FORC_DICDI
ID FORC_DICDI Reviewed; 1158 AA.
AC Q54KF1; Q8IU40;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Formin-C;
GN Name=forC; ORFNames=DDB_G0287295;
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, FUNCTION, AND SUBCELLULAR
RP LOCATION.
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:0000269|PubMed:12538772}.
CC -!- SUBUNIT: Interacts (via GBD/FH3 domain) with activated Rho-GTPases.
CC {ECO:0000269|PubMed:16762450}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12538772}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12538772}. Note=Found
CC localized to the crowns, which are macropinocytotic cups rich in F-
CC actin.
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 -!- DISRUPTION PHENOTYPE: Null cells grow normally during the vegetative
CC phase and, when starved, migrate normally and form tight aggregates.
CC Subsequently, however, null cells make aberrant fruiting bodies with
CC short stalks and sori that remain unlifted. Aggregates are also unable
CC to migrate as slugs, suggesting it is involved in mediating cell
CC movement during multicellular stages of Dictyostelium development.
CC {ECO:0000269|PubMed:12538772}.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000305}.
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DR EMBL; AB082544; BAC16798.1; -; Genomic_DNA.
DR EMBL; AAFI02000100; EAL63715.1; -; Genomic_DNA.
DR RefSeq; XP_637272.1; XM_632180.1.
DR PDB; 2L1A; NMR; -; A=1-100.
DR PDBsum; 2L1A; -.
DR AlphaFoldDB; Q54KF1; -.
DR BMRB; Q54KF1; -.
DR SMR; Q54KF1; -.
DR STRING; 44689.DDB0191362; -.
DR PaxDb; Q54KF1; -.
DR EnsemblProtists; EAL63715; EAL63715; DDB_G0287295.
DR GeneID; 8626103; -.
DR KEGG; ddi:DDB_G0287295; -.
DR dictyBase; DDB_G0287295; forC.
DR eggNOG; KOG1922; Eukaryota.
DR eggNOG; KOG1925; Eukaryota.
DR HOGENOM; CLU_287208_0_0_1; -.
DR InParanoid; Q54KF1; -.
DR OMA; PERWCLM; -.
DR PRO; PR:Q54KF1; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005911; C:cell-cell junction; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0044354; C:macropinosome; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0010467; P:gene expression; IDA:dictyBase.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
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; IPR024574; ELMO_ARM.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR014768; GBD/FH3_dom.
DR Pfam; PF11841; DUF3361; 1.
DR Pfam; PF02181; FH2; 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 3D-structure; Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..1158
FT /note="Formin-C"
FT /id="PRO_0000363915"
FT DOMAIN 20..388
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 601..998
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1134..1158
FT /note="DAD"
FT REGION 8..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 479..515
FT /evidence="ECO:0000255"
FT COMPBIAS 10..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 334
FT /note="L -> S (in Ref. 1; BAC16798)"
FT /evidence="ECO:0000305"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:2L1A"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2L1A"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2L1A"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2L1A"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2L1A"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:2L1A"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:2L1A"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2L1A"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2L1A"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:2L1A"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2L1A"
SQ SEQUENCE 1158 AA; 131001 MW; BEFFC76EFBC6823C CRC64;
MKIRVELING NEHRTSSTPQ QPQQNPSVSH IFDGETAVKD HIKVLLTHFK IPVDKVSSYA
LQNPFTLAYV EDSFLTPERL VEAEKSYFIL RMKPHAIADR VVDQLTKIEP TSPHIKDTIF
NIRYQMKDVE YVEEFIIKGG INQLLAVIIK SRGNTQSYAL TALRCFMGYN SGLEEVMSRP
QLIDKLYSLV CSVGVLPSVC RQAIELLFCV CNFDGFQLVH RSAKNHAQET STPAYSNLIT
LLSSGDMETQ LNTLTLFNCL LDNAPNPRKS EKLLSRWQQL GIIKILKSQE HVTHSDFRTQ
IARFQANSGF GIDGSGRKRT LTRQLSTQEL EFQLHQFREQ QPLISLLTSE LKFLRNAIKS
AIENGSYINY RAPTERYDEY SQRKLEMIGD SPTNLQFLKR NDKFTNAFRK SMYVRSPNTS
DLFDSSTLED TYDGNNDTNS CTSISTSSTP IHISQPTTLI VPSTTPNHPP QQSQQTPPLQ
LQKEKEKEKE KEKEKEKEKE KEQQQQQQQS NKQSTPKPNL SCLLSPITIS NTLNNNNNNN
NNTNNNIIKS NNNNNNNNCT IKDLSPIVKS EKSNEDEIHE ISLNGASSNH EEPIKYKLQP
TKSPITPSKR MKPLHWTRIL NSQFEGKKTI WNSYLPEVTF EEELFVDLFS LYTERIVSFS
GSPVGSGTSI SGGGPIKSKP IQKVISVLSQ KRSNAIIVMC GKLPSDDILI RAIRNLDSNK
LSLDGVSSII SNFPTSEELA SIHELHSNEV ILDKPERWCL MIDGFPMIKH RLRCWEFMLK
IEDSLKSIIE SIDTVLLACK ELRTSITINC LFSLLLQLGN YLNGGHLYRG QSDGFNLESL
SKMIEIKDNS NSGSLLDFAI KTLYQQSPMK GNSNTSIHLE LAHVPNASLI NFTDVGTSVS
KLLQDYSEIV LMSDEIQQTT DKDDPFLDIV PKFMGTILLI LKNLQTKFLE TEKYLFETID
YFNPTNQTLQ QYQQQQYQQY QQQQFQQNII NNNNNNNNNN SNNNNNNISG NTTTTTTTTT
TTTTGSIINN NNNNNNNNNN SNNNIINNNN SQSNLQSLLH PQYYLSNSSS SSSSSYKITP
PLSSSLSITS QEWNQQKFTC EKFFTLFSTI TTAFKKSPSK RLSQKGFGLK ISNSDDPMAV
IIEALKTGSP NDMVKRAF
