GACJJ_DICDI
ID GACJJ_DICDI Reviewed; 873 AA.
AC Q54FG5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Rho GTPase-activating protein gacJJ;
DE AltName: Full=GTPase activating factor for raC protein JJ;
GN Name=gacJJ; ORFNames=DDB_G0290873;
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).
CC -!- FUNCTION: Rho GTPase-activating protein involved in the signal
CC transduction pathway. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000171; EAL62001.1; -; Genomic_DNA.
DR RefSeq; XP_635506.1; XM_630414.1.
DR AlphaFoldDB; Q54FG5; -.
DR SMR; Q54FG5; -.
DR STRING; 44689.DDB0233754; -.
DR PaxDb; Q54FG5; -.
DR EnsemblProtists; EAL62001; EAL62001; DDB_G0290873.
DR GeneID; 8627873; -.
DR KEGG; ddi:DDB_G0290873; -.
DR dictyBase; DDB_G0290873; gacJJ.
DR eggNOG; KOG4270; Eukaryota.
DR HOGENOM; CLU_329137_0_0_1; -.
DR InParanoid; Q54FG5; -.
DR OMA; HSANNKM; -.
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:Q54FG5; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0022607; P:cellular component assembly; IEA:UniProt.
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 Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; GTPase activation; Reference proteome; SH3 domain.
FT CHAIN 1..873
FT /note="Rho GTPase-activating protein gacJJ"
FT /id="PRO_0000380208"
FT DOMAIN 301..402
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 428..621
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 628..694
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 64..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 715..761
FT /evidence="ECO:0000255"
FT COMPBIAS 64..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 97158 MW; 5133CCA37B06C684 CRC64;
MAAPSSNYQL YGLKIGFPPG GLMRNKQMKF NDYGITVKEA IQIITNKQGM QNPDSYTLQI
TYSDEPSSIN TSSGNIGSNN NSSSNTPLTG SLGMGPPPPS ASIGGGGGGG DNGITNSGNI
GSSSNSDLKK STSSGIVNVN NSSNAPTRRL KWMDDNEKLI SYPLGAHDVV IELKKKYQLI
KVYDGKQTMN LIVDITKPLS DLMDLVSCKF KLRSTSDCKL FTYGKEINLN SNIKNLNIDT
SLPFILRDNN DPNSLSLESI QWDNGNGFFV GGNGGIGGIG SDDDADDINN NLSVPAKSII
NPVREGYLKK QDKKKSWKTR YFKLTDKYLY WYKSPTAIKA SGMIICKDYH IKLAPSTHSK
EVKLEFTPKH MIAGATTIIH YIKFENEQEL KQWTVLPIVI ESSNDSGSNN SNTSGGNQSM
IGKKVFGVPI EKTVSGNNEI PAVVLQTIDY IEKKAMDIVG IFRLSGSVLT IEQWKAKYDK
GEKVDLFQEV DPHAVAGLLK LYLRELPDPL LTYEKYDNFI AAQSIDDFPS RIKLIKHLVK
SLPPVNYAVL SYLMAFVGKV ATHSAANKMQ VHNLSTVFGP NLIKDRQDSG DYGNNVQVLV
EDTPIINALA LSLIRDYQYI FTDKEIPEQK ILAKSLYEYA GNDDGTTSED DKDLLFPKGA
TIKVTQQGTD GWWTGEYQGK QGKFPASYVE LLPHSPSTLL RTKSNSNLTK KKKFMLEMES
TKTKNQEIDK NIKQLEITKK ELESTINDLE NEKAALENDP TIKAMMNLLA NAKTNKDIAM
IPKNIDVLFQ KFEEYKSSHE ALATTKTTLI DEYEQFNNNP KKRLDTKEKE QIQQKYDNLS
IIIDKSQKIR SKSINSKKII NDDLVELKKI FSL
