RGAA_DICDI
ID RGAA_DICDI Reviewed; 822 AA.
AC Q54K32; O15815; P90531;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ras GTPase-activating-like protein rgaA;
DE Short=DGAP1;
DE AltName: Full=Developmental gene 1029 protein;
GN Name=rgaA; Synonyms=DG1029, rasGAP1; ORFNames=DDB_G0287585;
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], FUNCTION, DISRUPTION PHENOTYPE,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=AX3;
RX PubMed=8830653; DOI=10.1016/0014-5793(96)00963-5;
RA Faix J., Dittrich W.;
RT "DGAP1, a homologue of rasGTPase activating proteins that controls growth,
RT cytokinesis, and development in Dictyostelium discoideum.";
RL FEBS Lett. 394:251-257(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX3;
RX PubMed=9056774; DOI=10.1242/dev.124.5.983;
RA Lee S., Escalante R., Firtel R.A.;
RT "A Ras GAP is essential for cytokinesis and spatial patterning in
RT Dictyostelium.";
RL Development 124:983-996(1997).
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 INTERACTION WITH RAC1A AND RACE, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9739079; DOI=10.1242/jcs.111.20.3059;
RA Faix J., Clougherty C., Konzok A., Mintert U., Murphy J., Albrecht R.,
RA Muhlbauer B., Kuhlmann J.;
RT "The IQGAP-related protein DGAP1 interacts with Rac and is involved in the
RT modulation of the F-actin cytoskeleton and control of cell motility.";
RL J. Cell Sci. 111:3059-3071(1998).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RAC1A; RAC1B AND
RP RAC1C.
RX PubMed=10825297; DOI=10.1242/jcs.113.12.2253;
RA Dumontier M., Hoecht P., Mintert U., Faix J.;
RT "Rac1 GTPases control filopodia formation, cell motility, endocytosis,
RT cytokinesis and development in Dictyostelium.";
RL J. Cell Sci. 113:2253-2265(2000).
RN [6]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH RAC1A AND CTXA.
RX PubMed=11447112; DOI=10.1093/emboj/20.14.3705;
RA Faix J., Weber I., Mintert U., Koehler J., Lottspeich F., Marriott G.;
RT "Recruitment of cortexillin into the cleavage furrow is controlled by Rac1
RT and IQGAP-related proteins.";
RL EMBO J. 20:3705-3715(2001).
CC -!- FUNCTION: Part of signaling pathway that is required for completion of
CC cytokinesis. gapA and rgaA control cortexillin localization to the
CC cleavage furrow and hence may be involved in cleavage of the midbody in
CC the final stage of cytokinesis by regulating the actin cytoskeleton.
CC Forms a complex by linking activated rac1A to ctxA. Assembly of this
CC complex is necessary for the recruitment of cortexillin to the midzone
CC of a dividing cell. Overexpression leads to the suppression of the
CC formation of cellular projections containing F-actin and to a defect in
CC cytokinesis. {ECO:0000269|PubMed:10825297, ECO:0000269|PubMed:11447112,
CC ECO:0000269|PubMed:8830653, ECO:0000269|PubMed:9739079}.
CC -!- SUBUNIT: Heterotetramer. Quaternary complex with activated rac1A, ctxA
CC and ctxB. Interacts directly with rac1A and ctxA. Preferentially
CC interacts with activated forms of rac1A, rac1B and rac1C. Interacts
CC with racE. {ECO:0000269|PubMed:10825297, ECO:0000269|PubMed:11447112,
CC ECO:0000269|PubMed:9739079}.
CC -!- INTERACTION:
CC Q54K32; Q54HG2: ctxA; NbExp=2; IntAct=EBI-1808670, EBI-1810875;
CC Q54K32; P34144: rac1A; NbExp=4; IntAct=EBI-1808670, EBI-1808643;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cleavage furrow.
CC Note=Enriched in the cortex of interphase cells and translocated to the
CC cleavage furrow during cytokinesis.
CC -!- DISRUPTION PHENOTYPE: No change in cytokinesis as gapA can functionally
CC replace this protein. Null cells project numerous filopodia, show
CC increased cell motility during growth and form multi-tipped aggregates
CC during development and show elevated levels of F-actin that is
CC organized in large leading edges, membrane ruffles or numerous large
CC filopods. RgaA and gapA double mutant prevents quaternary complex
CC formation (activated rac1A, ctxA, ctxB and either rgaA or gapA) and
CC localization of the cortexillins to the cleavage furrow; interferes
CC with cytokinesis to a similar extent as the simultaneous elimination of
CC ctxA and ctxB, shows extremely large, flat and multinucleate cells and
CC has increased cell motility and abnormal development.
CC {ECO:0000269|PubMed:10825297, ECO:0000269|PubMed:11447112,
CC ECO:0000269|PubMed:8830653, ECO:0000269|PubMed:9739079}.
CC -!- MISCELLANEOUS: rgaA lacks rasGAP activity in vitro. rgaA expression is
CC inversely correlated with the speed of cell motility.
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DR EMBL; L75794; AAB62276.1; -; Genomic_DNA.
DR EMBL; U81156; AAB39262.1; -; Genomic_DNA.
DR EMBL; AAFI02000103; EAL63601.1; -; Genomic_DNA.
DR RefSeq; XP_637132.1; XM_632040.1.
DR AlphaFoldDB; Q54K32; -.
DR SMR; Q54K32; -.
DR IntAct; Q54K32; 2.
DR STRING; 44689.DDB0191437; -.
DR PaxDb; Q54K32; -.
DR PRIDE; Q54K32; -.
DR EnsemblProtists; EAL63601; EAL63601; DDB_G0287585.
DR GeneID; 8626227; -.
DR KEGG; ddi:DDB_G0287585; -.
DR dictyBase; DDB_G0287585; rgaA.
DR eggNOG; KOG2128; Eukaryota.
DR HOGENOM; CLU_009455_0_0_1; -.
DR InParanoid; Q54K32; -.
DR OMA; MRIIMKE; -.
DR PhylomeDB; Q54K32; -.
DR Reactome; R-DDI-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013404; RAC2 GTPase cycle.
DR Reactome; R-DDI-9013406; RHOQ GTPase cycle.
DR Reactome; R-DDI-9013420; RHOU GTPase cycle.
DR Reactome; R-DDI-9013424; RHOV GTPase cycle.
DR PRO; PR:Q54K32; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0045180; C:basal cortex; IDA:dictyBase.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031254; C:cell trailing edge; IDA:dictyBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:dictyBase.
DR GO; GO:0031255; C:lateral part of motile cell; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0045294; F:alpha-catenin binding; IPI:dictyBase.
DR GO; GO:0005516; F:calmodulin binding; ISS:dictyBase.
DR GO; GO:0005096; F:GTPase activator activity; IDA:dictyBase.
DR GO; GO:0019887; F:protein kinase regulator activity; IMP:dictyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:dictyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IGI:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0140509; P:epithelium-like organization; IMP:dictyBase.
DR GO; GO:0000165; P:MAPK cascade; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0008104; P:protein localization; IMP:dictyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR GO; GO:0031149; P:sorocarp stalk cell differentiation; IMP:dictyBase.
DR GO; GO:0036360; P:sorocarp stalk morphogenesis; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR Gene3D; 1.10.506.10; -; 1.
DR InterPro; IPR000593; RasGAP_C.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF03836; RasGAP_C; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Reference proteome.
FT CHAIN 1..822
FT /note="Ras GTPase-activating-like protein rgaA"
FT /id="PRO_0000388253"
FT DOMAIN 218..445
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..822
FT /note="Required for interaction to rac1A"
FT COILED 104..152
FT /evidence="ECO:0000255"
FT CONFLICT 55
FT /note="F -> I (in Ref. 2; AAB39262)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="L -> W (in Ref. 2; AAB39262)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="I -> T (in Ref. 1; AAB62276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 822 AA; 94925 MW; D892AE507715C67A CRC64;
MNKEEYSDIS DSESEEVHET NNHNEHEHEE EDDTPEIVVP ERKFLKEDED YSVPFPVMRE
CLVLLLQSRR ILRDMMYYRF KMDRFLSGNL SVFEIQNLLH SQREDKESDW IAEIQELKRN
LVSEVRRNHT LERDLNRLDK RIALLIKNRG NIQDVLADKA GLKAPKHKGD QKKPELINDP
KKLEAYQNLF YLLQTEPKYL AGLVYLIQPE QMESFLGTVI LTLFGDAFTP REEFLLLSLY
RLSIQKEMAN IATVGDFLKA DTVVPKMIIT YNKRKQGTDY LKAVIGPILS NVIKQELNLE
LKPNLVYAAI ISEQEIRTGE KSTLDRNVSH EKALEVPEVT KTIKARVDQL ISICEQFLDG
IISSLNRLPY GIRWICKQIY QIAEKNFTKS TQDEILKVIG YFIYYRFIQV AMVSPEEYDL
VGREIHPTAR KNLINVSKVL QALFNFAQFG SSEKHFIPLN GWITSHMGDI KNYLQEIIEV
GEPEDYLQVD KYMELTQKTK PVIIISLPEI CNTHQLISKN LDSLVAKGEK DDPMRIIMKE
LDEFGPPPDI AADDDREVQL TLSNKFQKTI EEELSPGESL LSQTKEMVIS LLRALPTLPE
QKDQSDEPPN LVDVLNKARQ ADPSLEPEIK KILDNLKKLE EYNLTTSADN YSSFLKAVAL
EVVNRAEIRE QQKKEKQRLT TSLNNLRKHQ KYLNEQIAQY NQYLQDCRLK HYQNKSKKKK
KGDGAKVGPF KFSFSELHKK GVIVDSEVPQ ITRKKIKFVI SSDTVGVFDV SAKMAGIDVQ
TMRLELDDLL ELNSIGTTTL ELDQITLDVN MTIHLLNKLF LY
