FORD_DICDI
ID FORD_DICDI Reviewed; 1214 AA.
AC Q5TJ55; Q54SS9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Formin-D;
DE AltName: Full=Diaphanous-related formin dia4;
GN Name=forD; Synonyms=drf4; ORFNames=DDB_G0282245;
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 increases during transition to multi-
CC cellular stages, and levels remain constantly high throughout the rest
CC of 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; AJ812734; CAH25332.1; -; mRNA.
DR EMBL; AAFI02000046; EAL66328.1; -; Genomic_DNA.
DR RefSeq; XP_640306.1; XM_635214.1.
DR AlphaFoldDB; Q5TJ55; -.
DR SMR; Q5TJ55; -.
DR STRING; 44689.DDB0231188; -.
DR PaxDb; Q5TJ55; -.
DR PRIDE; Q5TJ55; -.
DR EnsemblProtists; EAL66328; EAL66328; DDB_G0282245.
DR GeneID; 8623482; -.
DR KEGG; ddi:DDB_G0282245; -.
DR dictyBase; DDB_G0282245; forD.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_269415_0_0_1; -.
DR InParanoid; Q5TJ55; -.
DR OMA; GNQPLKW; -.
DR PhylomeDB; Q5TJ55; -.
DR PRO; PR:Q5TJ55; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
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; 1.
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..1214
FT /note="Formin-D"
FT /id="PRO_0000363916"
FT DOMAIN 10..379
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 457..544
FT /note="FH1"
FT DOMAIN 562..1037
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1065..1095
FT /note="DAD"
FT REGION 462..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 401..448
FT /evidence="ECO:0000255"
FT COILED 1019..1056
FT /evidence="ECO:0000255"
FT COILED 1176..1207
FT /evidence="ECO:0000255"
FT COMPBIAS 462..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..558
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1214
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1214 AA; 137124 MW; C1C16F09ED22EA64 CRC64;
MVKLFGKSKK KEESPQSIDI AFQSILDEIG VVETEKKHLM ATMDTVRKQQ LIQSYSSKKF
SKNEFGNKSK KKSIITQSPH YFVDCLKNDP SKEVLTSLRV RLGNQPLKWL KEFLSLDGVS
LLIKVLILNE IKQVKNQEDI YKIAQCLHSL KLIMNTKFGL ESVIKQPTNI HSISLVMDTP
HLKTRIMVIE LLAALCVVNS KGLPLVLSAM DNYREVKREK KPFIHLFQGL KNPSGSLQAT
TFALINTLIS SSQSVEERQK IRNQFKKLGI TKVIEELEPE YANNPDLATQ KDLYEQECRW
DEQEQIENAR GDISDENPEA LVKAILDRTA GGPLYSSFTS ILRLLANSIT DQTKDQSLSN
YLFVEKVIGK MNNGESYLDD IGTFFGGGGG GDGSLDIAHV SGEKAVLIQK EIEDLKKQKK
RDQDKLAEKD KLLTKLAKRM RKMEEAIKLG KGLEYLNNQI EIESPPDSST STPQETTPGG
TKVPLKTSPV TKADLKHKLS TFTTAKAPNG VSDFLSGLDT TNQQGSTDAS QTEAGSGDGI
PLPPGAPPPP PPPGGKLAPS TPQLCSRPPS IKMKSYQWTR YRTRNVTNTF WKNVNLTKYN
DCLPHEQIEG LFGAAIFEKK EKELKKGSEV TVIDTKRAQN IGILLSRFKN VTHDAIYDAI
YSLDESILDL ETINQFIKYI PSKEEIDCII AFKQQQEQLP EEERMKLGKS EIFIDKISTI
PRLEQRIQAL HFKLNFPDKL YHAKPDIRKF NEAFVQLQNN NIFAIMELIL SIGNFINFGT
NRGNASGFKI DSINKMADTK SNIREKYTLV HYLIELLEST QPELLKVFDE IPSVVDAATL
SFNQSSSEIK LLRAGLIKLE KEIFVRQPKS VEPKPDDETI NNNGEDDINN TSSDEKTEGQ
QQRQGEEEEN DESESTGNSF ADSLKKKKSQ VNTNSTSDSK QSLEPLKDDD PLKLKLSEFL
LASKTELDDT ETLIAETEVL FKSICKFFGE DSTKIQPEEF LAIFKKFNDK FIMSKKDLEI
EKSIKDKSTQ RKNEKERKEM EIKKSKLEMI HSKLKKIGSP SSSNRILASN ESSPTSSTSS
VVHQHDDEDE ETIKEYINNP SPSQQSNSSE EEGMMDDLLN LIRDGNFREL RRMNLQQKKP
VRTKRVIAKQ PTRPQALDTP SSTYSSISSI YDAEPLDMSD QEDEDEEEEE DEEEEEEEEE
GDDDNDNDEE EGEN
