GPA5_DICDI
ID GPA5_DICDI Reviewed; 347 AA.
AC P34043; Q54M32;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Guanine nucleotide-binding protein alpha-5 subunit;
DE Short=G alpha-5;
GN Name=gpaE; ORFNames=DDB_G0286185;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8620848; DOI=10.1242/dev.122.4.1215;
RA Hadwiger J.A., Natarajan K., Firtel R.A.;
RT "Mutations in the Dictyostelium heterotrimeric G protein alpha subunit G
RT alpha5 alter the kinetics of tip morphogenesis.";
RL Development 122:1215-1224(1996).
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 [GENOMIC DNA] OF 205-322.
RX PubMed=1910174; DOI=10.1073/pnas.88.18.8213;
RA Hadwiger J.A., Wilkie T.M., Strathmann M., Firtel R.A.;
RT "Identification of Dictyostelium G alpha genes expressed during
RT multicellular development.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8213-8217(1991).
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. G(q) subfamily.
CC {ECO:0000305}.
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DR EMBL; U20806; AAB04097.1; -; Genomic_DNA.
DR EMBL; AAFI02000085; EAL64268.1; -; Genomic_DNA.
DR PIR; B40990; B40990.
DR RefSeq; XP_637799.1; XM_632707.1.
DR AlphaFoldDB; P34043; -.
DR SMR; P34043; -.
DR STRING; 44689.DDB0191246; -.
DR PaxDb; P34043; -.
DR EnsemblProtists; EAL64268; EAL64268; DDB_G0286185.
DR GeneID; 8625513; -.
DR KEGG; ddi:DDB_G0286185; -.
DR dictyBase; DDB_G0286185; gpaE.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P34043; -.
DR OMA; LWVDRGV; -.
DR PhylomeDB; P34043; -.
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-2485179; Activation of the phototransduction cascade.
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-4086398; Ca2+ pathway.
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 Reactome; R-DDI-9013148; CDC42 GTPase cycle.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR PRO; PR:P34043; -.
DR Proteomes; UP000002195; Chromosome 4.
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 GO; GO:0043326; P:chemotaxis to folate; IMP:dictyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IGI:dictyBase.
DR GO; GO:0031157; P:regulation of aggregate size involved in sorocarp development; IGI:dictyBase.
DR GO; GO:0030587; P:sorocarp development; 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 3: Inferred from homology;
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..347
FT /note="Guanine nucleotide-binding protein alpha-5 subunit"
FT /id="PRO_0000203663"
FT DOMAIN 27..347
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 30..43
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 260..267
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 317..322
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 35..42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 170..176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 195..199
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 264..267
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 319
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 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CONFLICT 248..263
FT /note="IVNSHWFRNTAFIIFF -> LLIVIGLEIQHSLYFL (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> R (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 284..286
FT /note="AYT -> VYP (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="K -> N (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="N -> S (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="I -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 40407 MW; 26A9A347BE103993 CRC64;
MGCILTIEAK KSRDIDYQLR KEEGSKNETK LLLLGPGESG KSTIFKQMKI IQDDGGFSID
ERLEYRYIIY GNCISQMKVL VTAAISQDLK PNNPDNETRF EKFSKISPGG NSWTLEIAED
IKQLWSDDSI QNIYRMKDKF YQLNDSAAYF FDNIGRFANE NYVPTQDDVL RSRVRTTGIQ
EAHFKFINIE FRMLDVGGQR SERRKWIHCF DSVTAVIFCV ALSEYDQTLR EEESQNRMKE
SLMLFDEIVN SHWFRNTAFI IFFNKVDLFR EKIAKIDLGD YFPAYTGGLS FDNSTQFIKK
MFLDLSTGNQ RIFAHFTCAI DTANIQFVFH AVRETLLKNI FNTIINY
