FH3_ARATH
ID FH3_ARATH Reviewed; 785 AA.
AC O23373; D0QAN4; F4JJE7; O23374;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Formin-like protein 3;
DE Short=AtFH3;
DE Short=AtFORMIN-3;
DE Flags: Precursor;
GN Name=FH3; OrderedLocusNames=At4g15200/At4g15190;
GN ORFNames=Dl3645c/Dl3640c, FCAALL.218;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=20023198; DOI=10.1105/tpc.109.068700;
RA Ye J., Zheng Y., Yan A., Chen N., Wang Z., Huang S., Yang Z.;
RT "Arabidopsis formin3 directs the formation of actin cables and polarized
RT growth in pollen tubes.";
RL Plant Cell 21:3868-3884(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP GENE FAMILY ORGANIZATION.
RX PubMed=11104517; DOI=10.1186/gb-2000-1-1-research001;
RA Cvrckova F.;
RT "Are plant formins integral membrane proteins?";
RL Genome Biol. 1:RESEARCH001.1-RESEARCH001.7(2000).
RN [6]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=12417149; DOI=10.1016/s1360-1385(02)02341-5;
RA Deeks M.J., Hussey P.J., Davies B.;
RT "Formins: intermediates in signal-transduction cascades that affect
RT cytoskeletal reorganization.";
RL Trends Plant Sci. 7:492-498(2002).
RN [7]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=15256004; DOI=10.1186/1471-2164-5-44;
RA Cvrckova F., Novotny M., Pickova D., Zarsky V.;
RT "Formin homology 2 domains occur in multiple contexts in angiosperms.";
RL BMC Genomics 5:44-44(2004).
CC -!- FUNCTION: Acts as actin nucleation factor that directs the formation of
CC actin cables and polarized growth in pollen tubes.
CC {ECO:0000269|PubMed:20023198}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O23373-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10298.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g15190 and At4g15200.; Evidence={ECO:0000305};
CC Sequence=CAB10299.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g15190 and At4g15200.; Evidence={ECO:0000305};
CC Sequence=CAB10299.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB78561.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g15190 and At4g15200.; Evidence={ECO:0000305};
CC Sequence=CAB78562.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g15190 and At4g15200.; Evidence={ECO:0000305};
CC Sequence=CAB78562.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ415316; ACQ91096.1; -; mRNA.
DR EMBL; Z97338; CAB10298.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z97338; CAB10299.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161540; CAB78561.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161540; CAB78562.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A71416; A71416.
DR PIR; H71415; H71415.
DR AlphaFoldDB; O23373; -.
DR SMR; O23373; -.
DR STRING; 3702.AT4G15200.1; -.
DR PaxDb; O23373; -.
DR PeptideAtlas; O23373; -.
DR PRIDE; O23373; -.
DR ProteomicsDB; 230575; -. [O23373-1]
DR EnsemblPlants; AT4G15200.2; AT4G15200.2; AT4G15200.
DR Gramene; AT4G15200.2; AT4G15200.2; AT4G15200.
DR Araport; AT4G15200; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_020967_0_0_1; -.
DR InParanoid; O23373; -.
DR PhylomeDB; O23373; -.
DR PRO; PR:O23373; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23373; baseline and differential.
DR Genevisible; O23373; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR Gene3D; 1.20.58.2220; -; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR027643; Formin-like_plant.
DR PANTHER; PTHR23213; PTHR23213; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR PROSITE; PS51444; FH2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..785
FT /note="Formin-like protein 3"
FT /id="PRO_0000308528"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 321..747
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 96..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..304
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 170
FT /note="A -> T (in Ref. 1; ACQ91096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 785 AA; 85894 MW; 3C6BA460E9876409 CRC64;
MGRLRLAFLA ISLVVFVCVS EEIFSRGGLN LLRFSVYGED VAEQTWIHQN PRRKLISYPK
KFSVSAPNLA FGPAPSFAPG PGPSFAPGPA PNPRSYDWLA PASSPNEPPA ETPDESSPSP
SEETPSVVAP SQSVPGPPRP PPQREKKDDI LMKLIIAVAS TAVLTFVFVA LMFLCCFKRN
CNNAVGSRDG PRDEGPLLRL STGSTENSPT VASTSRKMFS VASSKKRSFL SRVSLKRNGH
EFSTAESSSA AGLPPLKLPP GRSAPPPPPA AAPPPQPPPP PPPKPQPPPP PKIARPPPAP
PKGAAPKRQG NTSSGDASDV DSETGAPKTK LKPFFWDKMA NPDQKMVWHE ISAGSFQFNE
EAMESLFGYN DGNKNKNGQK STDSSLRESP LQYIQIIDTR KAQNLSILLR ALNVTTEEVV
DAIKEGNELP VELLQTLLKM APTSEEELKL RLYSGDLHLL GPAERFLKIL VDIPFAFKRI
ESLLFMISLQ EEVSGLKEAL GTLEVACKKL RNSRLFLKLL EAVLKTGNRM NVGTFRGDAQ
AFKLDTLLKL SDVKGTDGKT TLLHFVVLEI IRSEGVRALR LQSRSFSSVK TDDSNADSSP
QSVERYRSTG LQVVTGLTTE LEDVKRAAII DADGLAATLA NISGSLTNAR EFLKTMDEES
DFERALAGFI ERADADFKWL KEEEERIMVL VKSSADYFHG KSAKNEGLRL FAIVRDFLIM
LEKVCREVKE TTKTTNHSGK KESEMTTSDS NQPSPDFRQR LFPAIAERRM DSSDDSDDEE
DSSPS
