MGP1_DICDI
ID MGP1_DICDI Reviewed; 920 AA.
AC Q54GD0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=GTPase activating protein homolog 1;
DE AltName: Full=GTPase activating factor for raC protein BB;
DE AltName: Full=Rho GTPase-activating protein gacBB;
GN Name=mgp1; Synonyms=gacBB; ORFNames=DDB_G0290233;
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, SUBCELLULAR LOCATION, 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 {ECO:0000269|PubMed:18334553}.
CC Contractile vacuole {ECO:0000269|PubMed:18334553}. Note=Localized to
CC tubules of the contractile network.
CC -!- DISRUPTION PHENOTYPE: Show a strong cytoskeletal phenotype.
CC mgp1-/mgp2- cells have a severe fruiting defect, an overabundance of
CC filopodia and slug motility and function are affected. They empty their
CC contractile vacuoles less efficiently than normal and consequently they
CC have three times the usual number. {ECO:0000269|PubMed:18334553}.
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; AAFI02000161; EAL62338.1; -; Genomic_DNA.
DR RefSeq; XP_635848.1; XM_630756.1.
DR AlphaFoldDB; Q54GD0; -.
DR SMR; Q54GD0; -.
DR STRING; 44689.DDB0233877; -.
DR PaxDb; Q54GD0; -.
DR PRIDE; Q54GD0; -.
DR EnsemblProtists; EAL62338; EAL62338; DDB_G0290233.
DR GeneID; 8627556; -.
DR KEGG; ddi:DDB_G0290233; -.
DR dictyBase; DDB_G0290233; mgp1.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG3565; Eukaryota.
DR HOGENOM; CLU_316994_0_0_1; -.
DR InParanoid; Q54GD0; -.
DR OMA; NNLCHPF; -.
DR PhylomeDB; Q54GD0; -.
DR Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q54GD0; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0033298; P:contractile vacuole organization; IMP: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:1903013; P:response to differentiation-inducing factor 1; HDA:dictyBase.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0016050; P:vesicle organization; IBA:GO_Central.
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..920
FT /note="GTPase activating protein homolog 1"
FT /id="PRO_0000380224"
FT DOMAIN 90..344
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 533..716
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 65..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..276
FT /evidence="ECO:0000255"
FT COMPBIAS 748..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 102301 MW; 1AC46D30E7483110 CRC64;
MNVENQDPNI MVIPNNNLGP IDGNNISPAM NDENSNNGSS FLKNLVNTGT NLLFSSSSSI
ASPPNLGGLS NDSTNNNSNS NNTIDSSKPL SFENDMSDGY EALVRRSEIA IDQCKELLDF
FKKRASEEEK YSKNISNMFS KFKVKDDHDT FQKGVSLLNK INDAESTIHR SFSQNITTNL
YHPLNEAIKD MEKSRKRLLE DGKKLKNDLK DSIENVKKSN QKYEKLCREM EQAKLELIEE
GNDTKSGKVE TLEKKLEKTK LASIKAEDEY KEQINETNEF ISGVYQNRLS ENLREFQQFE
LTRLEIMKSN IRNYIGFMKD IPQALQCEID STKGFVDIID PEVDLQNYIM NNSNPKKVLL
PFIFEAYNDH KPFVDQHNQN SSSSSSTNAL NYASPMSASG SITNTITSQS GSTIISNGAS
QPIEIPSPQP ISEQQQIPPQ QQQQQQQAQV PPTSINQSSS PPVNPMGRQQ SLKENIFGFF
NKATTNLKSS TSSLLTKDGN STTSSNTSTS NSNQLSKSGI GLPIINTNSI FGVELEVLIE
NDNSKKKGNG VELEVPLILT QFVQALLKLE SFKMDGVFVS LPSHFNIQQE KQKLDQTGTL
ENITDVYLIA SLFKNWIGDL PNPLISYAIY QEIIEAPDNA WKIIESGIPI LHRRVLHYII
DFLVDFVNCS KMDTHSISLI FTPVLIRSPF NGDSLLNSKK EVAVIENMII DSLETKRGNY
ILKRNLPIIP DDENSDDDDD DSGHIDDENN SSTSGENDIN TTNINNNNNV NSNNDTNNNN
NNSNTTTTNN NNNNDSNNSN STNNNNNNNN NNTNNDDNES NNSGYGVSSN GNNINSSVGG
SVTHHFLYQT TPTNNVTPVL SDFFDTNSSN GSSKANTNTH NLGVRNSSNI SFDTISTNQS
DSEPVLVEYD NDDFDILSYK
