FOR3_SCHPO
ID FOR3_SCHPO Reviewed; 1461 AA.
AC O94532;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Formin-3;
GN Name=for3; ORFNames=SPCC895.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11696322; DOI=10.1016/s0960-9822(01)00525-5;
RA Feierbach B., Chang F.;
RT "Roles of the fission yeast formin for3p in cell polarity, actin cable
RT formation and symmetric cell division.";
RL Curr. Biol. 11:1656-1665(2001).
RN [3]
RP FUNCTION, INTERACTION WITH RHO3, AND SUBCELLULAR LOCATION.
RX PubMed=12415007; DOI=10.1242/jcs.00150;
RA Nakano K., Imai J., Arai R., Toh-e A., Matsui Y., Mabuchi I.;
RT "The small GTPase Rho3 and the diaphanous/formin For3 function in polarized
RT cell growth in fission yeast.";
RL J. Cell Sci. 115:4629-4639(2002).
RN [4]
RP FUNCTION, INTERACTION WITH TEA1 AND TEA4, AND SUBCELLULAR LOCATION.
RX PubMed=15809031; DOI=10.1016/j.devcel.2005.02.008;
RA Martin S.G., McDonald W.H., Yates J.R. III, Chang F.;
RT "Tea4p links microtubule plus ends with the formin for3p in the
RT establishment of cell polarity.";
RL Dev. Cell 8:479-491(2005).
RN [5]
RP INTERACTION WITH RAX2.
RX PubMed=17085965;
RA Choi E., Lee K., Song K.;
RT "Function of rax2p in the polarized growth of fission yeast.";
RL Mol. Cells 22:146-153(2006).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Involved in controlling polarized cell growth. Required for
CC interphase actin cable formation and microtubule organization.
CC {ECO:0000269|PubMed:11696322, ECO:0000269|PubMed:12415007,
CC ECO:0000269|PubMed:15809031}.
CC -!- SUBUNIT: Interacts with rax2, rho3 and tea4. Interacts with tea1 in the
CC presence of tea4. {ECO:0000269|PubMed:12415007,
CC ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:17085965}.
CC -!- INTERACTION:
CC O94532; O60132: tea4; NbExp=5; IntAct=EBI-1102572, EBI-1099982;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11696322,
CC ECO:0000269|PubMed:12415007, ECO:0000269|PubMed:15809031,
CC ECO:0000269|PubMed:16823372}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11696322, ECO:0000269|PubMed:12415007,
CC ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:16823372}. Note=Found
CC at the cell periphery and the growing tips of interphase cells.
CC Localized to the septum region during cell division and upon cell
CC division begins to localize to the new end, with some remaining at the
CC older end.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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DR EMBL; CU329672; CAA22841.1; -; Genomic_DNA.
DR PIR; T41643; T41643.
DR RefSeq; NP_588046.1; NM_001023038.2.
DR AlphaFoldDB; O94532; -.
DR SMR; O94532; -.
DR BioGRID; 276050; 64.
DR IntAct; O94532; 2.
DR STRING; 4896.SPCC895.05.1; -.
DR iPTMnet; O94532; -.
DR MaxQB; O94532; -.
DR PaxDb; O94532; -.
DR PRIDE; O94532; -.
DR EnsemblFungi; SPCC895.05.1; SPCC895.05.1:pep; SPCC895.05.
DR GeneID; 2539487; -.
DR KEGG; spo:SPCC895.05; -.
DR PomBase; SPCC895.05; for3.
DR VEuPathDB; FungiDB:SPCC895.05; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_254054_0_0_1; -.
DR InParanoid; O94532; -.
DR OMA; EKMSIFV; -.
DR PRO; PR:O94532; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:1902716; C:cell cortex of growing cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0036391; C:medial cortex septin ring; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISM:PomBase.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:PomBase.
DR GO; GO:0061572; P:actin filament bundle organization; IMP:PomBase.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0061245; P:establishment or maintenance of bipolar cell polarity; IMP:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IGI:PomBase.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; EXP:PomBase.
DR GO; GO:1904498; P:protein localization to mitotic actomyosin contractile ring; IMP:PomBase.
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; 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; 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; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Cell shape; Coiled coil;
KW Membrane; Reference proteome.
FT CHAIN 1..1461
FT /note="Formin-3"
FT /id="PRO_0000194904"
FT DOMAIN 92..508
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 845..1257
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..515
FT /note="Interaction with tea4"
FT REGION 431..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 540..639
FT /evidence="ECO:0000255"
FT COMPBIAS 1..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..786
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1461 AA; 166227 MW; C34E2C9672DA01CE CRC64;
MASKMPEGSP PTSRSIQSRN SSYSTSSNER IGTPSTISLS ENSDLSKLQS TNDFESREDL
SLTSDDNNDP EYVMCYNTVY HQKTKINDKL LSETEQLRKI YPLESRVFPK PTIVKEITNE
RTKRYTFYDD DAPLTNQHTV LDEATYNRIL KRIDFFIEKV VEVPPTYHFL SLLNVQLRIQ
PIWWMDEFAE RNGIESLLSA LRNLGHYPER ASKTPLESQI IQSLFHCLNS ENCRRRYQSS
AKCSVPGFNA LGTIAETVLS KSLNSARMAT FLLKFLCNKK GLSYFKAVIR AFEWLVEQKL
SKTRFSAWMH SFNDVITGVR VCADSSPQAI VHMDEFEDTD CLIDYLVATL ALIRDLCAAP
PDLQLRCALR HELLSAGLQK AIDSLLKWRN RHVRDALQLL IKEHNADARR FRSGSDVNNV
DRKCVKKQMN YREESHTPHG NTTRKTSTPV SNNRPTTPEQ QAVWDVFQRI YTRFTGSEGS
KESFIKLLEY FVTEPDNGKI QKSMQLLTHT LEALEGFKTA KADTNVGLTI LSQRLLDKLG
TAEEIAEYKT KYNGAMLENK HLKEQVESML SQLNVGPRDP MQFLKKQLDE LKAELNLRDN
LLASMQREFE TRYRAQIQAY NKLQSQMEHV QNSNEQHLQP GLLNKVSKSF DSVHRRNLSQ
DSLDAMTEQF SYHVEPNILS GSGIPVRVHT PSKTEDLDES FSGSEISSSP SPLLPDVSDT
VEEQQKLLLK SPPPPPPAVI VPTPAPAPIP VPPPAPIMGG PPPPPPPPGV AGAGPPPPPP
PPPAVSAGGS RYYAPAPQAE PEPKIDETSL TEEQKIQLEE ARKQRKAADD AARAAIEKYT
SIPSLRDLHK PTRPLKRVHW QRVDPLPGPN VFTKFCLNFD ITAKVFIDNG LLDFLDEKFD
NTPREDFVAV EISDQRSSLL PDTVEQNMAI ILRSVSNMPV EDLVQKFLVE PDFLPASILY
FDRASLASTN AYTDPFIPYS TDYTKKNPKE PTADVNSLSY FEKFFVLFVV NLRHYFQERM
KALKFRSTLF GDLEILEVRM KEVIDTSDSI MEDKNFAEFF QVLLIIGNYF NEPYDRASAF
SLYMIYRLET LRDSSSALTL MHYFDEIIRT RFPELLQAES TFKKIQSVSG YNIDAMVAGV
DGAYDEFCDF QTSLKDGALS KCDQHHPDDK AYDILSEWLP EAKERIRNIK KLKTDMLTKL
ENTVKYLCEY DSIDKVRNSF FKNLNSFYEM YSIAKAENEE RFEKEKRRIM SEDRDKLIRG
RQKTSIVAKY RNKRELPEDS DDKQDTASKD KNSLETIDEK MEDASKIEGD AKTGDDNEME
DLDKMEDLEK PDYAEEKDPY ITVMSELRSR IQNVPKRTVT VYSDEGVATL EPGAQGDDVV
DKAKMILEKM EGHSQLLTSS ANPDEEVLRA KLKAAERLQK PAIPRTRRKG HTEPKSAKSL
LAELTNGSNA SNLVENDRQK Q
