GACJ_DICDI
ID GACJ_DICDI Reviewed; 906 AA.
AC Q54MV3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Rho GTPase-activating protein gacJ;
DE AltName: Full=GTPase activating factor for raC protein J;
GN Name=gacJ; ORFNames=DDB_G0285641;
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}.
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DR EMBL; AAFI02000079; EAL64658.1; -; Genomic_DNA.
DR RefSeq; XP_638190.1; XM_633098.1.
DR AlphaFoldDB; Q54MV3; -.
DR SMR; Q54MV3; -.
DR STRING; 44689.DDB0233842; -.
DR PaxDb; Q54MV3; -.
DR EnsemblProtists; EAL64658; EAL64658; DDB_G0285641.
DR GeneID; 8625236; -.
DR KEGG; ddi:DDB_G0285641; -.
DR dictyBase; DDB_G0285641; gacJ.
DR eggNOG; KOG1453; Eukaryota.
DR HOGENOM; CLU_320413_0_0_1; -.
DR InParanoid; Q54MV3; -.
DR OMA; NHAMAPE; -.
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:Q54MV3; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
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 Cytoplasm; GTPase activation; Reference proteome.
FT CHAIN 1..906
FT /note="Rho GTPase-activating protein gacJ"
FT /id="PRO_0000380207"
FT DOMAIN 161..348
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 53..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..538
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..561
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..738
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 99495 MW; BD521170490BFEA5 CRC64;
MEEQQPPSIK KKIVDFLTNF LKKRPSHEDL RRDNILVAPN NVSPAIQPSR YELEGHLNPS
SHNRDDSSNN NNNNNNNNNT VEYSRGHSKS HSRSDSKHHN RENSKSDRDN SRSDNIRFGR
KDTFKNAWDY LRNIDFTFSK TKYGNTVVHR LKHPQFGLSP EELQSLYPDQ PHGIPIVLTK
CFEYLSKHLE TEGLFRVPGS NREVSLLKFK IEDGDLDFSE VLIPYNICGL ISTFFKELPE
PLIPFDYYND AILITKLGSK DKYIIGLRDL VLSLPPANLC MLRKLLEFLL TVEKKNEFNK
MTISNISIIF GVTLLKDPDT VDPMKSLNNI QAQSTIIKYM LEYFNDIFKE ASVVKAYRKS
IVPKEPMDTT SISYLDPAES NGGSPRTSNT PYQQQHQLSS QSMANIKPRP PSRSKMMRET
IVLSPRVSGG NNQVYANATM TRPMSRLFFD PEIIPSPPPT TTTTTTTTTN TTTTTTTTNT
TPNNTTTVNI QQKPVPPKPN LIPRKLPPNP NYSTYPAPLP PRQPNTIPLA PIPPPKPNST
YKKQITQPPP PRKPTSPSPP IATLKPTSKS DFIPSTNNNL NNNNTTTTTS SLISIPKAKP
PPPKRNNVVS PAIEEPINPN LNINSTTTTP TPPLASFKNN GTISSGSKSN PNLQNLLNTN
QPLVSSNGPP NKPPPQPFEL LKSKPITTTP TIKKGVTFSE TPKISNSPPS PSSSSPSPPH
NQPIIVNKPI PSKSAPPPVR TTSSPSIVTK KFVPTIPTQT TTASSSSTPT TPKNQHLSKD
DSSIPPINTS QTNNNISNSS IPSPKSKSAL SLSTPKDSIT GKPIKPPSNS DLSISTTPLP
PTSSSPTSSS PLQSPKISSP SVLTVSQKIA LNEKIAANQA KKNPLSNSGG LKQISPDLIK
SNNINK
