GPA9_DICDI
ID GPA9_DICDI Reviewed; 342 AA.
AC Q54R41;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Guanine nucleotide-binding protein alpha-9 subunit;
DE Short=G alpha-9;
GN Name=gpaI; Synonyms=gpa9; ORFNames=DDB_G0283419;
OS Dictyostelium discoideum (Slime mold).
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).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=12176329; DOI=10.1016/s0960-9822(02)00953-3;
RA Brzostowski J.A., Johnson C., Kimmel A.R.;
RT "Galpha-mediated inhibition of developmental signal response.";
RL Curr. Biol. 12:1199-1208(2002).
RN [3]
RP FUNCTION.
RX PubMed=15059962; DOI=10.1101/gad.1173404;
RA Brzostowski J.A., Parent C.A., Kimmel A.R.;
RT "A G alpha-dependent pathway that antagonizes multiple chemoattractant
RT responses that regulate directional cell movement.";
RL Genes Dev. 18:805-815(2004).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. G alpha-9 antagonizes broad chemotactic response. It functions
CC rapidly following receptor stimulation to negatively regulate
CC PI3K/PTEN, adenylyl cyclase, and guanylyl cyclase pathways.
CC {ECO:0000269|PubMed:12176329, ECO:0000269|PubMed:15059962}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- DEVELOPMENTAL STAGE: Expressed primarily at the mound stage.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; AAFI02000055; EAL65694.1; -; Genomic_DNA.
DR RefSeq; XP_639050.1; XM_633958.1.
DR AlphaFoldDB; Q54R41; -.
DR SMR; Q54R41; -.
DR STRING; 44689.DDB0230128; -.
DR PaxDb; Q54R41; -.
DR PRIDE; Q54R41; -.
DR EnsemblProtists; EAL65694; EAL65694; DDB_G0283419.
DR GeneID; 8624075; -.
DR KEGG; ddi:DDB_G0283419; -.
DR dictyBase; DDB_G0283419; gpaI.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q54R41; -.
DR OMA; CCVSAED; -.
DR PhylomeDB; Q54R41; -.
DR PRO; PR:Q54R41; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; 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:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:dictyBase.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:dictyBase.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IMP:dictyBase.
DR GO; GO:0051093; P:negative regulation of developmental process; TAS:dictyBase.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:dictyBase.
DR GO; GO:0061123; P:negative regulation of positive chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:dictyBase.
DR GO; GO:0031157; P:regulation of aggregate size involved in 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 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..342
FT /note="Guanine nucleotide-binding protein alpha-9 subunit"
FT /id="PRO_0000312528"
FT DOMAIN 28..342
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 31..44
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 165..173
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 188..197
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 257..264
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 314..319
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 167..173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 192..196
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 261..264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 316
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"
SQ SEQUENCE 342 AA; 39660 MW; B76D35C412F2D8D3 CRC64;
MGCNSSSEAK QSDKIDRTLY DEKKSQEREI KLLLLGSGDS GKSTIAKQMR YIHTKGFSNE
EIATFVEIMH SNVLSSIQIL IRNVPVEQLG SDLKDKANYY SSINPYELPL TPDIGLEIDR
LWKNEAIQKL FSTNRAELNL PEVTAYCLDQ VERISSETYT PTQEDVLRCR QRTTGMKETQ
FNVEDIKFRL IDVGGQKNER RKWMHYFEDV KSIIFCVALG DYDMNLVEDE TINRMEDSLK
LWNDIVNNPF FKNTSFVLFL NKNDIFREKI KKIPLVDYFP DYQGGYNYEK GIEYIRNKFF
SSVPTATTIV AHVTTATDTE NITIVFDAVR RNIIQSILKL HY
