FORE_DICDI
ID FORE_DICDI Reviewed; 1561 AA.
AC Q5TJ57; Q55DK4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Formin-E;
DE AltName: Full=Diaphanous-related formin dia3;
GN Name=forE; Synonyms=dia3, drf3; ORFNames=DDB_G0269626;
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;
RA Nagendran R., Schleicher M., Faix J.;
RT "The Diaphanous-related formin dDia3 regulates actin cytoskeleton-plasma
RT membrane interaction in Dictyostelium discoideum.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 decreases 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; AJ812236; CAH23233.1; -; mRNA.
DR EMBL; AAFI02000005; EAL72163.1; -; Genomic_DNA.
DR RefSeq; XP_646127.1; XM_641035.1.
DR AlphaFoldDB; Q5TJ57; -.
DR SMR; Q5TJ57; -.
DR STRING; 44689.DDB0231181; -.
DR PaxDb; Q5TJ57; -.
DR EnsemblProtists; EAL72163; EAL72163; DDB_G0269626.
DR GeneID; 8617076; -.
DR KEGG; ddi:DDB_G0269626; -.
DR dictyBase; DDB_G0269626; forE.
DR eggNOG; KOG1922; Eukaryota.
DR eggNOG; KOG1924; Eukaryota.
DR HOGENOM; CLU_245935_0_0_1; -.
DR InParanoid; Q5TJ57; -.
DR OMA; IFEMEDM; -.
DR PhylomeDB; Q5TJ57; -.
DR PRO; PR:Q5TJ57; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031254; C:cell trailing edge; IDA:dictyBase.
DR GO; GO:0032433; C:filopodium tip; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005522; F:profilin binding; ISS: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; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IGI:dictyBase.
DR CDD; cd00029; C1; 1.
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; IPR046349; C1-like_sf.
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 InterPro; IPR002219; PE/DAG-bd.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Coiled coil; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..1561
FT /note="Formin-E"
FT /id="PRO_0000363917"
FT DOMAIN 581..929
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 1019..1081
FT /note="FH1"
FT DOMAIN 1086..1475
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1488..1518
FT /note="DAD"
FT ZN_FING 379..427
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1526..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..85
FT /evidence="ECO:0000255"
FT COILED 158..208
FT /evidence="ECO:0000255"
FT COILED 541..573
FT /evidence="ECO:0000255"
FT COILED 952..989
FT /evidence="ECO:0000255"
FT COILED 1398..1491
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1092
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1561 AA; 174238 MW; 935F93B3ACEF4782 CRC64;
MDNHSSSSNP SSLSSSSSSS SSSSSFLSDH VKKEEQNGLD TIKEEIENKI ENEEEEEKIE
EKPIEKVEEE KIIVQKEEEE KIEEEPIEKE EEKKVEEEKF EQDNINTTVE AKTLETSTEP
IATEVVDEKS ITSNNENLEE QQKEDVISIP PPQQEQQEQQ EQQEKQKEET KPSIREEVKE
KIKGKLSEIK EEIKDIKEEI KHVIREEVTE PIIVVENNNS PPPPPPPPSI TVQSSSPVSS
QISSPVSSPV SSPKPSVTFN EDGRKRKEGG ITASISSEDI MALSSSTSTN NKGIPKENKR
TASTILRSKS SPNPGANNPN HNKDGNNSSS SSSSNNNSDN NNNSDNNSNN NNINNNNSSS
NNLNYDSSDI DTEAIPKFYH DFKIHRGTSS CVYCGENTRL WSTSYKCFFC GVVCHKKCLD
SMNTIPCSSA IHNIKGKNRS QTISGYAPPN SLALQAPPYI SVAKPSSITN SSSKSTPSLL
SAPPSQSNSN NSSPNISSKS NPNSPITTSA TTTTTTATIS SLSPTSISSP PIASEQPPSP
LLQQQQQQQQ QQQQQQQQQQ QQQQQQQQIS TTQLQDLNNT SEKPDDDMIN LMFDTLMVDL
DLNLPASKLS TTQKWLLLEQ KFKLKKDELL PEYFINALKE QPSKSIFQSL VVILRTNVTK
NWMCSFVQLN GVEILFEILS KSKRKDYKDD CLSCIGKVMS NPIGLNSVAQ LPMAPKTITK
VLRSKQYCIK SKAMAIELLT VMLLDKYVPG GCSLVLKALT KTKEKKRFSF FVRFIKDNES
LELKTKALCF INVLIFEMED MNVRVNIRSE FLRLGLYTYL REIKKTITHE KTLFTQIEIF
EEMMNEDTQE LDLRLEDLKR QLGIDIDDVD QVFKALKNTT SKSGLNRQLL NILQNLLVIK
ACDPTDGVKY FILCDTLVKQ ISLHKGGFED PSNFDFRGLM VGLESATAEV TLNRKLGELE
KQNIDKAMKI QEQDINIKSL LDLLKQLKDG GTAPDASMIK KIEEMIKQME PPPPPISVKS
PDDPNNAAPI VVAPIPPPPP PISGAPPPPP PPPPPMKGGA GPPPPPPPPG KLGAKKPPAG
VQCRPPPKVP KPSHPLKAYQ WVKLAPVKVN DSLFDKLGPM NDINLPWNQI EEEFAAKVIV
REKKAIVKPK GPTQVIDPKL GQNISIFLSQ FKGVEPKQLI TYIQSMDESK MSRDQVKQIS
KLLPSREDLA ALKEFLQAED RSKLSIADQY CIDIGAFPFA SEKISMFLLK SELKSRLDEV
KPQIAAVSVA CDEVYKSKKL IRIIEIILVL GNFINYGTPR GDISGYKLDS LIKLSDTKSS
DLSSNLINTF VKYCQEKEPN LLTFADELPS LTTARKTIWS GVVADVSSIG RDVHSVKQIV
ETLQKSNEPF NQSIIDFLAT ASTEVEKLRK LLESTQENFK KLCKYFAEEE GKSQPEEFFD
IFGRFITLFE NATTQLQQQK EEQLKEEKRL QQKQQRQERA VRKLTTSNES ASASPNHAKS
TDDKSDEDDD IVNDLLMAVR DGDAFRQAKG RRRTTHQIAT SKMISNNLDP SKILPTSPNK
N
