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 01-MAY-2013, entry version 54.
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; Mycetozoa; Dictyosteliida; 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-
RT loxP 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.,
RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA 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.,
RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP NOMENCLATURE.
RX PubMed=15726806;
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
CC actin and the formation of linear actin filaments (By similarity).
CC -!- SUBUNIT: Interacts (via GBD/FH3 domain) with activated Rho-
CC GTPases.
CC -!- DEVELOPMENTAL STAGE: Expression gradually increased after the
CC onset of development.
CC -!- DOMAIN: The DAD domain regulates activation via by an
CC autoinhibitory interaction with the GBD/FH3 domain. This
CC autoinhibition is released upon competitive binding of an
CC activated GTPase. The release of DAD allows the FH2 domain to then
CC nucleate and elongate nonbranched actin filaments (By similarity).
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily.
CC -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain.
CC -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC 3) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ812237; CAH23234.1; -; mRNA.
DR EMBL; AAFI02000148; EAL62593.1; -; Genomic_DNA.
DR RefSeq; XP_636106.1; XM_631014.1.
DR HSSP; O08808; 1Z2C.
DR ProteinModelPortal; Q5TJ56; -.
DR EnsemblProtists; DDB0231185; DDB0231185; DDB_G0289763.
DR GeneID; 8627319; -.
DR KEGG; ddi:DDB_G0289763; -.
DR dictyBase; DDB_G0289763; forF.
DR eggNOG; NOG149898; -.
DR InParanoid; Q5TJ56; -.
DR OMA; NIEIKIA; -.
DR ProtClustDB; CLSZ2429750; -.
DR GO; GO:0005522; F:profilin binding; ISS:dictyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR003104; Actin-bd_FH2/DRF_autoreg.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010472; Drf_FH3.
DR InterPro; IPR010473; Drf_GTPase-bd.
DR InterPro; IPR015425; FH2_actin-bd.
DR InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM-type_fold; 1.
DR SUPFAM; SSF101447; FH2_actin_bd; 1.
DR PROSITE; PS51231; DAD; FALSE_NEG.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Coiled coil; Complete proteome; Reference proteome.
FT CHAIN 1 1220 Formin-F.
FT /FTId=PRO_0000363918.
FT DOMAIN 6 373 GBD/FH3.
FT DOMAIN 532 655 FH1.
FT DOMAIN 656 1054 FH2.
FT DOMAIN 1083 1158 DAD.
FT COILED 392 428 Potential.
FT COILED 1032 1062 Potential.
FT COMPBIAS 496 499 Poly-Gln.
FT COMPBIAS 528 536 Poly-Ser.
FT COMPBIAS 547 554 Poly-Gln.
FT COMPBIAS 577 588 Poly-Pro.
FT COMPBIAS 594 601 Poly-Pro.
FT COMPBIAS 604 607 Poly-Gly.
FT COMPBIAS 608 615 Poly-Pro.
FT COMPBIAS 621 626 Poly-Pro.
FT COMPBIAS 633 637 Poly-Pro.
FT COMPBIAS 638 643 Poly-Gly.
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
//
