE LDSENFLWNK
EIGETCLKLW NDSGIQKIFQ SQFSEFFGYF FKHLQRISDE NYTPTPQDLN FIKLTQNGII
EGKFTFERCL IKMIEMGIQT STLKKWINCF SEVQAIIYVI DLSVYDIVES EDCSKSINKL
EKSLNGFKEI IESKYLHGCG VIVFFNKKDI FREKLKTVPF KTYDKDYIGE NDFESTTNFI
KNKLLDYYSN PNKNVYFLIN EESEVDICRS TFNILKDIVL NITYNSVKN
//
