ID   FORF_DICDI              Reviewed;        1220 AA.
AC   Q5TJ56; Q54H12;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Formin-F;
DE   AltName: Full=Diaphanous-related formin dia1;
GN   Name=forF; Synonyms=drf1; ORFNames=DDB_G0289763;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX2;
RX   PubMed=15507682; DOI=10.1093/nar/gnh136;
RA   Faix J., Kreppel L., Shaulsky G., Schleicher M., Kimmel A.R.;
RT   "A rapid and efficient method to generate multiple gene disruptions in
RT   Dictyostelium discoideum using a single selectable marker and the Cre-loxP
RT   system.";
RL   Nucleic Acids Res. 32:E143-E143(2004).
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 gradually increased after the onset of
CC       development. {ECO:0000269|PubMed:15740615}.
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; AJ812237; CAH23234.1; -; mRNA.
DR   EMBL; AAFI02000148; EAL62593.1; -; Genomic_DNA.
DR   RefSeq; XP_636106.1; XM_631014.1.
DR   AlphaFoldDB; Q5TJ56; -.
DR   SMR; Q5TJ56; -.
DR   STRING; 44689.DDB0231185; -.
DR   PaxDb; Q5TJ56; -.
DR   PRIDE; Q5TJ56; -.
DR   EnsemblProtists; EAL62593; EAL62593; DDB_G0289763.
DR   GeneID; 8627319; -.
DR   KEGG; ddi:DDB_G0289763; -.
DR   dictyBase; DDB_G0289763; forF.
DR   eggNOG; KOG1924; Eukaryota.
DR   HOGENOM; CLU_279717_0_0_1; -.
DR   InParanoid; Q5TJ56; -.
DR   OMA; KENHKER; -.
DR   PhylomeDB; Q5TJ56; -.
DR   PRO; PR:Q5TJ56; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
DR   GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005522; F:profilin binding; IPI:dictyBase.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0070060; P:'de novo' actin filament nucleation; IDA:dictyBase.
DR   GO; GO:0030041; P:actin filament polymerization; IDA:dictyBase.
DR   GO; GO:0046956; P:positive phototaxis; 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; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR027645; Formin_F/D.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   PANTHER; PTHR45725:SF11; PTHR45725:SF11; 3.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM01139; Drf_FH3; 1.
DR   SMART; SM01140; Drf_GBD; 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..1220
FT                   /note="Formin-F"
FT                   /id="PRO_0000363918"
FT   DOMAIN          6..373
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT   DOMAIN          532..655
FT                   /note="FH1"
FT   DOMAIN          656..1054
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   DOMAIN          1083..1158
FT                   /note="DAD"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1049..1192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          392..428
FT                   /evidence="ECO:0000255"
FT   COILED          1032..1062
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..640
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1085
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1096..1114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1115..1149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1151..1192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1220 AA;  135806 MW;  3F2DAEA23D46036C CRC64;
     MNRIFGRKKK DKDSDEKGST ESENDFLSSL PAKANKRYSM AYSSLQPDGN NSTNSKSADK
     FDDKGKAVDT PEFFVNTINL LPNIEILAQL CSSLQSKPSA WSKSLIDCNG IEALLNVLAF
     IERNGQKDSD VILQSLAVTC LLSLLNSKYG IEKAIATPNS MIRLITSMDT PKADTRSSVF
     EILTAICMIS EKGYQLILEA MTHFKQVRKE RFRFTFLVES MKKVMNSSDK EYLTTCLTLV
     NGIVNSSEEI DERIQLRTEF TRLGLDEVIS VNKNIPYEEA PDLLTQIDVY EDEQRADQEE
     LSERFEDLDI DINDPQVIFN EIYKQAKDRL HHPLLAILQS LLSISSDTEV GMLSWFLIEK
     LVLQISVNKP MIGDDDGKVS LEDLLASTAP SVALQSEFQK NIEELAKVKD QLKKANFDLN
     IANQELSSRS HESSVLKSNM FNTVKQKDQE IIKLRGQMKR IDSNFFSPPG GDGDDHINVI
     NTPEESSPHH ESPRKQQQQT SKPPLNPKSS KPPISSSQLK EKSKSNLSSS SSDSLSNDFK
     SQVEVAQQQQ PQQQNIESTL TPEPTQIIKE EPIVTTPPPA PPAPPPPPMM GGGPPPPPPP
     PMMGGGGPPP PPPPPMMGGG PPPPPPMGGK GGPPPPPGGG GFGLFNSNKP PANAPKFTVS
     KPTTKVKQFQ WTKIPNKKLG ETIFTNLGTI KTDWLNVGEI ENLFFAPEAN SQKKLEASDK
     KSTSSTKPGT VSVIDPKKSQ NLAIYLSKFK CPLEEIKTAL YTLDEDIFTM ESLKALEQYL
     PTDEDMEAIK DYLKKDGELK MLTKAEHFLL EMDSVSSLAE RVKSFYLKIL FPDKLKEIKP
     DLELFTKTIK DIKNSKNFLK VMEVVLIIGN FLNGGTARGD CFGFKLDALL KLADTKTANN
     KSNLLVYIIS ELEQKFPDSL KFMDDLSGVQ ECVKISMNTI SADLNLLKKD LDAVNNGIGK
     MKRSKEESYF FSTMDDFIKD ANIEIKIAFD QFQEAEKNFQ ELAVLFGEES KIPSEEFFVT
     INRFIVMFDK CYKDFQRDKE AAERAIKRDE AKAKKAQQLK RMNGKIASST NNKNPLASSS
     TSVGDGGMVE DIMQSVRDGD AFKQRRRLKG TKENTDDSSS ITTISEQSEN SNTSSITITT
     PSGIELDITP SKSGSRREKK TSKSSDKDKE KEKEKEKQCE STESEDINKK DINVAAKALT
     IVMRSKQTMH SRIDTFNFDA