ID   MGP3_DICDI              Reviewed;        1337 AA.
AC   Q55DK5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=GTPase activating protein homolog 3;
DE   AltName: Full=GTPase activating factor for raC protein AA;
DE   AltName: Full=Rho GTPase-activating protein gacAA;
GN   Name=mgp3; Synonyms=gacAA; ORFNames=DDB_G0269624;
OS   Dictyostelium discoideum (Social amoeba).
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   IDENTIFICATION.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Contractile vacuole {ECO:0000250}.
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DR   EMBL; AAFI02000005; EAL72162.1; -; Genomic_DNA.
DR   RefSeq; XP_646126.1; XM_641034.1.
DR   AlphaFoldDB; Q55DK5; -.
DR   SMR; Q55DK5; -.
DR   PaxDb; 44689-DDB0233874; -.
DR   EnsemblProtists; EAL72162; EAL72162; DDB_G0269624.
DR   GeneID; 8617075; -.
DR   KEGG; ddi:DDB_G0269624; -.
DR   dictyBase; DDB_G0269624; mgp3.
DR   eggNOG; KOG2398; Eukaryota.
DR   HOGENOM; CLU_258661_0_0_1; -.
DR   InParanoid; Q55DK5; -.
DR   OMA; PFEYEPY; -.
DR   PRO; PR:Q55DK5; -.
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:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07610; FCH_F-BAR; 1.
DR   CDD; cd04389; RhoGAP_KIAA1688; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 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   PANTHER; PTHR45876; FI04035P; 1.
DR   PANTHER; PTHR45876:SF8; FI04035P; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 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..1337
FT                   /note="GTPase activating protein homolog 3"
FT                   /id="PRO_0000380226"
FT   DOMAIN          14..264
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT   DOMAIN          422..611
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          279..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1041..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1114..1166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          830..859
FT                   /evidence="ECO:0000255"
FT   COILED          1189..1219
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        290..305
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..689
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..817
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1337 AA;  150248 MW;  73393E0FD5FD8AF4 CRC64;
     MTVDNSQIPN LNQPESFADL WDGYENVSKA TEKGVLLLKD ITKFFKKRIQ SEDEYSKTLS
     KLVLKFEPMA PDGYIGPRLK NTWDQIKLET LTHSNHHENI CNNISTHIIE PIEGLIVDLE
     QKMKSIHVDA EKSFIHYQES VAKLKKAKQN YDRLCKDSFE ITGVSKGETQ KVQKRAIKAA
     QDVIKADKDY RAQINETNTS QKQFLTELIP KIMNDLQRLE MVRIHMVKSY FHRYFKSMES
     TPQKFNTETE NLLNLINSIN NEDEIQDFVR KSKTTHKYPK PFEYEPYLDR FTTPPPPPPP
     QISSPQLLSP RGDISIQHSS SSNSLPIFPT QHQLLSNKEK ADNNITNSLS LSSDSLQTNL
     NNGNNGGNGN NGSNTPTKEK KPSSWGLKRF STSVSSTSDR KLLNKQIQSI GLAHNGGNIF
     NCKIEDIMVA QKKKYPYLEI PFIVVFLKHK LVALDVFKTQ GIFRVPGNVV DINSLKKRFD
     EGNYEVAPTE NVYTIASLLK LWLREITEPL FPLTVYDQCI ENSNKREKIF EIISSLPILN
     QKTISYIIEL LQECGKSVNV EHNKMNFPNL AMVFSPCFLR CSHTDPNILL GNIFKEKEFV
     QNIIEHFKPL QVNDSLEGPP SSSSSSSTSI NQSSIESPPT SPLRSSTNSN ANKSSTPIKP
     SSPSQQQQQQ QQQQQSSTPS TPLSSTTNTN VKHNILSPIV EQQSPNNGKQ PIALTQTYSH
     LNIGSVPLII NTVNNNNQNQ NQNQNQNQNQ DQNQNQSKQP IQSSNQTQQQ VSAPATPHTV
     AVNPKINQIK AETITTPQKS IGDGNGLIGQ SPSAHLMSPS EVKRRSNAIY LEDQERCKQR
     IDELHTQVNE LYSDITTIET TTYFAMQSSL LITKLTKSLE SFLTIDMWNL TLQDIKEAIE
     KNKFVSPPPI NFKIPSKMPK LSPIELVQNE QSSELLRSWL SNVTLTVNRI NEYLCYLGGV
     VIRIHSPDTL FAISNLFTDY DLSPQQNPKF VSLTLEQSTI FIQKTLALLE PLNPFTSDEL
     NINVKVQDTI TPASFSPALI SDPDCNSPPT ISNTTNRLLN TSGSTDFSTT PLSSSPSTSS
     TSLSTNNNNN NNGNRNLDIN NSPTIVITNS SLNKSALSTN NNNNNNNNNN NNPTTKLSSS
     TSSTSTTTTT NTNTNTTTNE KIAHAIISPS SSTTSFKFDD DEDEDEDLLE INNKLHSQLT
     EELKKKQQQY KQLIFDIIDM IKDKKKLMNS LDLTNSDSQL DIKSIAKLSL SLKRALDNFT
     SESGFDIEDE QDPIINKEND SFVNLKIMTS HFISRIVLIL TTILSISNEF NSTLYQLLLP
     FNENNNNNNE NNNINNQ
//