GPA1_DICDI
ID GPA1_DICDI Reviewed; 356 AA.
AC P16894; Q54R78;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit;
DE Short=G alpha-1;
GN Name=gpaA; ORFNames=DDB_G0283349;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2500658; DOI=10.1073/pnas.86.13.4892;
RA Pupillo M., Kumagai A., Pitt G.S., Firtel R.A., Devreotes P.N.;
RT "Multiple alpha subunits of guanine nucleotide-binding proteins in
RT Dictyostelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4892-4896(1989).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-35.
RX PubMed=2539262; DOI=10.1016/0092-8674(89)90964-1;
RA Kumagai A., Pupillo M., Gundersen R., Miake-Lye R., Devreotes P.N.,
RA Firtel R.A.;
RT "Regulation and function of G alpha protein subunits in Dictyostelium.";
RL Cell 57:265-275(1989).
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 -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; M25060; AAA33207.1; -; mRNA.
DR EMBL; AAFI02000054; EAL65751.1; -; Genomic_DNA.
DR PIR; A32384; A32384.
DR PIR; A32945; A32945.
DR RefSeq; XP_639105.1; XM_634013.1.
DR AlphaFoldDB; P16894; -.
DR SMR; P16894; -.
DR STRING; 44689.DDB0191255; -.
DR PaxDb; P16894; -.
DR PRIDE; P16894; -.
DR EnsemblProtists; EAL65751; EAL65751; DDB_G0283349.
DR GeneID; 8624038; -.
DR KEGG; ddi:DDB_G0283349; -.
DR dictyBase; DDB_G0283349; gpaA.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P16894; -.
DR OMA; QVIWADA; -.
DR PhylomeDB; P16894; -.
DR PRO; PR:P16894; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0003925; F:G protein activity; IDA:dictyBase.
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 GO; GO:0030154; P:cell differentiation; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:1900275; P:negative regulation of phospholipase C activity; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IMP:dictyBase.
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 PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
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:0000255"
FT CHAIN 2..356
FT /note="Guanine nucleotide-binding protein alpha-1 subunit"
FT /id="PRO_0000203660"
FT DOMAIN 35..355
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 38..51
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 175..183
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 198..207
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 267..274
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 325..330
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 43..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 177..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 202..206
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 271..274
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 356 AA; 40188 MW; D3F9C3BE399634B0 CRC64;
MGNICGKPEL GSPEEIKANQ HINSLLKQAR SKLEGEIKLL LLGAGESGKS TIAKQMKIIH
LNGFNDEEKS SYKTIIYNNT VGSMRVLVNA AEELKIGISE NNKEAASRIS NDLGDHFNGV
LTAELAQDIK ALWADPGIQN TFQRSSEFQL NDSAAYYFDS IDRISQPLYL PSENDVLRSR
TKTTGIIETV FEIQNSTFRM VDVGGQRSER KKWMHCFQEV TAVIFCVALS EYDLKLYEDD
TTNRMQESLK LFKEICNTKW FANTAMILFL NKRDIFSEKI TKTPITVCFK EYDGPQTYEG
CSEFIKQQFI NQNENPKKSI YPHLTCATDT NNILVVFNAV KDIVLNLTLG EAGMIL
