ID   MGP2_DICDI              Reviewed;         877 AA.
AC   Q55CK2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=GTPase activating protein homolog 2;
DE   AltName: Full=GTPase activating factor for raC protein CC;
DE   AltName: Full=Rho GTPase-activating protein gacCC;
GN   Name=mgp2; Synonyms=gacCC; ORFNames=DDB_G0270024;
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   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=18334553; DOI=10.1242/jcs.021113;
RA   Heath R.J., Insall R.H.;
RT   "Dictyostelium MEGAPs: F-BAR domain proteins that regulate motility and
RT   membrane tubulation in contractile vacuoles.";
RL   J. Cell Sci. 121:1054-1064(2008).
CC   -!- FUNCTION: Rho GTPase-activating protein involved in the signal
CC       transduction pathway (By similarity). Regulator of the contractile
CC       vacuole network as well as involved in driving vacuole emptying.
CC       {ECO:0000250, ECO:0000269|PubMed:18334553}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Contractile vacuole {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Show a subtle phototaxis defect. mgp1-/mgp2-cells
CC       have a severe fruiting defect, an overabundance of filopodia and slug
CC       motility and function are affected. They empty their contractile
CC       vacuoles less efficiently than normal and consequently they have three
CC       times the usual number. {ECO:0000269|PubMed:18334553}.
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DR   EMBL; AAFI02000005; EAL72362.1; -; Genomic_DNA.
DR   RefSeq; XP_646479.1; XM_641387.1.
DR   AlphaFoldDB; Q55CK2; -.
DR   SMR; Q55CK2; -.
DR   STRING; 44689.DDB0233875; -.
DR   PaxDb; Q55CK2; -.
DR   EnsemblProtists; EAL72362; EAL72362; DDB_G0270024.
DR   GeneID; 8617441; -.
DR   KEGG; ddi:DDB_G0270024; -.
DR   dictyBase; DDB_G0270024; mgp2.
DR   eggNOG; KOG3565; Eukaryota.
DR   HOGENOM; CLU_328022_0_0_1; -.
DR   InParanoid; Q55CK2; -.
DR   OMA; AMIKDME; -.
DR   PhylomeDB; Q55CK2; -.
DR   PRO; PR:Q55CK2; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0000331; C:contractile vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0033298; P:contractile vacuole organization; IGI:dictyBase.
DR   GO; GO:0006887; P:exocytosis; IGI:dictyBase.
DR   GO; GO:0051490; P:negative regulation of filopodium assembly; IMP:dictyBase.
DR   GO; GO:0042331; P:phototaxis; IGI:dictyBase.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; GTPase activation; Reference proteome; Vacuole.
FT   CHAIN           1..877
FT                   /note="GTPase activating protein homolog 2"
FT                   /id="PRO_0000380225"
FT   DOMAIN          14..285
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT   DOMAIN          374..560
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          589..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          130..214
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        591..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   877 AA;  97411 MW;  0768199C71AC5E70 CRC64;
     MSSSANSSPA TTKFKFTDNL WDGFDLLVKR TDNDLIQSKN ILNFFKKKAE LEEQHSKKLE
     KLSLKTMMTI DESTSINAIS YNSSWKKIIN SSMMESEQHT LLNTSILNKV IQPLQAMIKD
     METKRKKILQ EGIKLKQDMK EMVDELKKSQ FKYDKAGKDL ESSRMELREY REQLDHQQQQ
     QPSDSDLNNI SKIERRIQRC EQDFSNCDEE YREQIKATND FQHLYNTEKL PKILNDFEHF
     VISHSHFSKS YFTNLVSVLI ELPSAYQQNY EFVKKSVEMI DITNDVQEFI RKNLMKKQLA
     QPFQYEPYIE GKLTKKTISL TWNNKILSQF SRSSNNNTAT ANNTSSGNLN PYLNGGIGGT
     KKDEPILPTA SFKVSLDELM NRQKDNHPTL EVPYVLQVLS TRIAQMKGHV TEGIFRVPGI
     ISTIKETRLR IDKADFNLSN IDDVRTPAAL LKQWLRDIPT ALIPDSLYQQ CIDTPTNAIA
     IVKTIPIINQ RVLCYLINFL QIFTKFEFVA HSKMGTSNLA MVFAPCILRC TSTDANVMLN
     NVPNERLFVE TLIKQIPPPL NTNEFLNLPI SMSDAINDSE DIEELNDLDQ LSNDDNNNSN
     TNTSNISIGS GSNSNIVVNY SNNSPNIESS TLPSQSVVTT IETLPPLNDD HNSGSGNESN
     SSSSNSTTTP TGSPTTASKP RGPRTQTLGW VRIKPAPKPS AEPTITLSSS IAAGTTTTTT
     TATGITTTTT TTAGPEKTII SPVIIKPAAA TPTTTTPTTT PTTTTSPTTA TIPAVSTSTI
     KTSSPDRTTP LTSSPPLAST KSTDELMKKL DQFTQETTPS IRIATTTTPT TITTPTTTAT
     TTTITTDKTT PVTSSPPTAS NISSEDLMKK LDQFINF