FH1_ARATH
ID FH1_ARATH Reviewed; 1051 AA.
AC Q9SE97; Q0WVK4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Formin-like protein 1;
DE Short=AtFH1;
DE Short=AtFORMIN-8;
DE Flags: Precursor;
GN Name=FH1; Synonyms=AFH1; OrderedLocusNames=At3g25500; ORFNames=MWL2.16;
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 INTERACTION WITH FIP2.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10929945; DOI=10.1093/pcp/41.5.617;
RA Banno H., Chua N.-H.;
RT "Characterization of the Arabidopsis formin-like protein AFH1 and its
RT interacting protein.";
RL Plant Cell Physiol. 41:617-626(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1051.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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).
RN [9]
RP FUNCTION.
RX PubMed=14671023; DOI=10.1105/tpc.016550;
RA Cheung A.Y., Wu H.-M.;
RT "Overexpression of an Arabidopsis formin stimulates supernumerary actin
RT cable formation from pollen tube cell membrane.";
RL Plant Cell 16:257-269(2004).
RN [10]
RP INDUCTION.
RX PubMed=15319477; DOI=10.1105/tpc.104.024372;
RA Favery B., Chelysheva L.A., Lebris M., Jammes F., Marmagne A.,
RA De Almeida-Engler J., Lecomte P., Vaury C., Arkowitz R.A., Abad P.;
RT "Arabidopsis formin AtFH6 is a plasma membrane-associated protein
RT upregulated in giant cells induced by parasitic nematodes.";
RL Plant Cell 16:2529-2540(2004).
RN [11]
RP FUNCTION.
RX PubMed=15994911; DOI=10.1105/tpc.105.030908;
RA Michelot A., Guerin C., Huang S., Ingouff M., Richard S., Rodiuc N.,
RA Staiger C.J., Blanchoin L.;
RT "The formin homology 1 domain modulates the actin nucleation and bundling
RT activity of Arabidopsis FORMIN1.";
RL Plant Cell 17:2296-2313(2005).
CC -!- FUNCTION: Might be involved in the organization and polarity of the
CC actin cytoskeleton. Involved in polar pollen cell growth process by
CC maintaining tip-focused cell membrane expansion for the polar extension
CC of pollen tubes. {ECO:0000269|PubMed:14671023,
CC ECO:0000269|PubMed:15994911}.
CC -!- SUBUNIT: Interacts with FIP2. {ECO:0000269|PubMed:10929945}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated during gall formation induced by root-knot
CC nematodes. {ECO:0000269|PubMed:15319477}.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC {ECO:0000305}.
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DR EMBL; AF174427; AAF14548.1; -; mRNA.
DR EMBL; AB025639; BAB01320.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77017.1; -; Genomic_DNA.
DR EMBL; AY080793; AAL87275.1; -; mRNA.
DR EMBL; AY142579; AAN13148.1; -; mRNA.
DR EMBL; AK226743; BAE98844.1; -; mRNA.
DR RefSeq; NP_189177.1; NM_113446.5.
DR PDB; 6IQJ; X-ray; 1.92 A; C/D=524-536.
DR PDBsum; 6IQJ; -.
DR AlphaFoldDB; Q9SE97; -.
DR SMR; Q9SE97; -.
DR BioGRID; 7467; 3.
DR STRING; 3702.AT3G25500.1; -.
DR iPTMnet; Q9SE97; -.
DR PaxDb; Q9SE97; -.
DR PRIDE; Q9SE97; -.
DR ProteomicsDB; 230095; -.
DR EnsemblPlants; AT3G25500.1; AT3G25500.1; AT3G25500.
DR GeneID; 822136; -.
DR Gramene; AT3G25500.1; AT3G25500.1; AT3G25500.
DR KEGG; ath:AT3G25500; -.
DR Araport; AT3G25500; -.
DR TAIR; locus:2094493; AT3G25500.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_007699_0_0_1; -.
DR InParanoid; Q9SE97; -.
DR OMA; QTTPRCV; -.
DR OrthoDB; 1204639at2759; -.
DR PRO; PR:Q9SE97; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SE97; baseline and differential.
DR Genevisible; Q9SE97; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0003779; F:actin binding; ISS:TAIR.
DR GO; GO:0051015; F:actin filament binding; IDA:TAIR.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:TAIR.
DR GO; GO:0045010; P:actin nucleation; IDA:TAIR.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:TAIR.
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 1: Evidence at protein level;
KW 3D-structure; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1051
FT /note="Formin-like protein 1"
FT /id="PRO_0000308526"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 588..1010
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 35..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..538
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 5
FT /note="L -> R (in Ref. 5; BAE98844)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="P -> T (in Ref. 5; BAE98844)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="V -> D (in Ref. 5; BAE98844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1051 AA; 115148 MW; 916378018529B808 CRC64;
MLFFLFFFYL LLSSSSDLVF ADRRVLHEPF FPIDSPPPSP PSPPPLPKLP FSSTTPPSSS
DPNASPFFPL YPSSPPPPSP ASFASFPANI SSLIVPHATK SPPNSKKLLI VAISAVSSAA
LVALLIALLY WRRSKRNQDL NFSDDSKTYT TDSSRRVYPP PPATAPPTRR NAEARSKQRT
TTSSTNNNSS EFLYLGTMVN QRGIDEQSLS NNGSSSRKLE SPDLQPLPPL MKRSFRLNPD
VGSIGEEDEE DEFYSPRGSQ SGREPLNRVG LPGQNPRSVN NDTISCSSSS SGSPGRSTFI
SISPSMSPKR SEPKPPVIST PEPAELTDYR FVRSPSLSLA SLSSGLKNSD EVGLNQIFRS
PTVTSLTTSP ENNKKENSPL SSTSTSPERR PNDTPEAYLR SPSHSSASTS PYRCFQKSPE
VLPAFMSNLR QGLQSQLLSS PSNSHGGQGF LKQLDALRSR SPSSSSSSVC SSPEKASHKS
PVTSPKLSSR NSQSLSSSPD RDFSHSLDVS PRISNISPQI LQSRVPPPPP PPPPLPLWGR
RSQVTTKADT ISRPPSLTPP SHPFVIPSEN LPVTSSPMET PETVCASEAA EETPKPKLKA
LHWDKVRASS DREMVWDHLR SSSFKLDEEM IETLFVAKSL NNKPNQSQTT PRCVLPSPNQ
ENRVLDPKKA QNIAILLRAL NVTIEEVCEA LLEGNADTLG TELLESLLKM APTKEEERKL
KAYNDDSPVK LGHAEKFLKA MLDIPFAFKR VDAMLYVANF ESEVEYLKKS FETLEAACEE
LRNSRMFLKL LEAVLKTGNR MNVGTNRGDA HAFKLDTLLK LVDVKGADGK TTLLHFVVQE
IIRAEGTRLS GNNTQTDDIK CRKLGLQVVS SLCSELSNVK KAAAMDSEVL SSYVSKLSQG
IAKINEAIQV QSTITEESNS QRFSESMKTF LKRAEEEIIR VQAQESVALS LVKEITEYFH
GNSAKEEAHP FRIFLVVRDF LGVVDRVCKE VGMINERTMV SSAHKFPVPV NPMMPQPLPG
LVGRRQSSSS SSSSSTSSSD EDEHNSISLV S
