ID   FORG_DICDI              Reviewed;        1074 AA.
AC   Q1ZXK2; Q86AQ6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Formin-G;
GN   Name=forG; ORFNames=DDB_G0277175;
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=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
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   [3]
RP   NOMENCLATURE.
RX   PubMed=15726806; DOI=10.1007/s00709-004-0058-2;
RA   Cvrckova F., Rivero F., Bavlnka B.;
RT   "Evolutionarily conserved modules in actin nucleation: lessons from
RT   Dictyostelium discoideum and plants. Review article.";
RL   Protoplasma 224:15-31(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15740615; DOI=10.1186/1471-2164-6-28;
RA   Rivero F., Muramoto T., Meyer A.-K., Urushihara H., Uyeda T.Q.P.,
RA   Kitayama C.;
RT   "A comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD
RT   architecture in formins from Dictyostelium, fungi and metazoa.";
RL   BMC Genomics 6:28-28(2005).
RN   [5]
RP   INTERACTION WITH RHO GTPASE.
RX   PubMed=16762450; DOI=10.1016/j.ejcb.2006.04.011;
RA   Vlahou G., Rivero F.;
RT   "Rho GTPase signaling in Dictyostelium discoideum: insights from the
RT   genome.";
RL   Eur. J. Cell Biol. 85:947-959(2006).
CC   -!- FUNCTION: Formins play an important role in the nucleation of actin and
CC       the formation of linear actin filaments. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via GBD/FH3 domain) with activated Rho-GTPases.
CC       {ECO:0000269|PubMed:16762450}.
CC   -!- DEVELOPMENTAL STAGE: Expression is kept at constant levels after the
CC       onset of development. {ECO:0000269|PubMed:15740615}.
CC   -!- DOMAIN: DRFs are regulated by intramolecular GBD-DAD binding where Rho-
CC       GTP activates the DRFs by disrupting the GBD-DAD interaction.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC       interaction with the GBD/FH3 domain. This autoinhibition is released
CC       upon competitive binding of an activated GTPase. The release of DAD
CC       allows the FH2 domain to then nucleate and elongate nonbranched actin
CC       filaments (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000019; EAS66907.1; -; Genomic_DNA.
DR   RefSeq; XP_001134591.1; XM_001134591.1.
DR   AlphaFoldDB; Q1ZXK2; -.
DR   SMR; Q1ZXK2; -.
DR   STRING; 44689.DDB0231630; -.
DR   PaxDb; Q1ZXK2; -.
DR   EnsemblProtists; EAS66907; EAS66907; DDB_G0277175.
DR   GeneID; 8620897; -.
DR   KEGG; ddi:DDB_G0277175; -.
DR   dictyBase; DDB_G0277175; forG.
DR   eggNOG; KOG1922; Eukaryota.
DR   eggNOG; KOG1925; Eukaryota.
DR   HOGENOM; CLU_287208_0_0_1; -.
DR   InParanoid; Q1ZXK2; -.
DR   OMA; HIGNNDE; -.
DR   PRO; PR:Q1ZXK2; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0070687; C:macropinocytic cup cytoskeleton; IDA:dictyBase.
DR   GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR   GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR   GO; GO:0005522; F:profilin binding; ISS:dictyBase.
DR   GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:dictyBase.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:dictyBase.
DR   GO; GO:1905303; P:positive regulation of macropinocytosis; IMP:dictyBase.
DR   GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IMP:dictyBase.
DR   Gene3D; 1.20.58.2220; -; 1.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024574; ELMO_ARM.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   Pfam; PF11841; DUF3361; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Coiled coil; Reference proteome.
FT   CHAIN           1..1074
FT                   /note="Formin-G"
FT                   /id="PRO_0000363919"
FT   DOMAIN          34..423
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT   DOMAIN          597..623
FT                   /note="FH1"
FT   DOMAIN          631..1031
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   DOMAIN          1037..1073
FT                   /note="DAD"
FT   REGION          476..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1053..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          502..530
FT                   /evidence="ECO:0000255"
FT   COILED          914..971
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        566..615
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1074
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1074 AA;  118522 MW;  989657746965520A CRC64;
     MILSITFQLD PISNNSTSLS NSIDNRSSIN VTALQMQQGS KTYNLDQNSS YKTVFLAICQ
     LFGIKESSAQ DYCLQLESSK KYLNWPPQSD ESKTKHIVKQ LYESGETALV LQLNPTYRSS
     KWVKALNDSE TNEKDIMFHL KYKLQENEFA ESFIEQNGME GILRMVTNGK GNAQTYSLAS
     LRACLEYVSA MEIITKTPHL VKQLFSLVDS NVVGVCRGAL ELLFVLCDFR KEEGFKSVHL
     AAKGTAVAQG KKPYLNVIKL LDSGDLETKI NAFTLLNVLL SNCPTDEKVG KLCKKWGELG
     LDDKLRSLTS IQQQEFQIQL EIYEETSGVN LRTKASRLEA ICNRLKSKLT EYEAQQPLIA
     ILKEELKLAQ QLIKEASTDR VFLSSHPMQR YLGPTIQSYP ADLSFLKTTA AERDKINEFE
     KKILAINEQL RQETKLSEEL KNQVLANKKQ FDSTIAELNE ENQRLTQVEV KFKLQQSISP
     SQDSSNNQKA SSSSSNTSTL NDSDIQSIQS SLKEATLEIE RLKLAIEEKM PPNEAQQIFS
     QSLITTAAFT PTSPDISNDG QPISGGGAPP PSPSPPPPIS GGGAPPPPPP PPPPPSGGGA
     PPPPPPPPPS GGKKAGAPGA PPTGPAAIQP NKPVINPSSK MKPLYWKRII LPPSNRNESI
     WDQVLEPTFD SKDFENLFCA KKKAVDSSLS TNPSSTTGKE GEKVKLVSLV DIKKSNSIAF
     MLAKIPTAEG LKKAIDTVDN SILGKEIIKT LITNVPTEQD YQLIKGSEIH ESKLDKPERW
     ILEIYGFPMM KERLVAWLFQ LEYQEMYNNI IQILEKLQNA IKDTKSSDSL KKILGIVLVL
     GNYMNGGSGR GQADGFTLEI LDSLATSKDV ENKTSLLDYV SKISMEKYPK TMNVAQELDS
     LKLVQLSISD MSTDINDLEK QFNISKNNCK KVLEANIPSS SKFQSTIGSF LEKTEIDIKN
     LKENQKNIVD SFIQLVEFFG YPKSYATTAS CQQFFNSIYS FSLLFSKQCQ KIEKEREALA
     KASGDNGAVQ NKKIAGGADP LAALANAIKL GQTGLRKRPG PENSSGGSQL NLNK