GACQ_DICDI
ID GACQ_DICDI Reviewed; 531 AA.
AC Q54SL6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Rho GTPase-activating protein gacQ;
DE AltName: Full=GTPase activating factor for raC protein Q;
GN Name=gacQ; ORFNames=DDB_G0282395;
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.
RX PubMed=18635356; DOI=10.1016/j.cub.2008.06.068;
RA Kamimura Y., Xiong Y., Iglesias P.A., Hoeller O., Bolourani P.,
RA Devreotes P.N.;
RT "PIP3-independent activation of TorC2 and PKB at the cell's leading edge
RT mediates chemotaxis.";
RL Curr. Biol. 18:1034-1043(2008).
CC -!- FUNCTION: Rho GTPase-activating protein involved in the signal
CC transduction pathway. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; AAFI02000047; EAL66057.1; -; Genomic_DNA.
DR RefSeq; XP_640023.1; XM_634931.1.
DR AlphaFoldDB; Q54SL6; -.
DR SMR; Q54SL6; -.
DR STRING; 44689.DDB0233774; -.
DR PaxDb; Q54SL6; -.
DR EnsemblProtists; EAL66057; EAL66057; DDB_G0282395.
DR GeneID; 8623547; -.
DR KEGG; ddi:DDB_G0282395; -.
DR dictyBase; DDB_G0282395; gacQ.
DR eggNOG; KOG4270; Eukaryota.
DR HOGENOM; CLU_513329_0_0_1; -.
DR InParanoid; Q54SL6; -.
DR OMA; YLMKFLC; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-9013148; CDC42 GTPase cycle.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR Reactome; R-DDI-9013424; RHOV GTPase cycle.
DR PRO; PR:Q54SL6; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; GTPase activation; Reference proteome.
FT CHAIN 1..531
FT /note="Rho GTPase-activating protein gacQ"
FT /id="PRO_0000380215"
FT DOMAIN 67..255
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..51
FT /evidence="ECO:0000255"
FT COMPBIAS 1..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 59040 MW; 992707BC3C4AB14F CRC64;
MKFGKKKEKE NLENIEKDKD RDKEKEIKEK EKKDKKSKDK KKNQEIEKDN NINNNNNNNN
VKKVFGGSLP FLFEEELPTI LVQTIDYLQL FGLQTPGIFR ENGSLASIQS YRSLYDNDKP
VNFPPHEAHV VASLLKAYLR ELKVPLCTFE HYDMFIACES IADEKVKVEL LKKVIAHLPP
FNRKVMKYIF SFLQKVVENS NVNKMTPDAL SIVFLPTILR PQANTDLEIL QFTVEDSKST
KTLMSSILLN YDEIFEDPNL FQPRTRQARA QTDFVSPPSS QNSTSSSSYL SSKNPISPRS
PIGSSPNFTT ASILSALPPP PISPILSSNT TNTTLPPPII TSSIDDNNEP SLSPRIITTT
TTTTPSPQPT TTTTTHRLPP SNPIPPTPTS NSQSQLYPNL PPPSSDPIIK STTTPTLNSQ
SQSQLYPNLP PPLPDKNKCK LLPITPITTN ESNTLQPTTP TSTNIPPLSI PPQIGGNSDS
NPISPTKNQS QLPILPPKPP SLTLPPKPIP KIPTILEYEN NVRQRSNTTM V
