ID D7LKI8_ARALL Unreviewed; 891 AA.
AC D7LKI8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 22-FEB-2023, entry version 54.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN ORFNames=ARALYDRAFT_483497 {ECO:0000313|EMBL:EFH56327.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC {ECO:0000256|ARBA:ARBA00025793}.
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DR EMBL; GL348716; EFH56327.1; -; Genomic_DNA.
DR RefSeq; XP_002880068.1; XM_002880022.1.
DR AlphaFoldDB; D7LKI8; -.
DR STRING; 81972.D7LKI8; -.
DR EnsemblPlants; fgenesh2_kg.4__2557__AT2G43800.1; fgenesh2_kg.4__2557__AT2G43800.1; fgenesh2_kg.4__2557__AT2G43800.1.
DR Gramene; fgenesh2_kg.4__2557__AT2G43800.1; fgenesh2_kg.4__2557__AT2G43800.1; fgenesh2_kg.4__2557__AT2G43800.1.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_007699_0_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; IEA:EnsemblPlants.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:EnsemblPlants.
DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IEA:EnsemblPlants.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR027643; Formin-like_plant.
DR PANTHER; PTHR23213:SF368; FORMIN-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR23213; FORMIN-RELATED; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..891
FT /note="Formin-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003102479"
FT TRANSMEM 156..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 435..862
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 45..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 98088 MW; 18939EF21D9B7A78 CRC64;
MTKLPLSFFC LLFVAFFFSS STADQRFHSR HLLHQPFFPV VTAAPPPYQP PVSSQPPSPS
PHIHHHHKKQ LATPPPPPHE KHLFSSVANP PPPPPSPPHP NPFFPSSDPT STASHPPPAP
PPPASLPTFP ANISSLLFPT HNKPSKPPSN GHIARLVTIT ASVICAAALL SLFAVFIIFI
RRTRHRRRSS PADDTKSTRS DALQLFNASP SDGTKKHKQH QQPPKYTSSH TSSEFLYLGT
LVNSRSGGLE QQKSPISLSG GITGVLELPP PASSSSTSSY SQYHKLGSPE LRPLPPLPKL
QSFTPVYKST EQLNPKRQYF DGDDNENDEF FSPRGSSGRK QDVDQIGDRS INGSGSNSCS
PTNSVPSLNA SPGTSLKPKS VSPPVSLHSQ NSSNNGVSKR LCPARPPPPP PPPPQFLEIP
ATMSHSPPDG DSDPEKKVET MKPKLKTLHW DKVRARSSRV MVWDQIKSNS FQVNEEMIET
LFKVNDTNSR TRDGVVQSAN QENRFLDPRK SHNIAILLRA LNVTADEVCE ALVEGNSDTL
GPELLECLLK MAPTKEEEDK LKELKDNDDG SPSKIGPAEK FLKALLNIPL AFKRIDAMLY
IVKFESETEY LNRSFDTLEA ASGELKNTRM FLKLLEAVLK TGNRMNIGTN RGDAHAFKLD
TLLKLVDIKG ADGKTTLLHF VVQEIIKFEG ARVPFTPTQS HIGNDMAEQS AFQDDLELKK
LGLQVVSGLS SQLINVKKAA AMDSNSLINE TAETARGIAK VKEVLAELKE ETGVERFLES
MNSFLNKAEK EITEIQSHGD NVMKMVKEVT EYFHGNSETH HFRIFAVVRD FLTILDQVCK
EVGRVNERTV YGSVPRHSPS NQTATPLFPV VNNNNSRLSP SGSLDEDDDS F
//
