FORA_DICDI
ID FORA_DICDI Reviewed; 1218 AA.
AC Q54WH2; Q8IU42;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Formin-A;
GN Name=forA; ORFNames=DDB_G0279607;
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], AND DISRUPTION PHENOTYPE.
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 {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; AB082542; BAC16796.1; -; mRNA.
DR EMBL; AAFI02000032; EAL67578.1; -; Genomic_DNA.
DR RefSeq; XP_641581.1; XM_636489.1.
DR AlphaFoldDB; Q54WH2; -.
DR SMR; Q54WH2; -.
DR STRING; 44689.DDB0214996; -.
DR PaxDb; Q54WH2; -.
DR EnsemblProtists; EAL67578; EAL67578; DDB_G0279607.
DR GeneID; 8622155; -.
DR KEGG; ddi:DDB_G0279607; -.
DR dictyBase; DDB_G0279607; forA.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_269012_0_0_1; -.
DR InParanoid; Q54WH2; -.
DR OMA; ELANFWH; -.
DR PhylomeDB; Q54WH2; -.
DR PRO; PR:Q54WH2; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0032154; C:cleavage furrow; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:dictyBase.
DR GO; GO:0005522; F:profilin binding; IBA:GO_Central.
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; IDA:dictyBase.
DR GO; GO:0045010; P:actin nucleation; IDA:dictyBase.
DR GO; GO:0016477; P:cell migration; IMP:dictyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:1904171; P:negative regulation of bleb assembly; IMP:dictyBase.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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; PF00168; C2; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00239; C2; 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; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 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..1218
FT /note="Formin-A"
FT /id="PRO_0000363913"
FT DOMAIN 1..108
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 139..539
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 652..737
FT /note="FH1"
FT DOMAIN 759..1155
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1174..1209
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 634..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 563..638
FT /evidence="ECO:0000255"
FT COILED 1034..1061
FT /evidence="ECO:0000255"
FT COMPBIAS 646..751
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 281..284
FT /note="NKKS -> QQKD (in Ref. 1; BAC16796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1218 AA; 135329 MW; EC21EA1D40053AF1 CRC64;
MADKLYQIKL DIKKGKNIVG SDGSVCSPYL RVTWGGKKQQ KTKVITKSAE PEWNFSCLLE
IKKEKNPQKP GLEFELIEHK QFSEKEISST TYQLPESLIL GEACNYSVPM SIATSKGDQK
CEILIAITAI NFGKDKQDEE KKRHDEIQKK FAQLVEQLAT DSKAREGMMK LPYEARAQLV
EQHRDKLANE KHPDEYVVLL IKEITRKNIQ LAGGLQKSHS ASNASLGSLS PVTPRVDDGL
SVAELKNISV ALRSRGLDWI HQFHKLGATT RLVELLSLYV NKKSHTEESL QKQLECLNCI
KNLMNNNVGI GYIFGIKDSF KTIVLCLGSE YEKVNELAIG LLNTICFLPK INGHKLLIEL
LNYFKEEKKE SRRFISIVKS LKSKAGVIET KETLKTKSIY LSFINIIVNT PAEIDLRLAL
RQEFYWLGIK EILVKLSNYT YDESPELDTQ ITVFEEEESK DNKEMSERFQ EFKGLNLDNV
DDVLKTLMDR IRPKGLVDCM REISKDLLLL PIDDDVGIRN WVLASRIIKQ ISLRDKNIGI
DEDILPLENL LLMCEQEAKE VPLKSQIESL KKDAQDLAKK ITTQDIELKE KVEIIKKNEE
LTTKQLEEQI NIAKKKDEEI NQLKALVEQL KLTQGTAKPD SAAASTSVAP PPPPPPMTGG
GAPPPPPPPP PMTGGGGPPP PPPPPPMTGG GPPPPPPPPP MTGGGPPPPP PPPGGGPPPP
PPPPGAKAGG PPPPPPPFGK GPPPPPGGFG MKKAAAPPRK EVPVPALKMK GLQWVSLNDK
KIQGTIFSKF NLDTSKDINL DYKDIEGVFA AKVIEKKEST APKKTGPVSI IDPKTSQNLS
IFLSQFKGKS YDDICGAISK GDETVFQPNH IDALIGFLPS EDDINNINEF LREEKDITKL
GPPEQFSMKI HSVPQVKARL QAMKFKYAYE SKKSDLKVDI DNFKQGTQEI KGSEKIPKLL
EVILILGNFI NGGTARGNAY GFKLNTITKL ADTKSTDNKL SLVNYLTRVV IKDFPHLNSF
AQDLGHVEAA GRVSLSQVQA EVATLRKEFV QVQKSIETLN SGTGEEAVDP FKVKYEEFCT
QTAEDIDLIT SSSQQIETDY KDLLAMFGED SKSEPSEFFG MFTKFMDQYD KATKENEQLS
IQAEKIAKRE AAKKLKEEED AKKKQLAEER KQKGETVEVK ESVVDDLLDT IASGDAFKNR
RRRARKTDQD STIEPIDL
