ID   FH10_ARATH              Reviewed;         841 AA.
AC   Q9SRR2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Formin-like protein 10;
DE            Short=AtFH10;
DE   Flags: Precursor;
GN   Name=FH10; OrderedLocusNames=At3g07540; ORFNames=F21O3.25;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
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   [3]
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   [4]
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   [5]
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   [6]
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).
CC   -!- FUNCTION: Might be involved in the organization and polarity of the
CC       actin cytoskeleton. {ECO:0000250}.
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; AC009853; AAF02158.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74558.1; -; Genomic_DNA.
DR   EMBL; AF446866; AAL38599.1; -; mRNA.
DR   EMBL; AY050396; AAK91412.1; -; mRNA.
DR   RefSeq; NP_566311.1; NM_111632.3.
DR   AlphaFoldDB; Q9SRR2; -.
DR   SMR; Q9SRR2; -.
DR   BioGRID; 5278; 15.
DR   IntAct; Q9SRR2; 14.
DR   STRING; 3702.AT3G07540.1; -.
DR   iPTMnet; Q9SRR2; -.
DR   PaxDb; Q9SRR2; -.
DR   PRIDE; Q9SRR2; -.
DR   ProteomicsDB; 230091; -.
DR   EnsemblPlants; AT3G07540.1; AT3G07540.1; AT3G07540.
DR   GeneID; 819943; -.
DR   Gramene; AT3G07540.1; AT3G07540.1; AT3G07540.
DR   KEGG; ath:AT3G07540; -.
DR   Araport; AT3G07540; -.
DR   TAIR; locus:2079711; AT3G07540.
DR   eggNOG; KOG1922; Eukaryota.
DR   HOGENOM; CLU_007699_0_0_1; -.
DR   InParanoid; Q9SRR2; -.
DR   OMA; LTTNDVC; -.
DR   OrthoDB; 1204639at2759; -.
DR   PhylomeDB; Q9SRR2; -.
DR   PRO; PR:Q9SRR2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SRR2; baseline and differential.
DR   Genevisible; Q9SRR2; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; ISS:TAIR.
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   Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..841
FT                   /note="Formin-like protein 10"
FT                   /id="PRO_0000308535"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          469..841
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   REGION          137..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..446
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   841 AA;  93012 MW;  94504DCF954BE217 CRC64;
     MDGLCYVIFI IFSLLSCAFS PLSYASPATF SRRHLLQAPV TDPSTFSPPF FPLYSSTSPP
     PPPSPPQPLP PPAPTFATFP ANISALVLPR SPKPQTPSRT LLIPAISAVL AAATLIALAF
     FFYGRWRGQT SHFKDESKSL ASDISQSQQQ TLPCPPPRNN NTQNKLSVAP STSDVLYLGN
     VVTSSGSGFV KPESPDISPL PPLPARSFLL QHHSEANLDE EEEDDDFYSP LASIAGQESR
     DRRINPYSNC SCSISSHSDS PAMSPSAAMS PPMNSTAPHW STNQNTHSPS SPERTVRNNK
     RYGGQSLRMF SLWNQNLGFP RISSASTSPE RGMIRTPDAY ARSSMYSSVS TTPDRFFRKV
     LDSSPPRWND FSRNVKSLFL SSTSASPARD FCINISESSR SLKSSWEKPE LDTTQQRESA
     AAAVTLPPPQ RPPPAMPEPP PLVPPSQSFM VQKSGKKLSF SELPQSCGEG TTDRPKPKLK
     PLPWDKVRPS SRRTNTWDRL PYNSSNANSK QRSLSCDLPM LNQESKVLDP RKSQNVAVLL
     TTLKLTTNDV CQALRDGHYD ALGVELLESL ARVAPSEEEE KKLISYSDDS VIKLAPSERF
     LKELLNVPFV FKRVDALLSV ASFDSKVKHL KRSFSVIQAA CEALRNSRML LRLVGATLEA
     GMKSGNAHDF KLEALLGLVD IKSSDGRTSI LDSVVQKITE SEGIKGLQVV RNLSSVLNDA
     KKSAELDYGV VRMNVSKLYE EVQKISEVLR LCEETGHSEE HQWWKFRESV TRFLETAAEE
     IKKIEREEGS TLFAVKKITE YFHVDPAKEE AQLLKVFVIV RDFLKILEGV CKKMEVTSSL
     A