GPA2_DICDI
ID GPA2_DICDI Reviewed; 357 AA.
AC P16051; Q551U8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Guanine nucleotide-binding protein alpha-2 subunit;
DE Short=G alpha-2;
GN Name=gpaB; ORFNames=DDB_G0276267;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE OF 4-33, FUNCTION, AND INDUCTION.
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).
RN [5]
RP PHOSPHORYLATION AT SER-113.
RX PubMed=8063709; DOI=10.1016/s0021-9258(17)31910-5;
RA Chen M.Y., Devreotes P.N., Gundersen R.E.;
RT "Serine 113 is the site of receptor-mediated phosphorylation of the
RT Dictyostelium G protein alpha-subunit G alpha 2.";
RL J. Biol. Chem. 269:20925-20930(1994).
RN [6]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=10404398;
RX DOI=10.1002/(sici)1097-4644(19990801)74:2<301::aid-jcb14>3.0.co;2-9;
RA Root P.A., Prince A., Gundersen R.E.;
RT "Aggregation of Dictyostelium discoideum is dependent on myristoylation and
RT membrane localization of the G protein alpha-subunit, G alpha 2.";
RL J. Cell. Biochem. 74:301-311(1999).
RN [7]
RP INTERACTION WITH GFLB, AND FUNCTION.
RX PubMed=27237792; DOI=10.1016/j.devcel.2016.05.001;
RA Liu Y., Lacal J., Veltman D.M., Fusetti F., van Haastert P.J., Firtel R.A.,
RA Kortholt A.;
RT "A Galpha-Stimulated RapGEF Is a Receptor-Proximal Regulator of
RT Dictyostelium Chemotaxis.";
RL Dev. Cell 37:458-472(2016).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. G alpha-2 is required for the early aggregation process and
CC most of the known cAMP receptor-mediated responses (PubMed:2539262).
CC Interacts with downstream effector gflB, a Rap guanine nucleotide
CC exchange factor, to regulate the balance between Ras and Rap signaling
CC at the leading edge of chemotaxing cells (PubMed:27237792).
CC {ECO:0000269|PubMed:2539262, ECO:0000269|PubMed:27237792}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site (Probable).
CC Interacts with the RAP guanine nucleotide exchange factor glfB
CC (PubMed:27237792). {ECO:0000269|PubMed:27237792, ECO:0000305}.
CC -!- INDUCTION: Expression is induced by cAMP pulses and during aggregation.
CC {ECO:0000269|PubMed:2539262}.
CC -!- PTM: Ser-113 is transiently phosphorylated following stimulation with
CC extracellular cAMP. {ECO:0000269|PubMed:8063709}.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; M25061; AAA33208.1; -; mRNA.
DR EMBL; AAFI02000014; EAL69280.1; -; Genomic_DNA.
DR PIR; B32384; B32384.
DR PIR; B32945; B32945.
DR RefSeq; XP_643229.1; XM_638137.1.
DR AlphaFoldDB; P16051; -.
DR SMR; P16051; -.
DR STRING; 44689.DDB0191327; -.
DR iPTMnet; P16051; -.
DR SwissPalm; P16051; -.
DR PaxDb; P16051; -.
DR PRIDE; P16051; -.
DR EnsemblProtists; EAL69280; EAL69280; DDB_G0276267.
DR GeneID; 8620433; -.
DR KEGG; ddi:DDB_G0276267; -.
DR dictyBase; DDB_G0276267; gpaB.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P16051; -.
DR OMA; TMGCRQS; -.
DR PhylomeDB; P16051; -.
DR PRO; PR:P16051; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0003925; F:G protein activity; IMP:dictyBase.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:dictyBase.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IC:dictyBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030041; P:actin filament polymerization; IMP:dictyBase.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:dictyBase.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:1905099; P:positive regulation of guanyl-nucleotide exchange factor activity; IDA:dictyBase.
DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IMP:dictyBase.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; IMP:dictyBase.
DR GO; GO:0046825; P:regulation of protein export from nucleus; IMP:dictyBase.
DR GO; GO:0046578; P:regulation of Ras protein 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; IPR002975; Fungi_Gprotein_alpha.
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 PRINTS; PR01241; GPROTEINAFNG.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
KW Transducer.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..357
FT /note="Guanine nucleotide-binding protein alpha-2 subunit"
FT /id="PRO_0000203661"
FT DOMAIN 30..356
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 33..46
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 177..185
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 200..209
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 268..275
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 326..331
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 38..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 179..185
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 204..208
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 272..275
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8063709"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:10404398"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 40841 MW; 063E571175212CF4 CRC64;
MGICASSMEG EKTNTDINLS IEKERKKKHN EVKLLLLGAG ESGKSTISKQ MKIIHQSGYS
NEERKEFKPI ITRNILDNMR VLLDGMGRLG MTIDPSNSDA AVMIKELTSL QASIVTDCWG
ELNEDQGKKI KALWTDPGVK QAMRRANEFS TLPDSAPYFF DSIDRMTSPV YIPTDQDILH
TRVMTRGVHE TNFEIGKIKF RLVDVGGQRS ERKKWLSCFD DVTAVVFCVA LSEYDLLLYE
DNSTNRMLES LRVFSDVCNS WFVNTPIILF LNKSDLFREK IKHVDLSETF PEYKGGRDYE
RASNYIKERF WQINKTEQKA IYSHITCATD TNNIRVVFEA VKDIIFTQCV MKAGLYS
