FORB_DICDI
ID FORB_DICDI Reviewed; 1126 AA.
AC Q54SP2; Q8IU41;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Formin-B;
GN Name=forB; ORFNames=DDB_G0282297;
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], DISRUPTION PHENOTYPE, AND INTERACTION WITH PFYA
RP AND PFYB.
RX PubMed=12538772; DOI=10.1242/jcs.00265;
RA Kitayama C., Uyeda T.Q.P.;
RT "ForC, a novel type of formin family protein lacking an FH1 domain, is
RT involved in multicellular development in Dictyostelium discoideum.";
RL J. Cell Sci. 116:711-723(2003).
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 Interacts with pfyA and pfyB. {ECO:0000269|PubMed:12538772,
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 -!- DISRUPTION PHENOTYPE: No visible phenotype. ForA and forB double null
CC cells also show no phenotype. {ECO:0000269|PubMed:12538772}.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000305}.
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DR EMBL; AB082543; BAC16797.1; -; Genomic_DNA.
DR EMBL; AAFI02000047; EAL66270.1; -; Genomic_DNA.
DR RefSeq; XP_640259.1; XM_635167.1.
DR AlphaFoldDB; Q54SP2; -.
DR SMR; Q54SP2; -.
DR STRING; 44689.DDB0215000; -.
DR PaxDb; Q54SP2; -.
DR EnsemblProtists; EAL66270; EAL66270; DDB_G0282297.
DR GeneID; 8623518; -.
DR KEGG; ddi:DDB_G0282297; -.
DR dictyBase; DDB_G0282297; forB.
DR eggNOG; KOG1922; Eukaryota.
DR eggNOG; KOG1923; Eukaryota.
DR HOGENOM; CLU_279717_0_0_1; -.
DR InParanoid; Q54SP2; -.
DR OMA; HSERTRF; -.
DR PhylomeDB; Q54SP2; -.
DR PRO; PR:Q54SP2; -.
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; IPR014767; DAD_dom.
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; PS51231; DAD; 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..1126
FT /note="Formin-B"
FT /id="PRO_0000363914"
FT DOMAIN 38..406
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 527..611
FT /note="FH1"
FT DOMAIN 612..1011
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1071..1100
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 463..514
FT /evidence="ECO:0000255"
FT COILED 980..1010
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..612
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 240
FT /note="K -> N (in Ref. 1; BAC16797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1126 AA; 123608 MW; CC7EE3BC1C07573C CRC64;
MFFKGKKKDK EKEKSHGNIG NVISVENKTG SQSNLHVEQN LSNEDLKIQF SQLLYELGVP
EAKRVEMELW SNDKKWMLLV QNKDKIKENE EKMKQKGSLY ETPQFYLSLL RENASIQKTI
SDLKVSLASN KLSWIDSFIG LSGFDEILKI FQTFQLKPEK NSIDFLILFD CVNIIKSILN
SQSGVKSVMT TSHTFKVLVL CLDQSYPPEL RNAVLQLTAA LTLLPTVGHS YVLEAIENFK
VSNREKVRFQ TIIEGAKSVS NTQLHYEYLT SFMNLVNSIV NSPADLQVRI GLRSEFTALK
LIELISNSKG VSEDLDTQIN LFFECMEEDN DEVGAHYKEV NIRSPSEVST KIDTLLQSHP
ALHHHFISII KGLYTLASTQ SDLGGSMWNI LDESVGLILK DPSKESQLEK LQNENNNLKL
QLSEIKLNNS NNNNNNNNSN NNNNDSNVST PNINTGSPLL PPQQYQDLEQ KLQLTQNEKN
ESQNKVKQLE SEIKGLNSTL TGLQLKVTKL EADLLSVSVT TPPSDTNGTT SPPIEAPSSP
SLGAPPPPPP PPPAPPVSGG GPPPPPPPPP PSSGGGPPPP PPPPSSGGPP PPPPPPGGMK
KPGAPAVPNL PPKKSSVPSV KMVGLQWKKV NNNVIENSIW MNVKDYNLND QFKQLEELFQ
VKKPTATTPT APVGGASNVA VGGGSGSKSI VSTPTISILD PKRSQAIMIM LSRFKISFPD
LSKAITNLDE SKLNLEDAKS LLKFVPSSEE IELLKEEDPS CFGKPEQFLW ELSKINRISE
KLECFIFKQK LSTQIEELTP DINALLKGSM ETKNNKSFHQ ILEIVLSLGN FINGGTPRGD
IYGFKLDSLS GLLDCRSPSD SKVTLMTWLI QFLENKHPSL LEFHQEFTAI DEAKRVSIQN
LRSEVASLKK GLTLLTNEVE KSEGASKTIL SGFVGKSTDA VTLIEKQFNT ALESFNSTVQ
FYGEDVKTSS PEEFFQHVSK FKNEFKRTIE SIQKERENVQ KLAARKKAAA SGPSVPSASG
SSINIAPKSG VSPITPTSKS SISISQKPPQ STQPSISVQQ QQQQHHGDDD DDIPQNGTFM
DQLMSKMKGG EAIRASRRAS QYVFTQNGAG GVGAIDALNA ALKNKK
