ID D7L7E0_ARALL Unreviewed; 1054 AA.
AC D7L7E0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN ORFNames=ARALYDRAFT_673666 {ECO:0000313|EMBL:EFH61984.1};
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; GL348715; EFH61984.1; -; Genomic_DNA.
DR RefSeq; XP_002885725.1; XM_002885679.1.
DR AlphaFoldDB; D7L7E0; -.
DR STRING; 81972.D7L7E0; -.
DR EnsemblPlants; Al_scaffold_0003_2863; Al_scaffold_0003_2863; Al_scaffold_0003_2863.
DR GeneID; 9319692; -.
DR Gramene; Al_scaffold_0003_2863; Al_scaffold_0003_2863; Al_scaffold_0003_2863.
DR KEGG; aly:9319692; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_007699_0_0_1; -.
DR OrthoDB; 623207at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; Formin, FH2 domain; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR027643; Formin-like_plant.
DR PANTHER; PTHR23213:SF276; FORMIN-LIKE PROTEIN 1; 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 Coiled coil {ECO:0000256|SAM:Coils}; 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..1054
FT /note="Formin-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003102405"
FT TRANSMEM 109..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 597..1017
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 36..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 766..793
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 36..56
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..549
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1054 AA; 115501 MW; 48C62EAC933E9BA4 CRC64;
MLFFLFLFFF YLLLSSSSDL VFADRRVLHE PFFPVDSPPP SPPSPPPLPK LPFSSTTPPS
SDPNTSPFFP LYPSSPPPPS PASFASFPAN ISSLIVPHAT KSPPNSKKLL IVAISAVSSA
ALVALLIALL YWRRRRTNQD LNFSDDSKTY TTDSSRRVYP PPPPATAAPT RRNAEARSKQ
RTTTRTSSTN NSSEFLYLGT MVNQRGIEEQ SLSNNGSSSR KLESPDLQPL PPLMKRSFRL
NPEVGSIGEE EEEEEFYSPR GSQSGRETLN RVGVPGQNPR SVNNDTISCS SSSSGSPGRS
TFISISPSMS PKRSEPKPVV ITTPEPPARI SPAELTDYRF VRSPSLSLAS LSSGFCPVKN
SDEGGLNQIS RSPTVTSLTA SPDNNKKENS PLSSASTSPE RRPNDTPEAY LRSPSHSSAS
TSPYRCFQKS PEVLPAFMSN LRQGLQSQLL SSPSNSHGGQ GFLKQLDALR SRSPSSSSSS
VCSSPEKASH KSPVTSPKLS SRNSQSLASS PDRDFSHSLD VSPRISNISP QILQSRVPPP
PPPPPPLWGR RNQVTHKAET ISKPPSLTPP SHPFVISSEN LPVTSPMETP ETVSASEPAE
ETPKPKLKAL HWDKVRASSD REMVWDHLRS SSFKLDEEMI ETLFVAKSLD NKPNQSQTTP
RCVLPSPNQE NRVLDPKKAQ NIAILLRALN VTIEEVCEAL LEGNADTLGT ELLESLLKMA
PTKEEERKLK AYKDDSPVKL GHAEKFLKAM LDIPFAFKRV DAMLYVANFE SEVEYLKKSF
ETLEAACEEL RNSRMFLKLL EAVLKTGNRM NVGTNRGDAH AFKLDTLLKL VDVKGADGKT
TLLHFVVQEI IRAEGTRLSG NNTDDIKCRK LGLQVVSSLC SELSNVKKAA AMDSEVLSSY
VSKLSQGIAK INEAIKVQST IIEESNSQRF SESMNTFLKR AEEEIIRVQA QESVALSLVK
EITEYFHGNS AKEEAHPFRI FLVVRDFLGV VDRVCKEVGM INERTMVSSA HKFPVPVNPM
LPQPLPGLVG RRQSSSSSSS SSASSSDDEH NSSH
//
