ID   GACV_DICDI              Reviewed;         520 AA.
AC   Q54BP9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Rho GTPase-activating protein gacV;
DE   AltName: Full=GTPase activating factor for raC protein V;
GN   Name=gacV; ORFNames=DDB_G0293510;
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: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AAFI02000217; EAL60690.1; -; Genomic_DNA.
DR   RefSeq; XP_629103.1; XM_629101.1.
DR   AlphaFoldDB; Q54BP9; -.
DR   SMR; Q54BP9; -.
DR   PaxDb; Q54BP9; -.
DR   EnsemblProtists; EAL60690; EAL60690; DDB_G0293510.
DR   GeneID; 8629262; -.
DR   KEGG; ddi:DDB_G0293510; -.
DR   dictyBase; DDB_G0293510; gacV.
DR   eggNOG; KOG4270; Eukaryota.
DR   HOGENOM; CLU_524227_0_0_1; -.
DR   InParanoid; Q54BP9; -.
DR   OMA; KKWIRDL; -.
DR   Reactome; R-DDI-9013148; CDC42 GTPase cycle.
DR   Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR   Reactome; R-DDI-9013404; RAC2 GTPase cycle.
DR   Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR   PRO; PR:Q54BP9; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator 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; GTPase activation; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..520
FT                   /note="Rho GTPase-activating protein gacV"
FT                   /id="PRO_0000380219"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          195..472
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          33..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          28..192
FT                   /evidence="ECO:0000255"
FT   COILED          480..520
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        136..189
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..520
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  60594 MW;  0FDE45C4885A73F7 CRC64;
     MSNNSNNNIK TYYIIGIITL IFIVSAVIKN QLSSSNQEQQ EEEEETDSMG KSKGRGNKKG
     KKPEKIQEKK LDNHLKNLEK VKLQEDFKLQ QDEKQQLKKE ETILVEKQEI VVDELKNKKD
     EEKQQQQQEE DQQQQQQQQQ EEEEEEEEQQ EIEEDEEEEE GQEQEEEEEQ QEIEEGEEEQ
     QEEEQEEEQF SMFGVSIERL MDFQRQEDEN EGSDEVEESS KVPIVLSFML DRIKNLNGFK
     TEGLFRVNGN LKLVEQLATE GFDPFSDDLD PNVNTWASLL KKWIRDLPEP LIPHELNPII
     LDFCTNNNIN NTCNNNNDNN NNNNFNVCAS TNNLGNVLNL STNICNNNNN NNNNNNNNNN
     NNNNNDNNNN NNESIEKKIT NIINMIKSDD HRNVLYKIGE FFGEMLQEET VLITKINVES
     LSKILTPSLF KPNNIIDDFS NGSLNGSGNQ IPKYLTTLDL PSILLKQKKE IAFVSCLLNY
     FKDEYSKKLQ EQNDQEEDNQ EEEKDNQEED EDEEDKDQEE