ID FORJ_DICDI Reviewed; 2546 AA.
AC Q54ER5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Formin-J;
GN Name=forJ; ORFNames=DDB_G0291378;
OS Dictyostelium discoideum (Social amoeba).
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 -!- 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; AAFI02000177; EAL61673.1; -; Genomic_DNA.
DR RefSeq; XP_635175.1; XM_630083.1.
DR AlphaFoldDB; Q54ER5; -.
DR SMR; Q54ER5; -.
DR STRING; 44689.Q54ER5; -.
DR PaxDb; 44689-DDB0231633; -.
DR EnsemblProtists; EAL61673; EAL61673; DDB_G0291378.
DR GeneID; 8628121; -.
DR KEGG; ddi:DDB_G0291378; -.
DR dictyBase; DDB_G0291378; forJ.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_228212_0_0_1; -.
DR InParanoid; Q54ER5; -.
DR OMA; WVIDCLT; -.
DR PRO; PR:Q54ER5; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005522; F:profilin binding; ISS:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IEA:UniProt.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR000253; FHA_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR45733; FORMIN-J; 1.
DR PANTHER; PTHR45733:SF8; FORMIN-J; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Coiled coil; Reference proteome.
FT CHAIN 1..2546
FT /note="Formin-J"
FT /id="PRO_0000363921"
FT DOMAIN 391..444
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 457..963
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 1072..1098
FT /note="FH1"
FT DOMAIN 1106..1495
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1563..1593
FT /note="DAD"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2014..2033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2121..2369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2381..2473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2485..2510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2067..2118
FT /evidence="ECO:0000255"
FT COMPBIAS 987..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1045
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1099
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1728..1775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1840..1862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2121..2179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2189..2291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2298..2328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2354..2369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2390..2443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2454..2473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2485..2509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2546 AA; 279879 MW; 144C32ABB6688651 CRC64;
MEENTNNIDN GHMGDNNNEN NNNSNNNNNN NSNSSSSFVK GRIDSLNKST NGLIKIGRSV
ENSNNSITSG GSSSNSGEIS SNNNNNNNNN GILKNSTSGS KDNTPLSESS INLRSIKTSG
ENKLNSSSSS NSNNNNIGVI NKGVSTNLKS IMNALSSKSS ENLSNFNNNN SLSSSPLKEN
QLVKSFDKNI TPSKNNSPRA HLNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNTTP
TLNSPRNKNS IYNTNSNNNS NTTNSTPNSA ITPNIIVENK IKEKIQLWGM LKSNCKKYKD
MELNQIETSF GRGSADYNFD DEKVVSSNHF KIILHKTVLP YGISNGSLNN SPKPLSTIIP
SSNTITTATT NNNNDNAESL TTYSESSEIS TDSTGVCSSS SSTSSTLSSK SSSSSSFNKF
MEFLLIYIED NDSTNGTWVN GNKLNRGERV QLDDKSKITL STPDFSSLSF TFESNISSLS
DEEKGKLLKA IVILKDSLDD STNSFGSSTT TTISGGGSGS SSVNSSGGGS GTTPINVTPN
SSNVSVTKKV INRTPSFKMS NLSTKPEGFV SILKNEPTLK NIQLLLSTIK TSDDQWKENF
IQTDCILMIV DLLSSNYKKL RYNEIDQAID IECLSILSTI FTCSKSNQNA LKQLSKSNEL
NFNDIFMLFL LNQQNSNHSV KTKSQFLQFL NSITSNEICH KMIISSIEKI HSIKKDKLKF
KWLVESMVFE SDFQYKLQSL TLINSLLSNC KNQTTLTKIK SDLQSLGIGK INDLLVLDSS
IKEMSIQLTK FNNNFNSSSS SSSISSNSIN NSQNNNNNNN NNNNTNNNNN NNSNNNNINN
NNNNLNTRKN NFNCKTLNLK DPISLVLLLQ NELKSNFSTS VPTSPTSKNP LITSNNNNTS
IGNNSNNIIT SILTDLYKIA NNNNNNNNNT NNKPKMDSNS ALTLLSDFSK IISSSISNEQ
EYQKSIPVLE EKIKILIPSF NNTCNNTTNN NSSAKNIEVD SSVNKSPNTE EDSTKKTINN
SPAEDAQIVS ASVPPPPPPP PGGNNNNESD VPSSSGGPPP PPPPPPPPGK SSGGGPPPPP
PPPPKGGKGG PPPPPPIGGI GSKVVKVKEE QPSVPMKQLF WSKVPVAKTK KTIWENKSDK
FELDKIQIEQ LFCQKKPANG KGSPKDGIEK EKEEKLELLD PRRSYAVSIL ISKYKLTPIW
VIDCLTSMDD KKLSKDMVRV LLHIVATNEE EEQFKKYEGD KSQLSDVDQF IIETLKVPKI
RQRLECIEYK IQFESTLQEL VLNAKCVQQV STSIMSSTSF HGLLHFILRI GNYMNAGSSR
GNAEGFKLGF LLTVGNTKSL DNKTSLLNYI IQFISEKYPQ FLITKSTIPH LEQASRILWS
EMLSQFEQLK SGMSMVQKEL ELQIKQIGSD NFTHKFKKFT SSKAEHLDSL QIFIKQVEET
YQSTIAYFCE ENIQPEEFFQ IIFNFINLVL KVHKENEDIR IAALPKSKKY QEQQNKPTQN
NDHSTKSKLS NLPSSSSIND ESSSSASLSS LSTNVNANTE NDNLELSKLG FLSKLRKKRS
KSEQEPVVEP IQITPKVGSA ASAEPSPSIK SRDKKESFKS PIFRSPKFKV SSISPKLKAT
LNSISKTLRK QQVESPSPNM SPFTSTAISE KASIYDKNIN NIQPSSSSSS SSSSSSSSST
ITGKKSHNTE SEIKKEFISN SSMDKDKEKI KEKEKGTISK GKALLFGHSR SKSTTTSPSS
SSSKKQIPSL SECLQESNKT HSRSSSYSPN SKVNSQLMSN PFIMMEQKQP KDSLPIAKDS
KEIHNMGTTT TTTPIKVEKI VSVNEKPTIV TMQTKPIPLV PTTTTSTTTT TQTTPPPVTI
NEKEKETQSK EVITKDFRDI KLKQTGIIEE DRKIQQERQR QFKTFNGKLN STNKFRTSSS
AVFSRNKSLQ NINSTKNPSS VGFGDLDLFQ KENITINSIK QKLLLKQTQI RSTRTDSSRI
KKGKNVSQIV KQVENESPLP NPNKTLSAIR RHNSNLSRKS SKSSNNSSTS SLESLVQTNV
INGLNNLKSV SSSSSSSSSM VVNKNGIDDN QQKQQKQQQQ QQQQQQQQQQ LPQPQQQQQQ
QQQQQQQQQQ QQQQQQQQPQ QQSTTTTTIS THHPQLKQVQ PQSPSSLSQQ PTQQILKPAQ
PSSPLQSHYK PQQKPQTTYI PKPKPYIANP FPSSTTSTNS SPSNASDLTE VIKSTQSPFE
REQTFTKPTL QPVKYPSSAS SNSSSVSGSS QSTPLSAASL QPVGNRNLRK QHVTPPSSSI
SNSTATTKSK KEGNIRFVDQ ASPSSSSLEQ SSNASNAGYT SPPRENSFSN LFKKHKKSHS
KSKSTDNTLN GEIESVDENE KSRKKPKTVT KIIDFSKKLF SHKKSKSVDQ SSKSNNTNNN
NNNNNNNNNN NNNNNSNIDY NNSLNDVGSS SSFSSSSSSP TSNPFPIIQP PNQSPPTKNI
SSGNISNNTS YSSLGSMNGN NLVASPSSSI TSCKPSPGAV SSTSSTLKTP DFFDHKKVQT
PEQLGIKSTD IPKVIIIPPN FYQQPV
//
