FORH_DICDI
ID FORH_DICDI Reviewed; 1087 AA.
AC Q54N00; Q5TJB8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Formin-H;
DE AltName: Full=Diaphanous-related formin dia2;
DE Short=dDia2;
GN Name=forH; Synonyms=dia2, drf2; ORFNames=DDB_G0285589;
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], SUBCELLULAR LOCATION, AND INTERACTION WITH PROB
RP AND RAC1A.
RC STRAIN=AX2;
RX PubMed=15908944; DOI=10.1038/ncb1266;
RA Schirenbeck A., Bretschneider T., Arasada R., Schleicher M., Faix J.;
RT "The Diaphanous-related formin dDia2 is required for the formation and
RT maintenance of filopodia.";
RL Nat. Cell Biol. 7:619-625(2005).
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 INTERACTION WITH VASP.
RC STRAIN=AX2;
RX PubMed=16675552; DOI=10.1073/pnas.0511243103;
RA Schirenbeck A., Arasada R., Bretschneider T., Stradal T.E.B.,
RA Schleicher M., Faix J.;
RT "The bundling activity of vasodilator-stimulated phosphoprotein is required
RT for filopodium formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7694-7699(2006).
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. Important for cell migration
CC and formation, elongation and maintenance of filopodia. Specifically
CC controls filopodial dynamics by regulating actin turnover at the barbed
CC ends of actin filaments.
CC -!- SUBUNIT: Interacts with vasP, proB/profilin-2 and rac1A. Interacts (via
CC GBD/FH3 domain) with activated Rho-GTPases.
CC {ECO:0000269|PubMed:15908944, ECO:0000269|PubMed:16675552,
CC ECO:0000269|PubMed:16762450}.
CC -!- INTERACTION:
CC Q54N00; P34144: rac1A; NbExp=2; IntAct=EBI-1808560, EBI-1808643;
CC Q54N00; Q5TJ65: vasp; NbExp=2; IntAct=EBI-1808560, EBI-1808546;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:15908944}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15908944}. Note=Enriched at the tips of filopodia.
CC The N-terminus of the protein targets the protein to the cell cortex
CC and the FH1/FH2 region refines the localization specifically to
CC filopodial tips.
CC -!- DEVELOPMENTAL STAGE: Expression is kept at constant levels after the
CC onset of development. During sexual development, displays a significant
CC increase in fusion competent cells. {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; AJ748258; CAG38079.1; -; mRNA.
DR EMBL; AAFI02000079; EAL64632.1; -; Genomic_DNA.
DR RefSeq; XP_638143.1; XM_633051.1.
DR AlphaFoldDB; Q54N00; -.
DR SMR; Q54N00; -.
DR DIP; DIP-46561N; -.
DR IntAct; Q54N00; 3.
DR STRING; 44689.DDB0231180; -.
DR PaxDb; Q54N00; -.
DR PRIDE; Q54N00; -.
DR EnsemblProtists; EAL64632; EAL64632; DDB_G0285589.
DR GeneID; 8625191; -.
DR KEGG; ddi:DDB_G0285589; -.
DR dictyBase; DDB_G0285589; forH.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_002356_1_0_1; -.
DR InParanoid; Q54N00; -.
DR OMA; MMPGFSP; -.
DR PhylomeDB; Q54N00; -.
DR PRO; PR:Q54N00; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031254; C:cell trailing edge; IDA:dictyBase.
DR GO; GO:0030175; C:filopodium; IDA:dictyBase.
DR GO; GO:0032433; C:filopodium tip; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0005522; F:profilin binding; IPI:dictyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:dictyBase.
DR GO; GO:0070060; P:'de novo' actin filament nucleation; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR GO; GO:0045010; P:actin nucleation; IDA:dictyBase.
DR GO; GO:0051638; P:barbed-end actin filament uncapping; IDA:dictyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IGI:dictyBase.
DR GO; GO:0046847; P:filopodium assembly; IMP:dictyBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:dictyBase.
DR GO; GO:0031268; P:pseudopodium organization; 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; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
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; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..1087
FT /note="Formin-H"
FT /id="PRO_0000327695"
FT DOMAIN 34..394
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 589..615
FT /note="FH1"
FT DOMAIN 623..1016
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1013..1051
FT /note="DAD"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 433..461
FT /evidence="ECO:0000255"
FT COMPBIAS 416..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 497
FT /note="G -> R (in Ref. 1; CAG38079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1087 AA; 121580 MW; F92BADEE145E0BD9 CRC64;
MSFDLESNSS GGSTIGRNSS IRLSSGLAPS ESTVSLNEII DLDREFELLL DKLAIEDPIK
RKQMQSLPDI SKRTLLEQNK ADIYRTVKHK GPIESFADVK SVISSINTKH VPIDIIKTLR
IHLNTADRDW IQSFLDNDGV QPILNILKRL ERNKNRKRKE HSILQWECTR CIAALMKIKI
GMEYIASFPQ TTNLMVLCLD TPLIKAKTLV LELLAAIAVT DRGHGAVLTS MIYHKEVKKE
ITRYFNLVQS LKIEKNAEYL TTCMSFINCI ISSPSDLPSR IEIRKAFLNL KILKYIENLR
ADYNEDKNLL TQLDVFEEEL STDEQLNSQQ GTQIGIEDLF SQISSRVTGT PSQQELITLM
THFQRMSSSN LGLGVWTLYN ALANQLEDEL KIHPDLDVTL VSLLFPEVKK SSSGLFGFGS
KSKSPSSSPA LSSMAKTELK KDNEEKQKTI EHLLKQLNKF SGGQNTERWM IEREEKNKLI
AQLMAQTKNG GGGGGGGVGG DSSLSNDEAL KRENQLLRME IENIKNNPSV LLNSGNSING
DVPNLFISSP GSTLSPSPSG EPPIPSTDFG ITSSSIHTST DKLTNSTEPI LGSPPPPPPP
PMSGGGGPPP PPPPPGGKSN KPAKPIIKPS VKMRNFNWIT IPALKVQGTF WDKLDETSFI
QSLDKVELES LFSAKAPTVK VESKQLTRKV VVTVIDMKKA NNCAIMLQHF KIPNEQLKKM
QIMLDEKHFS QENAIYLLQF APTKEDIEAI KEYQGDQMQL GAAEQYMLTV MDIPKLDSRL
KAFIFKQKFE GLVEDLVPDI KAIKAASLEL KKSKRLSDIL KFILAIGNYV NGSTTRGGAF
GFKVLETLPK MRDARSNDNK LSLLHFLAKT LQDRIPEIWN IGAELPHIEH ASEVSLNNII
SDSSEIKRSI DLIERDFVPM INDPLFAHDK HWIHKITEFQ KIAKVQYQRI EKEIDEMNKA
FEEITSYFGE PKSTQPDVFF STINNFLEDL EKAYGEYQAM IRKAELENSK MEDPEKGGLQ
DLSSQIRSGQ LFKDRRVGDS VIAQMQNVDS LRKNLKSTST TTPNTPPTIK IELPSQSILK
PSGQLKK
