ID   FORI_DICDI              Reviewed;         935 AA.
AC   Q54PI9;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Formin-I;
GN   Name=forI; ORFNames=DDB_G0284519;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
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   [2]
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   [3]
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   [4]
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   -!- DEVELOPMENTAL STAGE: Expression increases during transition to multi-
CC       cellular stages. During sexual development, displays a significant
CC       increase in fusion competent cells. {ECO:0000269|PubMed:15740615}.
CC   -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000066; EAL65186.1; -; Genomic_DNA.
DR   RefSeq; XP_638543.1; XM_633451.1.
DR   AlphaFoldDB; Q54PI9; -.
DR   SMR; Q54PI9; -.
DR   STRING; 44689.DDB0231631; -.
DR   PaxDb; Q54PI9; -.
DR   EnsemblProtists; EAL65186; EAL65186; DDB_G0284519.
DR   GeneID; 8624636; -.
DR   KEGG; ddi:DDB_G0284519; -.
DR   dictyBase; DDB_G0284519; forI.
DR   eggNOG; KOG1923; Eukaryota.
DR   HOGENOM; CLU_313406_0_0_1; -.
DR   InParanoid; Q54PI9; -.
DR   OMA; KKMRQLH; -.
DR   PRO; PR:Q54PI9; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005522; F:profilin binding; ISS:dictyBase.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   Gene3D; 1.20.58.2220; -; 1.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   PROSITE; PS51444; FH2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Coiled coil; Reference proteome.
FT   CHAIN           1..935
FT                   /note="Formin-I"
FT                   /id="PRO_0000363920"
FT   DOMAIN          444..505
FT                   /note="FH1"
FT   DOMAIN          506..935
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   REGION          52..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          35..76
FT                   /evidence="ECO:0000255"
FT   COILED          702..730
FT                   /evidence="ECO:0000255"
FT   COILED          803..834
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        380..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..484
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   935 AA;  106462 MW;  F061ACBD34BA9503 CRC64;
     MHDIDVAIQI NMLFLPPTNE LIRVDSNSKQ LNQPQQQQQQ QQQQINNENE NSINNQENKE
     NNNKDNNNNN NKEIKQSSEW GSKFSSLFSN MTKKKKSNFD LEMDAIKDAF LLNKPINNEE
     GLLIYSLDKS KKYIHSLSEL DIGYVYLTEK ETPIIRQNED EVILANKVII QANTMKRFSI
     KGILQSDVTT NALEIFTKRK MSQGVLFLEE DGSLCRIFYK IQDLITDTIY CNQDDTVMLQ
     KLPNNEGIRF RFRGSFNREQ VQQAMLAFSQ PSDPQTWKRT IILREQQHHS SQSFTGDSVA
     SRFLNKLSSK TKEDEESNDL KTKRENTVLK LKNRMKIDWD WKYTSTSVPI DQEPPTFIDN
     MVNRVREKIS GSNNKLSDLL SSAKKQPQQQ PQKDVTSSSS SSSNSSSPYL DSVDKLVITT
     NDSSSSNPLP DFDKLSLSSD DKVNNNNVQI ENTTPSVPPP PPVGAPPPPP PPPPPPPPPP
     PSTLKLNRNR ISTPKKPNNS GGGGGGGQLT PLQKKMRQLH WNAIPREKLK ETFWDNLSPV
     KGNDNDQTLV ESWFSLSPMA KEKMSKENLN NSNNNNNNNS NNNGEEQSLS DSGNTIVISK
     IIILDLRRSN NICILLSQFK LSYGAIKEAI LCFEDGKLSV EQLIALDAML PISEEEYQSL
     SSANYQSIEQ LGNAERFLIE MMSIQHLQQR VQTYLFKLEV CSLLDSIEIN NNQLSKAIEQ
     LRNSRKFIKV LKVIFHIGSI LNRGTYLNST KGFKLDSLSK LSETKSKDQK HTVVDFIEIY
     IRENQPELLN FYSELDLLDK IPQSSLENIL EESNEIENKF KQVDQEIQYH QQLLTNDNNN
     TLSSSSSSSY DQSKDTYLKV MSPFYDTFNT RFITIKQSTQ QTLKQFQECC IYFGEDPQNI
     TSKDFFSNIV KFSIAFKSSS NNAKKSLNLS TLNSK