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Database: UniProt
Entry: Q5TJ56
LinkDB: Q5TJ56
Original site: Q5TJ56 
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   16-APR-2014, entry version 60.
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.
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DR   EMBL; AJ812237; CAH23234.1; -; mRNA.
DR   EMBL; AAFI02000148; EAL62593.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q5TJ56; -.
DR   STRING; 44689.DDB_0231185; -.
DR   EnsemblProtists; DDB0231185; DDB0231185; DDB_G0289763.
DR   KEGG; ddi:DDB_G0289763; -.
DR   dictyBase; DDB_G0289763; forF.
DR   eggNOG; NOG149898; -.
DR   InParanoid; Q5TJ56; -.
DR   OMA; AHVENIQ; -.
DR   PhylomeDB; Q5TJ56; -.
DR   ProtClustDB; CLSZ2429750; -.
DR   GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR   GO; GO:0005522; F:profilin binding; IPI:dictyBase.
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; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR010473; GTPase-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; SSF48371; 1.
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
//
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